substrate_name: ADP

assay_conditions_summary: pH 8; 298.15 K; cofactor ADP

proof_lines: recombinant enzyme, pH 8.0, 25°C, reaction with formyl phosphate

proof_lines: recombinant enzyme, pH 8.0, 25°C, reaction with acetyl phosphate

proof_lines: recombinant enzyme, pH 8.0, 25°C, reaction with carbamoyl phosphate

substrate: ADP


organism: Escherichia coli

substrate_name: ATP

source_db: brenda

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: No sequence was resolved for this record, so variant-aware sequence handling could not be applied.

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP

proof_lines: recombinant enzyme, pH 8.0, 25°C, with formate

proof_lines: recombinant enzyme, pH 8.0, 25°C, with acetate

substrate: ATP

source: brenda


substrate_name: acetyl phosphate

smiles: CC(=O)OP(=O)(O)O

proof_lines: recombinant enzyme, pH 8.0, 25°C, reaction with ADP

substrate: acetyl phosphate


substrate_name: Carbamoyl phosphate

substrate: Carbamoyl phosphate


substrate_name: formyl phosphate

substrate: formyl phosphate


enzyme_display_name: lipoate--protein ligase

substrate_name: octanoyl-[CoA]

verification_status: unverified

sequence_variant_note: Mutation context is present, but no sequence was resolved for this record.

mutation_type: substitution

assay_conditions_summary: pH 7.8; 298.15 K; cofactor CoA

proof_lines: mutant enzyme K135A, with glycine cleavage system H protein as cosubstrate, at pH 7.8 and 25°C

enzyme: lipoate--protein ligase

substrate: octanoyl-[CoA]

status: unverified


proof_lines: mutant enzyme R71A, with glycine cleavage system H protein as cosubstrate, at pH 7.8 and 25°C


proof_lines: mutant enzyme G72A/G73A, with glycine cleavage system H protein as cosubstrate, at pH 7.8 and 25°C


proof_lines: wild type enzyme, with glycine cleavage system H protein as cosubstrate, at pH 7.8 and 25°C


substrate_name: R-lipoic acid

substrate: R-lipoic acid


assay_conditions_summary: pH 7; 310.15 K; cofactor ATP


substrate_name: apoH-protein

substrate: apoH-protein


substrate_name: DL-lipoic acid

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP

substrate: DL-lipoic acid


smiles: CCC(CCCCC(=O)[O-])S


enzyme_display_name: NAD(+) synthase

organism: Bacillus anthracis

substrate_name: deamido-NAD+

assay_conditions_summary: pH 8.5; 310.15 K; cofactor NAD+

proof_lines: in 60 mM EPPS pH 8.5 with 20 mM ammonium chloride, 20 mM potassium chloride, and 10 mM magnesium chloride, at 37°C

enzyme: NAD(+) synthase

substrate: deamido-NAD+


enzyme_display_name: glutamine synthetase

organism: Chlorella sorokiniana

enzyme: glutamine synthetase


assay_conditions_summary: cofactor ATP


assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP


substrate_name: L-glutamate

smiles: C(CC(=O)O)C(C(=O)O)N

substrate: L-glutamate


organism: Francisella tularensis

assay_conditions_summary: cofactor NAD+


substrate_name: deamido-NMN

substrate: deamido-NMN


organism: Medicago truncatula

substrate_name: L-Glu

proof_lines: non-phosphorylated GS1a, in the presence of 0.0005 mM microcystin

substrate: L-Glu


proof_lines: phosphorylated GS1a, in the presence of 0.0005 mM microcystin


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 7.5; cofactor ATP

proof_lines:
pH 7.5
Gln


substrate_name: formate

source_db: skid

protein_accession_database: UniProt

source_license: CC BY 4.0; CC BY-NC-ND 4.0

sequence_source: multiple

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.

proof_lines: kcat is 37.6 sec(-1) for transformylase activity (at pH 8). kcat is 0.309 sec(-1) for acetate kinase activity (at pH 8).

data_origin: experimental

source_databases_merged: skid uniprot

substrate: formate

source: skid


organism: Nocardia asteroides


substrate_name: Glu

substrate: Glu


organism: Homo sapiens


organism: Escherichia coli (strain K12)

substrate_name: acetate (at pH 8)

source_db: uniprot

assay_conditions_summary: pH 8; cofactor ADP

substrate: acetate (at pH 8)

source: uniprot


organism: Ovis aries


organism: Staphylococcus aureus

assay_conditions_summary: pH 8; cofactor NAD+

proof_lines: in 60 mM Tris-HCl pH 8.0, 10 mM NH4Cl, 10 mM MgCl2, 10 mM KCl


assay_conditions_summary: pH 8; cofactor ATP


enzyme_display_name: trypanothione synthase

organism: Trypanosoma brucei

substrate_name: ATP; Reduced glutathione; Spermidine

source_license: CC BY 4.0; SABIO-RK terms (free for academic use; see sabiork.h-its.org)

assay_conditions_summary: pH 8; 298.15 K; buffer recombinant enzyme

proof_lines: recombinant enzyme, pH 8.0, 25°C, HEPES buffer

proof_lines: recombinant enzyme, pH 8.0, 37°C, HEPES buffer

proof_lines: recombinant enzyme, pH 7.0, 37°C, phosphate buffer

enzyme: trypanothione synthase

substrate: ATP; Reduced glutathione; Spermidine


enzyme_display_name: aspartate--ammonia ligase

organism: Streptococcus equinus

enzyme: aspartate--ammonia ligase


substrate_name: L-Asp

substrate: L-Asp


organism: Chlorella sp.

substrate_name: Unknown

km_display: Not reported

ki_unit: mM

substrate: Unknown


organism: Trichormus variabilis

proof_lines:
enzyme from strain SA0, pH 6.8
enzyme from strain SA0, pH 7.5
enzyme from strain SA1, pH 7.5


substrate_name: ATP

assay_conditions_summary: pH 6.8; cofactor ATP

proof_lines:
enzyme from strain SA0, pH 6.8
enzyme from strain SA0, pH 7.5
enzyme from strain SA1, pH 6.8

substrate: ATP


enzyme_display_name: beta-citrylglutamate synthase

organism: Mus musculus

substrate_name: beta-Citryl-L-glutamate

enzyme: beta-citrylglutamate synthase

substrate: beta-Citryl-L-glutamate


proof_lines:
at pH 7.4 and 37°C
above


organism: Columba sp.


organism: Bacillus subtilis


organism: Escherichia coli


substrate_name: LplA acceptor peptide 2

substrate: LplA acceptor peptide 2


enzyme_display_name: o-succinylbenzoate--CoA ligase

proof_lines: pH and temperature not specified in the publication

enzyme: o-succinylbenzoate--CoA ligase


enzyme_display_name: peptidylprolyl isomerase

substrate_name: RNase T1

proof_lines: mutant Y15A, pH not specified in the publication, temperature not specified in the publication

enzyme: peptidylprolyl isomerase

substrate: RNase T1


enzyme_display_name: L-arabinose isomerase

substrate_name: L-arabinose

enzyme: L-arabinose isomerase

substrate: L-arabinose


enzyme_display_name: amino-acid racemase

substrate_name: D-homoserine

smiles: C(CO)C(C(=O)O)N

enzyme: amino-acid racemase

substrate: D-homoserine


proof_lines: mutant A82P, pH not specified in the publication, temperature not specified in the publication


enzyme_display_name: sulfoquinovose isomerase

substrate_name: beta-sulfoquinovose

proof_lines: formation of 6-deoxy-6-sulfo-D-fructose, pH and temperature not specified in the publication

enzyme: sulfoquinovose isomerase

substrate: beta-sulfoquinovose


proof_lines:
pH 7.0
pH 7.0, 30°C, isomerase acitivity


enzyme_display_name: UDP-glucose 4-epimerase

substrate_name: UDP-alpha-D-glucose

proof_lines: pH 6.2, temperature not specified in the publication, recombinant mutant K153M

enzyme: UDP-glucose 4-epimerase

substrate: UDP-alpha-D-glucose


enzyme_display_name: L-ribulose-5-phosphate 4-epimerase

substrate_name: L-ribulose 5-phosphate

smiles: C(C(C(C(=O)CO)O)O)OP(=O)(O)O

enzyme: L-ribulose-5-phosphate 4-epimerase

substrate: L-ribulose 5-phosphate


enzyme_display_name: UniProt Q2FV22

substrate_name: beta-Alanine

source_license: CC BY-NC-ND 4.0

smiles: C(CN)C(=O)O

enzyme: UniProt Q2FV22

substrate: beta-Alanine


substrate_name: (R)-pantoate

substrate: (R)-pantoate


enzyme_display_name: UniProt P0A6W9

substrate_name: L-alpha-aminobutyrate

smiles: CCC(C(=O)O)N

enzyme: UniProt P0A6W9

substrate: L-alpha-aminobutyrate


substrate_name: L-cysteine

smiles: C(C(C(=O)O)N)S

substrate: L-cysteine


enzyme_display_name: UniProt P32477

organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 8

enzyme: UniProt P32477


substrate_name: L-Glu

substrate: L-Glu


substrate_name: L-glutamate

substrate: L-glutamate


substrate_name: L-Cys

substrate: L-Cys


enzyme_display_name: Glutathione biosynthesis bifunctional protein GshAB

organism: Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R)


enzyme: Glutathione biosynthesis bifunctional protein GshAB


substrate_name: ATP (in the reaction with gamma-GCS)

substrate: ATP (in the reaction with gamma-GCS)


substrate_name: gamma-L-glutamyl-L-cysteine

smiles: C(CC(=O)NC(CS)C(=O)O)C(C(=O)O)N

substrate: gamma-L-glutamyl-L-cysteine


substrate_name: glycine

smiles: C(C(=O)O)N

substrate: glycine


enzyme_display_name: glutathione synthase

organism: Spinacia oleracea

substrate_name: ATP

enzyme: glutathione synthase

substrate: ATP


organism: [Candida] boidinii

substrate_name: gamma-Glu-Cys

substrate: gamma-Glu-Cys


substrate_name: Gly

substrate: Gly


enzyme_display_name: UniProt P48637

proof_lines:
Raw SKiD Env: Temp=37°C, pH=8.2
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt P48637


enzyme_display_name: UniProt Q9M426

organism: Glycine max

substrate_name: beta-Ala

enzyme: UniProt Q9M426

substrate: beta-Ala


organism: Homo sapiens

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=37°C, pH=8.2


enzyme_display_name: UniProt P07862

substrate_name: D-alanine

smiles: CC(C(=O)O)N

proof_lines:
Raw SKiD Env: Temp=37°C, pH=9.2
Raw SKiD Env: Temp=37°C, pH=7.5
Raw SKiD Env: Temp=37°C, pH=6

enzyme: UniProt P07862

substrate: D-alanine


enzyme_display_name: UniProt Q5SHZ3

organism: Thermus thermophilus

enzyme: UniProt Q5SHZ3


enzyme_display_name: UniProt Q2N4T5

organism: Helicobacter pylori

sequence_variant_note: Sequence identity was resolved, but no explicit wild-type or mutant call was captured.

proof_lines:
Raw SKiD Env: Temp=30°C, pH=9
Raw SKiD Env: Temp=30°C, pH=8

enzyme: UniProt Q2N4T5


proof_lines:
Raw SKiD Env: Temp=30°C, pH=8
Raw SKiD Env: Temp=30°C, pH=9


enzyme_display_name: UniProt Q5HEB7

organism: Staphylococcus aureus

enzyme: UniProt Q5HEB7


smiles: N


organism: Streptococcus pyogenes

source_db: oed

source: oed


substrate_name: L-Lysine

substrate: L-Lysine


kcat_over_km_origin: calculated


organism: Streptococcus pyogenes serotype M1

substrate_name: L-lysine

smiles: C(CCN)CC(C(=O)O)N

substrate: L-lysine


enzyme_display_name: glucose-6-phosphate isomerase

substrate_name: fructose 6-phosphate

smiles: C(C(C(C(C(=O)CO)O)O)O)OP(=O)(O)O

enzyme: glucose-6-phosphate isomerase

substrate: fructose 6-phosphate


enzyme_display_name: xylose isomerase

substrate_name: D-glucose

proof_lines: pH 7.0, 50°C, with 0.5 mM Mn2+ and 10 mM Mg2+

enzyme: xylose isomerase

substrate: D-glucose


enzyme_display_name: arabinose-5-phosphate isomerase

substrate_name: D-ribulose 5-phosphate

enzyme: arabinose-5-phosphate isomerase

substrate: D-ribulose 5-phosphate


smiles: CCCCCCCC=CC(=O)C(CNC(=O)C)S


enzyme_display_name: adenylate cyclase

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

proof_lines: pH 8.0, 37°C, recombinant catalytic domain, 10 mM Mg2+

enzyme: adenylate cyclase


substrate_name: UDP-N-acetyl-alpha-D-mannosamine

proof_lines: in presence of 1 mM UDP-N-acetylglucosamine

proof_lines: in presence of 0.5 mM UDP-N-acetylglucosamine

substrate: UDP-N-acetyl-alpha-D-mannosamine


organism: Mycobacterium tuberculosis


smiles: NCCCCC(=O)O


substrate_name: Taurine

substrate: Taurine


substrate_name: methylamine

smiles: CN

substrate: methylamine


smiles: NCCCC(=O)O


substrate_name: cysteamine

smiles: NCCS

substrate: cysteamine


substrate_name: ethylamine

smiles: CCN

substrate: ethylamine


substrate_name: glycolate

smiles: O=C(O)CO

substrate: glycolate


enzyme_display_name: UDP-N-acetylmuramate--L-alanine ligase

organism: Verrucomicrobium spinosum

substrate_name: L-alanine

proof_lines: pH 9.0, 37°C, recombinnant enzyme MurB/CVs

enzyme: UDP-N-acetylmuramate--L-alanine ligase

substrate: L-alanine


substrate_name: UDP-N-acetyl-alpha-D-muramate

proof_lines: pH 9.0, 37°C, recombinant enzyme MurB/CVs

substrate: UDP-N-acetyl-alpha-D-muramate


substrate_name: ATP

assay_conditions_summary: pH 9; 310.15 K; cofactor ATP

substrate: ATP


organism: Rattus norvegicus

smiles: CC(C)(COP(=O)(O)O)C(C(=O)NCCC(=O)O)O


organism: Lysinibacillus sphaericus

substrate_name: Lys

proof_lines:
in presence of 30 mM K2HPO4
in presence of 2 mM K2HPO4
in presence of 60 mM KCl

substrate: Lys


proof_lines:
in presence of 2 mM K2HPO4
in presence of 30 mM K2HPO4


substrate_name: UDP-N-acetylmuramoyl-L-Ala-D-Glu

substrate: UDP-N-acetylmuramoyl-L-Ala-D-Glu


organism: Setaria cervi

substrate_name: Gly

assay_conditions_summary: 310.15 K; cofactor ATP

substrate: Gly


smiles: NCC(O)CC(=O)O


substrate_name: beta-Alanine

substrate: beta-Alanine


assay_conditions_summary: pH 7.8; 298.15 K; cofactor ATP


substrate_name: Carbamate

substrate: Carbamate


substrate_name: D-Pantoate

substrate: D-Pantoate


enzyme_display_name: glutamate--cysteine ligase

organism: Escherichia coli

source_license: SABIO-RK terms (free for academic use; see sabiork.h-its.org)

enzyme: glutamate--cysteine ligase


substrate_name: ATP; L-alpha-Aminobutyrate; L-alpha-Methyl glutamate


substrate_name: ATP; L-Glutamate; 3-Cyano-L-alanine

substrate: ATP; L-Glutamate; 3-Cyano-L-alanine


substrate_name: L-Glutamate; L-alpha-Aminobutyrate; ATP

substrate: L-Glutamate; L-alpha-Aminobutyrate; ATP


substrate_name: L-alpha-Aminobutyrate; ATP; L-alpha-Ethyl glutamate


substrate_name: D-Glutamate; ATP; L-alpha-Aminobutyrate

substrate: D-Glutamate; ATP; L-alpha-Aminobutyrate


substrate_name: L-alpha-Aminobutyrate; ATP; L-Glutamate

substrate: L-alpha-Aminobutyrate; ATP; L-Glutamate


organism: Synechocystis sp.

substrate_name: L-glutamate

verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P74515 and applied mutation signature R248K to reconstruct the assayed variant sequence.

smiles: C(CC(=O)O)C(C(=O)O)N

column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row R248K, substrate Glutamate; column V/Etot (min^-1) = 0.5 ± 0.1; column Km (uM) = 3760 ± 427; column V/Km (M^-1·s^-1) = 2.2. captured primary segment: Table 2 | SynGCL mutant R248K | substrate Glutamate | V/Etot (kcat) 0.5 ± 0.1 min^-1 | Km 3760 ± 427 uM | V/Km (kcat/Km) 2.2 M^-1 s^-1

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row R248K, substrate Glutamate: V/Etot = 0.5 ± 0.1 min^-1 (the turnover cell, kcat); Km = 3760 ± 427 uM; printed V/Km = 2.2 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row R248K, substrate Glutamate

table_label: Table 2: Steady-state kinetic parameters of mutant SynGCL (Biochem. J. 2013, 450: 63-72), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1)

substrate: L-glutamate

status: corrected


assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row R248K, substrate ATP; column V/Etot (min^-1) = 0.5 ± 0.1; column Km (uM) = 969 ± 77; column V/Km (M^-1·s^-1) = 8.6. captured primary segment: Table 2 | SynGCL mutant R248K | substrate ATP | V/Etot (kcat) 0.5 ± 0.1 min^-1 | Km 969 ± 77 uM | V/Km (kcat/Km) 8.6 M^-1 s^-1

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row R248K, substrate ATP: V/Etot = 0.5 ± 0.1 min^-1 (the turnover cell, kcat); Km = 969 ± 77 uM; printed V/Km = 8.6 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row R248K, substrate ATP


substrate_name: L-cysteine

smiles: C(C(C(=O)O)N)S

column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row R248K, substrate Cysteine; column V/Etot (min^-1) = 0.6 ± 0.1; column Km (uM) = 857 ± 10; column V/Km (M^-1·s^-1) = 11.7. captured primary segment: Table 2 | SynGCL mutant R248K | substrate Cysteine | V/Etot (kcat) 0.6 ± 0.1 min^-1 | Km 857 ± 10 uM | V/Km (kcat/Km) 11.7 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 2 V/Etot cell 0.6 min^-1; the printed turnover column is per MINUTE, so 0.6 / 60 = 0.01 s^(-1); the exported value is 0.01 s^(-1). Km: printed Table 2 Km cell 857 uM; 1 uM is 1/1000 mM, so 857 / 1000 = 0.857 mM; the exported value is 0.857 mM. kcat/Km: printed Table 2 V/Km cell 11.7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 11.7 / 1000 = 0.0117 s^(-1)*mM^(-1); the exported value is 0.011668611435239206 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.01 / 0.857 = 0.011668611435239206 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row R248K, substrate Cysteine: V/Etot = 0.6 ± 0.1 min^-1 (the turnover cell, kcat); Km = 857 ± 10 uM; printed V/Km = 11.7 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row R248K, substrate Cysteine

substrate: L-cysteine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P74515 and applied mutation signature R167K to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row R167K, substrate Cysteine; column V/Etot (min^-1) = 1.5 ± 0.2; column Km (uM) = 1950 ± 180; column V/Km (M^-1·s^-1) = 12.8. captured primary segment: Table 2 | SynGCL mutant R167K | substrate Cysteine* (asterisk: reaction performed at sub-saturating 50 mM glutamate) | V/Etot (kcat) 1.5 ± 0.2 min^-1 | Km 1950 ± 180 uM | V/Km (kcat/Km) 12.8 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 2 V/Etot cell 1.5 min^-1; the printed turnover column is per MINUTE, so 1.5 / 60 = 0.025 s^(-1); the exported value is 0.025 s^(-1). Km: printed Table 2 Km cell 1950 uM; 1 uM is 1/1000 mM, so 1950 / 1000 = 1.95 mM; the exported value is 1.95 mM. kcat/Km: printed Table 2 V/Km cell 12.8 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 12.8 / 1000 = 0.0128 s^(-1)*mM^(-1); the exported value is 0.012820512820512822 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.025 / 1.95 = 0.012820512820512822 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row R167K, substrate Cysteine: V/Etot = 1.5 ± 0.2 min^-1 (the turnover cell, kcat); Km = 1950 ± 180 uM; printed V/Km = 12.8 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row R167K, substrate Cysteine


column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row R167K, substrate ATP; column V/Etot (min^-1) = 2.3 ± 0.3; column Km (uM) = 445 ± 71; column V/Km (M^-1·s^-1) = 86.1. captured primary segment: Table 2 | SynGCL mutant R167K | substrate ATP* (asterisk: reaction performed at sub-saturating 50 mM glutamate) | V/Etot (kcat) 2.3 ± 0.3 min^-1 | Km 445 ± 71 uM | V/Km (kcat/Km) 86.1 M^-1 s^-1

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row R167K, substrate ATP: V/Etot = 2.3 ± 0.3 min^-1 (the turnover cell, kcat); Km = 445 ± 71 uM; printed V/Km = 86.1 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row R167K, substrate ATP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R167K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P74515 and applied mutation signature H121A to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row H121A, substrate Cysteine; column V/Etot (min^-1) = 5.4 ± 0.1; column Km (uM) = 707 ± 49; column V/Km (M^-1·s^-1) = 127. captured primary segment: Table 2 | SynGCL mutant H121A | substrate Cysteine* (asterisk: reaction performed at sub-saturating 50 mM glutamate) | V/Etot (kcat) 5.4 ± 0.1 min^-1 | Km 707 ± 49 uM | V/Km (kcat/Km) 127 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 2 V/Etot cell 5.4 min^-1; the printed turnover column is per MINUTE, so 5.4 / 60 = 0.09 s^(-1); the exported value is 0.09 s^(-1). Km: printed Table 2 Km cell 707 uM; 1 uM is 1/1000 mM, so 707 / 1000 = 0.707 mM; the exported value is 0.707 mM. kcat/Km: printed Table 2 V/Km cell 127 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 127 / 1000 = 0.127 s^(-1)*mM^(-1); the exported value is 0.1272984441301273 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.09 / 0.707 = 0.1272984441301273 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row H121A, substrate Cysteine: V/Etot = 5.4 ± 0.1 min^-1 (the turnover cell, kcat); Km = 707 ± 49 uM; printed V/Km = 127 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row H121A, substrate Cysteine


column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row H121A, substrate ATP; column V/Etot (min^-1) = 5.9 ± 0.2; column Km (uM) = 310 ± 18; column V/Km (M^-1·s^-1) = 317. captured primary segment: Table 2 | SynGCL mutant H121A | substrate ATP* (asterisk: reaction performed at sub-saturating 50 mM glutamate) | V/Etot (kcat) 5.9 ± 0.2 min^-1 | Km 310 ± 18 uM | V/Km (kcat/Km) 317 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 2 V/Etot cell 5.9 min^-1; the printed turnover column is per MINUTE, so 5.9 / 60 = 0.09833333333333333 s^(-1); the exported value is 0.098 s^(-1). Km: printed Table 2 Km cell 310 uM; 1 uM is 1/1000 mM, so 310 / 1000 = 0.31 mM; the exported value is 0.31 mM. kcat/Km: printed Table 2 V/Km cell 317 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 317 / 1000 = 0.317 s^(-1)*mM^(-1); the exported value is 0.31612903225806455 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.09833333333333333 / 0.31 = 0.3172043010752688 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row H121A, substrate ATP: V/Etot = 5.9 ± 0.2 min^-1 (the turnover cell, kcat); Km = 310 ± 18 uM; printed V/Km = 317 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row H121A, substrate ATP


column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row H121A, substrate Glutamate; column V/Etot (min^-1) = 7.6 ± 2.4; column Km (uM) = 15200 ± 4900; column V/Km (M^-1·s^-1) = 8.3. captured primary segment: Table 2 | SynGCL mutant H121A | substrate Glutamate | V/Etot (kcat) 7.6 ± 2.4 min^-1 | Km 15200 ± 4900 uM | V/Km (kcat/Km) 8.3 M^-1 s^-1

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row H121A, substrate Glutamate: V/Etot = 7.6 ± 2.4 min^-1 (the turnover cell, kcat); Km = 15200 ± 4900 uM; printed V/Km = 8.3 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row H121A, substrate Glutamate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P74515 and applied mutation signature T117S to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row T117S, substrate Cysteine; column V/Etot (min^-1) = 8.0 ± 1.3; column Km (uM) = 186 ± 6.1; column V/Km (M^-1·s^-1) = 717. captured primary segment: Table 2 | SynGCL mutant T117S | substrate Cysteine | V/Etot (kcat) 8.0 ± 1.3 min^-1 | Km 186 ± 6.1 uM | V/Km (kcat/Km) 717 M^-1 s^-1

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row T117S, substrate Cysteine: V/Etot = 8.0 ± 1.3 min^-1 (the turnover cell, kcat); Km = 186 ± 6.1 uM; printed V/Km = 717 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row T117S, substrate Cysteine


column_label: Table 1 (Steady-state kinetic parameters of SynGCL), printed column heads Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 66, PDF page 4. substrate row ATP (wild-type SynGCL); column V/Etot (min^-1) = 30.6 ± 1.9; column Km (uM) = 145 ± 13; column V/Km (M^-1·s^-1) = 3520. captured primary segment: Table 1 | wild-type SynGCL | substrate ATP | V/Etot (kcat) 30.6 ± 1.9 min^-1 | Km 145 ± 13 uM | V/Km (kcat/Km) 3520 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 1 V/Etot cell 30.6 min^-1; the printed turnover column is per MINUTE, so 30.6 / 60 = 0.51 s^(-1); the exported value is 0.137 s^(-1). Km: printed Table 1 Km cell 145 uM; 1 uM is 1/1000 mM, so 145 / 1000 = 0.145 mM; the exported value is 0.145 mM. kcat/Km: printed Table 1 V/Km cell 3520 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3520 / 1000 = 3.52 s^(-1)*mM^(-1); the exported value is 0.9448275862068967 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.51 / 0.145 = 3.517241379310345 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 66, Table 1 (Steady-state kinetic parameters of SynGCL), substrate row ATP (wild-type SynGCL): V/Etot = 30.6 ± 1.9 min^-1 (the turnover cell, kcat); Km = 145 ± 13 uM; printed V/Km = 3520 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 1, substrate row ATP (wild-type SynGCL)

table_label: Table 1: Steady-state kinetic parameters of SynGCL (Biochem. J. 2013, 450: 63-72), printed column heads Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1)


column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row T117S, substrate Glutamate; column V/Etot (min^-1) = 8.2 ± 0.6; column Km (uM) = 6100 ± 150; column V/Km (M^-1·s^-1) = 22.4. captured primary segment: Table 2 | SynGCL mutant T117S | substrate Glutamate | V/Etot (kcat) 8.2 ± 0.6 min^-1 | Km 6100 ± 150 uM | V/Km (kcat/Km) 22.4 M^-1 s^-1

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row T117S, substrate Glutamate: V/Etot = 8.2 ± 0.6 min^-1 (the turnover cell, kcat); Km = 6100 ± 150 uM; printed V/Km = 22.4 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row T117S, substrate Glutamate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P74515 and applied mutation signature H121Q to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row H121Q, substrate Glutamate; column V/Etot (min^-1) = 11.3 ± 1.4; column Km (uM) = 1180 ± 135; column V/Km (M^-1·s^-1) = 160. captured primary segment: Table 2 | SynGCL mutant H121Q | substrate Glutamate | V/Etot (kcat) 11.3 ± 1.4 min^-1 | Km 1180 ± 135 uM | V/Km (kcat/Km) 160 M^-1 s^-1

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row H121Q, substrate Glutamate: V/Etot = 11.3 ± 1.4 min^-1 (the turnover cell, kcat); Km = 1180 ± 135 uM; printed V/Km = 160 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row H121Q, substrate Glutamate


column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row T117S, substrate ATP; column V/Etot (min^-1) = 13.5 ± 1.5; column Km (uM) = 352 ± 19; column V/Km (M^-1·s^-1) = 639. captured primary segment: Table 2 | SynGCL mutant T117S | substrate ATP | V/Etot (kcat) 13.5 ± 1.5 min^-1 | Km 352 ± 19 uM | V/Km (kcat/Km) 639 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 2 V/Etot cell 13.5 min^-1; the printed turnover column is per MINUTE, so 13.5 / 60 = 0.225 s^(-1); the exported value is 0.225 s^(-1). Km: printed Table 2 Km cell 352 uM; 1 uM is 1/1000 mM, so 352 / 1000 = 0.352 mM; the exported value is 0.352 mM. kcat/Km: printed Table 2 V/Km cell 639 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 639 / 1000 = 0.639 s^(-1)*mM^(-1); the exported value is 0.6392045454545455 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.225 / 0.352 = 0.6392045454545455 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row T117S, substrate ATP: V/Etot = 13.5 ± 1.5 min^-1 (the turnover cell, kcat); Km = 352 ± 19 uM; printed V/Km = 639 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row T117S, substrate ATP


column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row H121Q, substrate Cysteine; column V/Etot (min^-1) = 20.1 ± 2.7; column Km (uM) = 116 ± 16; column V/Km (M^-1·s^-1) = 2890. captured primary segment: Table 2 | SynGCL mutant H121Q | substrate Cysteine | V/Etot (kcat) 20.1 ± 2.7 min^-1 | Km 116 ± 16 uM | V/Km (kcat/Km) 2890 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 2 V/Etot cell 20.1 min^-1; the printed turnover column is per MINUTE, so 20.1 / 60 = 0.335 s^(-1); the exported value is 0.335 s^(-1). Km: printed Table 2 Km cell 116 uM; 1 uM is 1/1000 mM, so 116 / 1000 = 0.116 mM; the exported value is 0.116 mM. kcat/Km: printed Table 2 V/Km cell 2890 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2890 / 1000 = 2.89 s^(-1)*mM^(-1); the exported value is 2.8879310344827585 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.335 / 0.116 = 2.8879310344827585 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row H121Q, substrate Cysteine: V/Etot = 20.1 ± 2.7 min^-1 (the turnover cell, kcat); Km = 116 ± 16 uM; printed V/Km = 2890 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row H121Q, substrate Cysteine


column_label: Table 1 (Steady-state kinetic parameters of SynGCL), printed column heads Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 66, PDF page 4. substrate row Glutamate (wild-type SynGCL); column V/Etot (min^-1) = 21.0 ± 1.3; column Km (uM) = 953 ± 16; column V/Km (M^-1·s^-1) = 367. captured primary segment: Table 1 | wild-type SynGCL | substrate Glutamate | V/Etot (kcat) 21.0 ± 1.3 min^-1 | Km 953 ± 16 uM | V/Km (kcat/Km) 367 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 1 V/Etot cell 21.0 min^-1; the printed turnover column is per MINUTE, so 21.0 / 60 = 0.35 s^(-1); the exported value is 0.35 s^(-1). Km: printed Table 1 Km cell 953 uM; 1 uM is 1/1000 mM, so 953 / 1000 = 0.953 mM; the exported value is 0.953 mM. kcat/Km: printed Table 1 V/Km cell 367 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 367 / 1000 = 0.367 s^(-1)*mM^(-1); the exported value is 0.3672612801678909 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.35 / 0.953 = 0.3672612801678909 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 66, Table 1 (Steady-state kinetic parameters of SynGCL), substrate row Glutamate (wild-type SynGCL): V/Etot = 21.0 ± 1.3 min^-1 (the turnover cell, kcat); Km = 953 ± 16 uM; printed V/Km = 367 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 1, substrate row Glutamate (wild-type SynGCL)


column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row H121Q, substrate ATP; column V/Etot (min^-1) = 22.9 ± 2.2; column Km (uM) = 279 ± 66; column V/Km (M^-1·s^-1) = 1370. captured primary segment: Table 2 | SynGCL mutant H121Q | substrate ATP | V/Etot (kcat) 22.9 ± 2.2 min^-1 | Km 279 ± 66 uM | V/Km (kcat/Km) 1370 M^-1 s^-1

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row H121Q, substrate ATP: V/Etot = 22.9 ± 2.2 min^-1 (the turnover cell, kcat); Km = 279 ± 66 uM; printed V/Km = 1370 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row H121Q, substrate ATP


column_label: Table 1 (Steady-state kinetic parameters of SynGCL), printed column heads Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 66, PDF page 4. substrate row Cysteine (wild-type SynGCL); column V/Etot (min^-1) = 25.2 ± 1.7; column Km (uM) = 59 ± 0.5; column V/Km (M^-1·s^-1) = 7120. captured primary segment: Table 1 | wild-type SynGCL | substrate Cysteine | V/Etot (kcat) 25.2 ± 1.7 min^-1 | Km 59 ± 0.5 uM | V/Km (kcat/Km) 7120 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 1 V/Etot cell 25.2 min^-1; the printed turnover column is per MINUTE, so 25.2 / 60 = 0.42 s^(-1); the exported value is 0.42 s^(-1). Km: printed Table 1 Km cell 59 uM; 1 uM is 1/1000 mM, so 59 / 1000 = 0.059 mM; the exported value is 0.059 mM. kcat/Km: printed Table 1 V/Km cell 7120 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7120 / 1000 = 7.12 s^(-1)*mM^(-1); the exported value is 7.11864406779661 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.42 / 0.059 = 7.11864406779661 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 66, Table 1 (Steady-state kinetic parameters of SynGCL), substrate row Cysteine (wild-type SynGCL): V/Etot = 25.2 ± 1.7 min^-1 (the turnover cell, kcat); Km = 59 ± 0.5 uM; printed V/Km = 7120 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 1, substrate row Cysteine (wild-type SynGCL)


organism: Trypanosoma brucei

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E489A with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.

proof_lines: mutant E489A, pH 8.0, 37°C, in presence of Mn2+

proof_lines: mutant E489A, pH 8.0, 37°C, in presence of Mg2+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E93A to reconstruct the assayed variant sequence.

proof_lines: mutant E93A, pH 8.0, 37°C, in presence of Mg2+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q321A to reconstruct the assayed variant sequence.


proof_lines: mutant Q321A, pH 8.0, 37°C, in presence of Mn2+


proof_lines: wild-type and mutant enzyme, pH 8.0, 37°C

proof_lines: wild-type enzyme, pH 8.0, 37°C, in presence of Mn2+


proof_lines: mutant Q321A, pH 8.0, 37°C, in presence of Mg2+


substrate_name: L-alpha-aminobutyrate

smiles: CCC(C(=O)O)N

substrate: L-alpha-aminobutyrate


organism: Arabidopsis thaliana

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R454A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R454A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kin


smiles: C(C(=O)O)N

assay_conditions_summary: pH 7.5; cofactor NADH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K456M with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K456M, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kin


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R274K with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R274K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kin


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N376A with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N376A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kin


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R454K with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R454K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kin


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S155A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S155A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kin


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S153A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S153A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kin


organism: Allium cepa

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.

proof_lines: in the absence of Cd2+, pH and temperature not specified in the publication

proof_lines: in the presence of 0.1 mM Cd2+, pH and temperature not specified in the publication


organism: Pseudoalteromonas haloplanktis


assay_conditions_summary: pH 8; 288.15 K; cofactor ATP


enzyme_display_name: D-alanine--D-alanine ligase

assay_conditions_summary: pH 7.3; 310.15 K; cofactor ATP

proof_lines:
Raw SKiD Env: Temp=37°C, pH=8
kcat is 9.7 sec(-1) (at pH 7.3).

enzyme: D-alanine--D-alanine ligase


substrate_name: D-alanine

smiles: CC(C(=O)O)N

substrate: D-alanine


substrate_name: ATP

assay_conditions_summary: pH 7.8; cofactor ATP

proof_lines: pH 7.8, 10°C, recombinant enzyme, ATPase activity

proof_lines: pH 7.8, 15°C, recombinant enzyme, ATPase activity

proof_lines: pH 7.8, 20°C, recombinant enzyme, ATPase activity


substrate_name: gamma-L-glutamyl-L-cysteine

smiles: C(CC(=O)NC(CS)C(=O)O)C(C(=O)O)N

substrate: gamma-L-glutamyl-L-cysteine


substrate_name: glycine

substrate: glycine


substrate_name: L-Glu

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C319A to reconstruct the assayed variant sequence.

substrate: L-Glu


substrate_name: L-2-aminobutyric acid

substrate: L-2-aminobutyric acid


verification_status: verified

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q26820 and applied mutation signature R491A to reconstruct the assayed variant sequence.

column_label: Table 1, Table 1, enzyme row 'R491A'; column 'kcat (s-1)' = 0.055; column 'Kmapp(L-Glu) (mM)' = 0.61; column 'Kmapp(L-Aba) (mM)' = nd; column 'Kmapp(ATP) (mM)' = 0.11; Table 1 carries no kcat/Km column. The printed cells carry error terms that this pdftotext rendering shows with the plus-minus sign decoded as an opening parenthesis, and only the leading value of each cell is transcribed here.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.055 s-1; already in s^-1, so no unit conversion applies (this article prints no min^-1 kinetic cell); the paper value is 0.055 s^(-1). Km: printed Table 1 cell 0.61 mM; already in mM, so no unit conversion applies; the paper value is 0.61 mM. kcat/Km: Table 1 has no kcat/Km column, so the paper value 0.09016393442622951 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.055 / 0.61 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, Table 1, enzyme row 'R491A': kcat = 0.055 s-1; apparent Km = 0.61 mM; Table 1 prints no kcat/Km cell for this measurement.

row_label: Table 1, enzyme row 'R491A'

table_label: Table 1: Steady-State Kinetic Analysis of T. brucei gamma-GCS Mutant Enzymes (Biochemistry 2002, 41(8):2741-2750)

status: verified


smiles: C(CC(=O)O)CN

column_label: Table 3, Table 3, wild-type gamma-GCS column, rows 'kcat(GABA) (s-1)' and 'Kmapp(GABA) (mM)'; row 'kcat(GABA) (s-1)' = 0.14; row 'Kmapp(GABA) (mM)' = 150; row 'kcat(L-Glu) (s-1)' = 3.9; row 'Kmapp(L-Glu) (mM)' = 0.24; Table 3 carries no kcat/Km column. The printed cells carry error terms that this pdftotext rendering shows with the plus-minus sign decoded as an opening parenthesis, and only the leading value of each cell is transcribed here.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.14 s-1; already in s^-1, so no unit conversion applies (this article prints no min^-1 kinetic cell); the paper value is 0.14 s^(-1). Km: printed Table 3 cell 150 mM; already in mM, so no unit conversion applies; the paper value is 150.0 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 0.0009333333333333334 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.14 / 150 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, Table 3, wild-type gamma-GCS column, rows 'kcat(GABA) (s-1)' and 'Kmapp(GABA) (mM)': kcat = 0.14 s-1; apparent Km = 150 mM; Table 3 prints no kcat/Km cell for this measurement.

table_label: Table 3: Comparison of Wild-Type and R366A gamma-GCS Steady-State Kinetics for ATP Hydrolysis with L-Glu versus GABA as Substrates (Biochemistry 2002, 41(8):2741-2750)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q26820 and applied mutation signature R474A to reconstruct the assayed variant sequence.

column_label: Table 1, Table 1, enzyme row 'R474A'; column 'kcat (s-1)' = 0.24; column 'Kmapp(L-Glu) (mM)' = 1.6; column 'Kmapp(L-Aba) (mM)' = 56; column 'Kmapp(ATP) (mM)' = 1.3; Table 1 carries no kcat/Km column. The printed cells carry error terms that this pdftotext rendering shows with the plus-minus sign decoded as an opening parenthesis, and only the leading value of each cell is transcribed here.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.24 s-1; already in s^-1, so no unit conversion applies (this article prints no min^-1 kinetic cell); the paper value is 0.24 s^(-1). Km: printed Table 1 cell 1.6 mM; already in mM, so no unit conversion applies; the paper value is 1.6 mM. kcat/Km: Table 1 has no kcat/Km column, so the paper value 0.15 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.24 / 1.6 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, Table 1, enzyme row 'R474A': kcat = 0.24 s-1; apparent Km = 1.6 mM; Table 1 prints no kcat/Km cell for this measurement.

row_label: Table 1, enzyme row 'R474A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q26820 and applied mutation signature R366A to reconstruct the assayed variant sequence.

column_label: Table 1, Table 1, enzyme row 'R366A'; column 'kcat (s-1)' = 0.32; column 'Kmapp(L-Glu) (mM)' = 130; column 'Kmapp(L-Aba) (mM)' = 34; column 'Kmapp(ATP) (mM)' = 2.8; Table 1 carries no kcat/Km column. The printed cells carry error terms that this pdftotext rendering shows with the plus-minus sign decoded as an opening parenthesis, and only the leading value of each cell is transcribed here.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.32 s-1; already in s^-1, so no unit conversion applies (this article prints no min^-1 kinetic cell); the paper value is 0.32 s^(-1). Km: printed Table 1 cell 130 mM; already in mM, so no unit conversion applies; the paper value is 130.0 mM. kcat/Km: Table 1 has no kcat/Km column, so the paper value 0.0024615384615384616 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.32 / 130 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, Table 1, enzyme row 'R366A': kcat = 0.32 s-1; apparent Km = 130 mM; Table 1 prints no kcat/Km cell for this measurement.

row_label: Table 1, enzyme row 'R366A'


column_label: Table 3, Table 3, R366A gamma-GCS column, rows 'kcat(GABA) (s-1)' and 'Kmapp(GABA) (mM)'; row 'kcat(GABA) (s-1)' = 0.59; row 'Kmapp(GABA) (mM)' = 20; row 'kcat(L-Glu) (s-1)' = 0.32; row 'Kmapp(L-Glu) (mM)' = 130; Table 3 carries no kcat/Km column. The printed cells carry error terms that this pdftotext rendering shows with the plus-minus sign decoded as an opening parenthesis, and only the leading value of each cell is transcribed here.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.59 s-1; already in s^-1, so no unit conversion applies (this article prints no min^-1 kinetic cell); the paper value is 0.59 s^(-1). Km: printed Table 3 cell 20 mM; already in mM, so no unit conversion applies; the paper value is 20.0 mM. kcat/Km: Table 3 has no kcat/Km column, so the paper value 0.0295 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.59 / 20 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 3, Table 3, R366A gamma-GCS column, rows 'kcat(GABA) (s-1)' and 'Kmapp(GABA) (mM)': kcat = 0.59 s-1; apparent Km = 20 mM; Table 3 prints no kcat/Km cell for this measurement.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q26820 and applied mutation signature R179A to reconstruct the assayed variant sequence.

column_label: Table 1, Table 1, enzyme row 'R179A'; column 'kcat (s-1)' = 0.61; column 'Kmapp(L-Glu) (mM)' = 5.2; column 'Kmapp(L-Aba) (mM)' = 380; column 'Kmapp(ATP) (mM)' = 0.14; Table 1 carries no kcat/Km column. The printed cells carry error terms that this pdftotext rendering shows with the plus-minus sign decoded as an opening parenthesis, and only the leading value of each cell is transcribed here.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.61 s-1; already in s^-1, so no unit conversion applies (this article prints no min^-1 kinetic cell); the paper value is 0.61 s^(-1). Km: printed Table 1 cell 5.2 mM; already in mM, so no unit conversion applies; the paper value is 5.2 mM. kcat/Km: Table 1 has no kcat/Km column, so the paper value 0.11730769230769231 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.61 / 5.2 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, Table 1, enzyme row 'R179A': kcat = 0.61 s-1; apparent Km = 5.2 mM; Table 1 prints no kcat/Km cell for this measurement.

row_label: Table 1, enzyme row 'R179A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q26820 and applied mutation signature T323A to reconstruct the assayed variant sequence.

column_label: Table 1, Table 1, enzyme row 'T323A'; column 'kcat (s-1)' = 0.79; column 'Kmapp(L-Glu) (mM)' = 1.7; column 'Kmapp(L-Aba) (mM)' = 7.5; column 'Kmapp(ATP) (mM)' = 7.0; Table 1 carries no kcat/Km column. The printed cells carry error terms that this pdftotext rendering shows with the plus-minus sign decoded as an opening parenthesis, and only the leading value of each cell is transcribed here.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.79 s-1; already in s^-1, so no unit conversion applies (this article prints no min^-1 kinetic cell); the paper value is 0.79 s^(-1). Km: printed Table 1 cell 1.7 mM; already in mM, so no unit conversion applies; the paper value is 1.7 mM. kcat/Km: Table 1 has no kcat/Km column, so the paper value 0.4647058823529412 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 0.79 / 1.7 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, Table 1, enzyme row 'T323A': kcat = 0.79 s-1; apparent Km = 1.7 mM; Table 1 prints no kcat/Km cell for this measurement.

row_label: Table 1, enzyme row 'T323A'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q26820 and applied mutation signature R487A to reconstruct the assayed variant sequence.

column_label: Table 1, Table 1, enzyme row 'R487A'; column 'kcat (s-1)' = 1.2; column 'Kmapp(L-Glu) (mM)' = 1.3; column 'Kmapp(L-Aba) (mM)' = 15; column 'Kmapp(ATP) (mM)' = 1.2; Table 1 carries no kcat/Km column. The printed cells carry error terms that this pdftotext rendering shows with the plus-minus sign decoded as an opening parenthesis, and only the leading value of each cell is transcribed here.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.2 s-1; already in s^-1, so no unit conversion applies (this article prints no min^-1 kinetic cell); the paper value is 1.2 s^(-1). Km: printed Table 1 cell 1.3 mM; already in mM, so no unit conversion applies; the paper value is 1.3 mM. kcat/Km: Table 1 has no kcat/Km column, so the paper value 0.923076923076923 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 1.2 / 1.3 of this measurement's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, Table 1, enzyme row 'R487A': kcat = 1.2 s-1; apparent Km = 1.3 mM; Table 1 prints no kcat/Km cell for this measurement.

row_label: Table 1, enzyme row 'R487A'


proof_lines: wild-type enzyme, pH 8.0, 37°C, in presence of Mg2+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R491A with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

substrate: ATP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R179A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R487A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R474A with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R366A with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T323A to reconstruct the assayed variant sequence.


column_label: Table 3 (Steady-state kinetic parameters of SynGS), printed column heads Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. substrate row Glycine (wild-type SynGS); column V/Etot (min^-1) = 253 ± 35; column Km (uM) = 407 ± 90; column V/Km (M^-1·s^-1) = 10 360. captured primary segment: Table 3 | wild-type SynGS | substrate Glycine | V/Etot (kcat) 253 ± 35 min^-1 | Km 407 ± 90 uM | V/Km (kcat/Km) 10 360 M^-1 s^-1 (plain numeral 10360 M^-1 s^-1)

raw_value_unit_evidence: Journal page 67, Table 3 (Steady-state kinetic parameters of SynGS), substrate row Glycine (wild-type SynGS): V/Etot = 253 ± 35 min^-1 (the turnover cell, kcat); Km = 407 ± 90 uM; printed V/Km = 10 360 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km, printed with a thousands space; plain numeral 10360).

row_label: Table 3, substrate row Glycine (wild-type SynGS)

table_label: Table 3: Steady-state kinetic parameters of SynGS (Biochem. J. 2013, 450: 63-72), printed column heads Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1)


column_label: Table 3 (Steady-state kinetic parameters of SynGS), printed column heads Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. substrate row γ-Glutamylcysteine (wild-type SynGS); column V/Etot (min^-1) = 277 ± 29; column Km (uM) = 99 ± 14; column V/Km (M^-1·s^-1) = 46 630. captured primary segment: Table 3 | wild-type SynGS | substrate γ-Glutamylcysteine | V/Etot (kcat) 277 ± 29 min^-1 | Km 99 ± 14 uM | V/Km (kcat/Km) 46 630 M^-1 s^-1 (plain numeral 46630 M^-1 s^-1)

normalized_value_unit_evidence: kcat: printed Table 3 V/Etot cell 277 min^-1; the printed turnover column is per MINUTE, so 277 / 60 = 4.616666666666666 s^(-1); the exported value is 4.62 s^(-1). Km: printed Table 3 Km cell 99 uM; 1 uM is 1/1000 mM, so 99 / 1000 = 0.099 mM; the exported value is 0.099 mM. kcat/Km: printed Table 3 V/Km cell 46 630 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 46630 / 1000 = 46.63 s^(-1)*mM^(-1); the exported value is 46.666666666666664 s^(-1)*mM^(-1). Quotient disclosure for this row: 4.616666666666666 / 0.099 = 46.63299663299663 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 67, Table 3 (Steady-state kinetic parameters of SynGS), substrate row γ-Glutamylcysteine (wild-type SynGS): V/Etot = 277 ± 29 min^-1 (the turnover cell, kcat); Km = 99 ± 14 uM; printed V/Km = 46 630 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km, printed with a thousands space; plain numeral 46630).

row_label: Table 3, substrate row γ-Glutamylcysteine (wild-type SynGS)


column_label: Table 3 (Steady-state kinetic parameters of SynGS), printed column heads Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. substrate row ATP (wild-type SynGS); column V/Etot (min^-1) = 324 ± 18; column Km (uM) = 136 ± 12; column V/Km (M^-1·s^-1) = 39 710. captured primary segment: Table 3 | wild-type SynGS | substrate ATP | V/Etot (kcat) 324 ± 18 min^-1 | Km 136 ± 12 uM | V/Km (kcat/Km) 39 710 M^-1 s^-1 (plain numeral 39710 M^-1 s^-1)

normalized_value_unit_evidence: kcat: printed Table 3 V/Etot cell 324 min^-1; the printed turnover column is per MINUTE, so 324 / 60 = 5.4 s^(-1); the exported value is 5.4 s^(-1). Km: printed Table 3 Km cell 136 uM; 1 uM is 1/1000 mM, so 136 / 1000 = 0.136 mM; the exported value is 0.136 mM. kcat/Km: printed Table 3 V/Km cell 39 710 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 39710 / 1000 = 39.71 s^(-1)*mM^(-1); the exported value is 39.705882352941174 s^(-1)*mM^(-1). Quotient disclosure for this row: 5.4 / 0.136 = 39.705882352941174 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 67, Table 3 (Steady-state kinetic parameters of SynGS), substrate row ATP (wild-type SynGS): V/Etot = 324 ± 18 min^-1 (the turnover cell, kcat); Km = 136 ± 12 uM; printed V/Km = 39 710 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km, printed with a thousands space; plain numeral 39710).

row_label: Table 3, substrate row ATP (wild-type SynGS)


organism: Actinobacillus succinogenes

assay_conditions_summary: pH 8.5; 313.15 K; cofactor ATP

proof_lines: pH 8.5, 40°C, recombinant His-tagged enzyme


organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

substrate_name: L-lysine (at pH 9.4)

smiles: C(CCN)CC(C(=O)O)N

proof_lines: The catalytic efficiency for the L-lysine adding activity is 4-fold and 10-fold higher than that for the D-lysine and meso-diaminopimelate adding activity, respectively.

substrate: L-lysine (at pH 9.4)


substrate_name: meso-diaminopimelate (at pH 9.4)

substrate: meso-diaminopimelate (at pH 9.4)


substrate_name: L-ornithine (at pH 9.4)

substrate: L-ornithine (at pH 9.4)


assay_conditions_summary: cofactor ATP


organism: Homo sapiens

substrate_name: L-Cys

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature P138L with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

proof_lines: mutant P138L, catalytic subunit, pH 8.0, 37°C

proof_lines: mutant P138L, CGL holoenzyme, pH 8.0, 37°C

substrate: L-Cys


enzyme_display_name: mandelate racemase

organism: Pseudomonas putida

substrate_name: (S)-Mandelate

sequence_variant_note: No sequence was resolved for this record, so variant-aware sequence handling could not be applied.

assay_conditions_summary: pH 7.5; buffer Na-HEPES

proof_lines: recombinant mandelate racemase, putative misfolded form with N-terminal hexahistidine tag, Na-HEPES buffer (0.1 M, pH 7.5), 3.3 mM MgCl2

proof_lines: recombinant mandelate racemase fusion protein bearing an N-terminal StrepII-tag and a C-terminal decahistidine tag, Na-HEPES buffer (0.1 M, pH 7.5), 3.3 mM MgCl2

proof_lines: recombinant mandelate racemase represents correctly folded enzyme, with N-terminal hexahistidine tag, in Na-HEPES buffer (0.1 M, pH 7.5), 3.3 mM MgCl2

enzyme: mandelate racemase

substrate: (S)-Mandelate


organism: Plasmodium berghei

sequence_variant_note: Sequence identity was resolved, but no explicit wild-type or mutant call was captured.

assay_conditions_summary: pH 8.2; cofactor ATP

proof_lines: pH 8.2, temperature not specified in the publication


organism: Drosophila melanogaster

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.

proof_lines: 25°C, recombinant His-tagged wild-type enzyme

proof_lines: 25°C, recombinant His-tagged wild-type catalytic subunit with recombinant His-tagged mutant modifier subunit C213S/C214S/C267S


organism: Spinacia oleracea


organism: Streptococcus agalactiae


organism: Enterococcus faecalis

substrate_name: D-Alanine; ATP

substrate: D-Alanine; ATP


organism: Enterococcus faecium

substrate_name: ATP; D-Alanine

substrate: ATP; D-Alanine


organism: Staphylococcus aureus (strain NCTC 8325 / PS 47)

substrate_name: UDP-N-acetylmuramoyl-L-Ala-D-Glu

substrate: UDP-N-acetylmuramoyl-L-Ala-D-Glu


proof_lines:
25°C, pH 7.5
pH 7.5, 25°C, substrate: (R)-mandelate
pH 6.3


substrate_name: (S)-lactate

proof_lines: pH 7.5, 25°C, recombinant wild-type enzyme

substrate: (S)-lactate


substrate_name: Unknown

substrate: Unknown


organism: Brassica juncea

substrate_name: L-cysteine

substrate: L-cysteine


substrate_name: L-glutamate

substrate: L-glutamate


organism: Mus musculus

substrate_name: L-Glutamate; ATP; L-alpha-Aminobutyrate

substrate: L-Glutamate; ATP; L-alpha-Aminobutyrate


organism: Trypanosoma brucei


organism: Arabidopsis thaliana

substrate_name: gamma-Glu-L-Cys

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N376A with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

proof_lines: mutant enzyme N376A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kin

substrate: gamma-Glu-L-Cys


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R454A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R454A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kin


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R274K with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R274K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kin


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S153A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S153A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kin


organism: Streptococcus pyogenes


organism: Escherichia coli

substrate_name: L-Alanine; UDP-N-acetylmuramate; ATP

substrate: L-Alanine; UDP-N-acetylmuramate; ATP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S155A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S155A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kin


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K456M with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K456M, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kin


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R454K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R454K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kin


organism: Pseudoalteromonas haloplanktis


organism: Synechocystis sp.

proof_lines: pH 7.5, 25°C, versus gamma-L-glutamyl-L-cysteine


organism: Homo sapiens


proof_lines: 37°C, Kis, noncompetitive versus 1-(5'-phosphoribosyl)-5-amino-4-carboxyimidazole


organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

proof_lines: The catalytic efficiency for the L-lysine adding activity is 4-fold and 10-fold higher than that for the D-lysine and meso-diaminopimelate adding activity, respectively.


substrate_name: ATP; L-Cysteine; L-Glutamate

substrate: ATP; L-Cysteine; L-Glutamate


column_label: Primary-paper abstract reports L-alpha-aminobutyrate apparent Km as 10 mM; source L-2-aminobutanoate is the same substrate name.

raw_value_unit_evidence: L-alpha-aminobutyrate apparent Km 10 mM

row_label: L-alpha-aminobutyrate apparent Km statement

table_label: PubMed primary-paper abstract for PMID 8663359


organism: Ovis aries


organism: Pasteurella multocida


organism: Plasmodium berghei

substrate_name: gamma-L-Glu-L-Cys

assay_conditions_summary: pH 8.2; 310.15 K; cofactor ATP

substrate: gamma-L-Glu-L-Cys


substrate_name: (R)-Pantoate; ATP; beta-Alanine

substrate: (R)-Pantoate; ATP; beta-Alanine


organism: Mycobacterium tuberculosis

substrate_name: ATP; D-Pantoate

substrate: ATP; D-Pantoate


substrate_name: L-Glutamate; ATP; L-Cysteine

substrate: L-Glutamate; ATP; L-Cysteine


organism: Ascaris suum

substrate_name: L-aminobutanoate

substrate: L-aminobutanoate


substrate_name: L-aminobutyrate

column_label: PubMed abstract maps L-glutamate/L-cysteine/L-gamma-aminobutyrate/ATP to 1.8/0.1/1.3/0.4 mM respectively

normalized_value_unit_evidence: km=1.3 mM

raw_value_unit_evidence: Km 1.3 mM for L-gamma-aminobutyrate, an L-cysteine surrogate

row_label: Km values respectively list: L-glutamate, L-cysteine, L-gamma-aminobutyrate, ATP

table_label: PubMed abstract

substrate: L-aminobutyrate


sequence_variant_note: Source notes indicate a mutant or variant enzyme, but no machine-applicable substitution signature was available.


organism: Actinobacillus succinogenes

proof_lines: pH 8.5, 40°C, recombinant His-tagged enzyme


substrate_name: ATP

substrate: ATP


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: beta-alanine

smiles: C(CN)C(=O)O

substrate: beta-alanine


smiles: C(CS)N


substrate_name: carbamate

substrate: carbamate


smiles: C(CCN)CC(=O)O


substrate_name: methylamine

smiles: CN

substrate: methylamine


substrate_name: glycine

substrate: glycine


substrate_name: ethylamine

substrate: ethylamine


substrate_name: taurine

substrate: taurine


substrate_name: glycolate

smiles: C(C(=O)O)O

substrate: glycolate


substrate_name: gamma-aminobutyrate

substrate: gamma-aminobutyrate


substrate_name: gamma-amino-beta-hydroxybutyrate

smiles: C(C(CN)O)C(=O)O

substrate: gamma-amino-beta-hydroxybutyrate


substrate_name: D-Alanine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E15Q with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

substrate: D-Alanine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S150A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y216F to reconstruct the assayed variant sequence.


enzyme_display_name: triose-phosphate isomerase

substrate_name: glycerone phosphate

smiles: C(C(=O)COP(=O)(O)O)O

enzyme: triose-phosphate isomerase

substrate: glycerone phosphate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P74515 and applied mutation signature H121A to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row H121A, substrate ATP; column V/Etot (min^-1) = 5.9 ± 0.2; column Km (uM) = 310 ± 18; column V/Km (M^-1·s^-1) = 317. captured primary segment: Table 2 | SynGCL mutant H121A | substrate ATP* (asterisk: reaction performed at sub-saturating 50 mM glutamate) | V/Etot (kcat) 5.9 ± 0.2 min^-1 | Km 310 ± 18 uM | V/Km (kcat/Km) 317 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 2 V/Etot cell 5.9 min^-1; the printed turnover column is per MINUTE, so 5.9 / 60 = 0.09833333333333333 s^(-1); the exported value is 0.098 s^(-1). Km: printed Table 2 Km cell 310 uM; 1 uM is 1/1000 mM, so 310 / 1000 = 0.31 mM; the exported value is 0.31 mM. kcat/Km: printed Table 2 V/Km cell 317 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 317 / 1000 = 0.317 s^(-1)*mM^(-1); the exported value is 0.31612903225806455 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.09833333333333333 / 0.31 = 0.3172043010752688 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row H121A, substrate ATP: V/Etot = 5.9 ± 0.2 min^-1 (the turnover cell, kcat); Km = 310 ± 18 uM; printed V/Km = 317 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row H121A, substrate ATP


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P74515 and applied mutation signature H121Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P74515 and applied mutation signature R167K to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row R167K, substrate ATP; column V/Etot (min^-1) = 2.3 ± 0.3; column Km (uM) = 445 ± 71; column V/Km (M^-1·s^-1) = 86.1. captured primary segment: Table 2 | SynGCL mutant R167K | substrate ATP* (asterisk: reaction performed at sub-saturating 50 mM glutamate) | V/Etot (kcat) 2.3 ± 0.3 min^-1 | Km 445 ± 71 uM | V/Km (kcat/Km) 86.1 M^-1 s^-1

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row R167K, substrate ATP: V/Etot = 2.3 ± 0.3 min^-1 (the turnover cell, kcat); Km = 445 ± 71 uM; printed V/Km = 86.1 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row R167K, substrate ATP


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P74515 and applied mutation signature R248K to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row R248K, substrate ATP; column V/Etot (min^-1) = 0.5 ± 0.1; column Km (uM) = 969 ± 77; column V/Km (M^-1·s^-1) = 8.6. captured primary segment: Table 2 | SynGCL mutant R248K | substrate ATP | V/Etot (kcat) 0.5 ± 0.1 min^-1 | Km 969 ± 77 uM | V/Km (kcat/Km) 8.6 M^-1 s^-1

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row R248K, substrate ATP: V/Etot = 0.5 ± 0.1 min^-1 (the turnover cell, kcat); Km = 969 ± 77 uM; printed V/Km = 8.6 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row R248K, substrate ATP


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P74515 and applied mutation signature T117S to reconstruct the assayed variant sequence.

column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row T117S, substrate ATP; column V/Etot (min^-1) = 13.5 ± 1.5; column Km (uM) = 352 ± 19; column V/Km (M^-1·s^-1) = 639. captured primary segment: Table 2 | SynGCL mutant T117S | substrate ATP | V/Etot (kcat) 13.5 ± 1.5 min^-1 | Km 352 ± 19 uM | V/Km (kcat/Km) 639 M^-1 s^-1

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row T117S, substrate ATP: V/Etot = 13.5 ± 1.5 min^-1 (the turnover cell, kcat); Km = 352 ± 19 uM; printed V/Km = 639 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row T117S, substrate ATP


sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.


substrate_name: L-glutamate

column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row H121A, substrate Glutamate; column V/Etot (min^-1) = 7.6 ± 2.4; column Km (uM) = 15200 ± 4900; column V/Km (M^-1·s^-1) = 8.3. captured primary segment: Table 2 | SynGCL mutant H121A | substrate Glutamate | V/Etot (kcat) 7.6 ± 2.4 min^-1 | Km 15200 ± 4900 uM | V/Km (kcat/Km) 8.3 M^-1 s^-1

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row H121A, substrate Glutamate: V/Etot = 7.6 ± 2.4 min^-1 (the turnover cell, kcat); Km = 15200 ± 4900 uM; printed V/Km = 8.3 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row H121A, substrate Glutamate

substrate: L-glutamate


column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row H121Q, substrate Glutamate; column V/Etot (min^-1) = 11.3 ± 1.4; column Km (uM) = 1180 ± 135; column V/Km (M^-1·s^-1) = 160. captured primary segment: Table 2 | SynGCL mutant H121Q | substrate Glutamate | V/Etot (kcat) 11.3 ± 1.4 min^-1 | Km 1180 ± 135 uM | V/Km (kcat/Km) 160 M^-1 s^-1

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row H121Q, substrate Glutamate: V/Etot = 11.3 ± 1.4 min^-1 (the turnover cell, kcat); Km = 1180 ± 135 uM; printed V/Km = 160 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row H121Q, substrate Glutamate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R167K to reconstruct the assayed variant sequence.


column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row R248K, substrate Glutamate; column V/Etot (min^-1) = 0.5 ± 0.1; column Km (uM) = 3760 ± 427; column V/Km (M^-1·s^-1) = 2.2. captured primary segment: Table 2 | SynGCL mutant R248K | substrate Glutamate | V/Etot (kcat) 0.5 ± 0.1 min^-1 | Km 3760 ± 427 uM | V/Km (kcat/Km) 2.2 M^-1 s^-1

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row R248K, substrate Glutamate: V/Etot = 0.5 ± 0.1 min^-1 (the turnover cell, kcat); Km = 3760 ± 427 uM; printed V/Km = 2.2 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row R248K, substrate Glutamate


column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row T117S, substrate Glutamate; column V/Etot (min^-1) = 8.2 ± 0.6; column Km (uM) = 6100 ± 150; column V/Km (M^-1·s^-1) = 22.4. captured primary segment: Table 2 | SynGCL mutant T117S | substrate Glutamate | V/Etot (kcat) 8.2 ± 0.6 min^-1 | Km 6100 ± 150 uM | V/Km (kcat/Km) 22.4 M^-1 s^-1

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row T117S, substrate Glutamate: V/Etot = 8.2 ± 0.6 min^-1 (the turnover cell, kcat); Km = 6100 ± 150 uM; printed V/Km = 22.4 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row T117S, substrate Glutamate


column_label: Table 1 (Steady-state kinetic parameters of SynGCL), printed column heads Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 66, PDF page 4. substrate row Glutamate (wild-type SynGCL); column V/Etot (min^-1) = 21.0 ± 1.3; column Km (uM) = 953 ± 16; column V/Km (M^-1·s^-1) = 367. captured primary segment: Table 1 | wild-type SynGCL | substrate Glutamate | V/Etot (kcat) 21.0 ± 1.3 min^-1 | Km 953 ± 16 uM | V/Km (kcat/Km) 367 M^-1 s^-1

raw_value_unit_evidence: Journal page 66, Table 1 (Steady-state kinetic parameters of SynGCL), substrate row Glutamate (wild-type SynGCL): V/Etot = 21.0 ± 1.3 min^-1 (the turnover cell, kcat); Km = 953 ± 16 uM; printed V/Km = 367 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 1, substrate row Glutamate (wild-type SynGCL)


substrate_name: L-Cysteine

column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row H121A, substrate Cysteine; column V/Etot (min^-1) = 5.4 ± 0.1; column Km (uM) = 707 ± 49; column V/Km (M^-1·s^-1) = 127. captured primary segment: Table 2 | SynGCL mutant H121A | substrate Cysteine* (asterisk: reaction performed at sub-saturating 50 mM glutamate) | V/Etot (kcat) 5.4 ± 0.1 min^-1 | Km 707 ± 49 uM | V/Km (kcat/Km) 127 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 2 V/Etot cell 5.4 min^-1; the printed turnover column is per MINUTE, so 5.4 / 60 = 0.09 s^(-1); the exported value is 0.09 s^(-1). Km: printed Table 2 Km cell 707 uM; 1 uM is 1/1000 mM, so 707 / 1000 = 0.707 mM; the exported value is 0.707 mM. kcat/Km: printed Table 2 V/Km cell 127 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 127 / 1000 = 0.127 s^(-1)*mM^(-1); the exported value is 0.1272984441301273 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.09 / 0.707 = 0.1272984441301273 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row H121A, substrate Cysteine: V/Etot = 5.4 ± 0.1 min^-1 (the turnover cell, kcat); Km = 707 ± 49 uM; printed V/Km = 127 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row H121A, substrate Cysteine

substrate: L-Cysteine


column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row H121Q, substrate Cysteine; column V/Etot (min^-1) = 20.1 ± 2.7; column Km (uM) = 116 ± 16; column V/Km (M^-1·s^-1) = 2890. captured primary segment: Table 2 | SynGCL mutant H121Q | substrate Cysteine | V/Etot (kcat) 20.1 ± 2.7 min^-1 | Km 116 ± 16 uM | V/Km (kcat/Km) 2890 M^-1 s^-1

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row H121Q, substrate Cysteine: V/Etot = 20.1 ± 2.7 min^-1 (the turnover cell, kcat); Km = 116 ± 16 uM; printed V/Km = 2890 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row H121Q, substrate Cysteine


column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row R167K, substrate Cysteine; column V/Etot (min^-1) = 1.5 ± 0.2; column Km (uM) = 1950 ± 180; column V/Km (M^-1·s^-1) = 12.8. captured primary segment: Table 2 | SynGCL mutant R167K | substrate Cysteine* (asterisk: reaction performed at sub-saturating 50 mM glutamate) | V/Etot (kcat) 1.5 ± 0.2 min^-1 | Km 1950 ± 180 uM | V/Km (kcat/Km) 12.8 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 2 V/Etot cell 1.5 min^-1; the printed turnover column is per MINUTE, so 1.5 / 60 = 0.025 s^(-1); the exported value is 0.025 s^(-1). Km: printed Table 2 Km cell 1950 uM; 1 uM is 1/1000 mM, so 1950 / 1000 = 1.95 mM; the exported value is 1.95 mM. kcat/Km: printed Table 2 V/Km cell 12.8 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 12.8 / 1000 = 0.0128 s^(-1)*mM^(-1); the exported value is 0.012820512820512822 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.025 / 1.95 = 0.012820512820512822 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row R167K, substrate Cysteine: V/Etot = 1.5 ± 0.2 min^-1 (the turnover cell, kcat); Km = 1950 ± 180 uM; printed V/Km = 12.8 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row R167K, substrate Cysteine


column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row R248K, substrate Cysteine; column V/Etot (min^-1) = 0.6 ± 0.1; column Km (uM) = 857 ± 10; column V/Km (M^-1·s^-1) = 11.7. captured primary segment: Table 2 | SynGCL mutant R248K | substrate Cysteine | V/Etot (kcat) 0.6 ± 0.1 min^-1 | Km 857 ± 10 uM | V/Km (kcat/Km) 11.7 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 2 V/Etot cell 0.6 min^-1; the printed turnover column is per MINUTE, so 0.6 / 60 = 0.01 s^(-1); the exported value is 0.01 s^(-1). Km: printed Table 2 Km cell 857 uM; 1 uM is 1/1000 mM, so 857 / 1000 = 0.857 mM; the exported value is 0.857 mM. kcat/Km: printed Table 2 V/Km cell 11.7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 11.7 / 1000 = 0.0117 s^(-1)*mM^(-1); the exported value is 0.011668611435239206 s^(-1)*mM^(-1). Quotient disclosure for this row: 0.01 / 0.857 = 0.011668611435239206 s^-1 mM^-1.

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row R248K, substrate Cysteine: V/Etot = 0.6 ± 0.1 min^-1 (the turnover cell, kcat); Km = 857 ± 10 uM; printed V/Km = 11.7 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row R248K, substrate Cysteine


column_label: Table 2 (Steady-state kinetic parameters of mutant SynGCL), printed column heads Mutant | Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. mutant row T117S, substrate Cysteine; column V/Etot (min^-1) = 8.0 ± 1.3; column Km (uM) = 186 ± 6.1; column V/Km (M^-1·s^-1) = 717. captured primary segment: Table 2 | SynGCL mutant T117S | substrate Cysteine | V/Etot (kcat) 8.0 ± 1.3 min^-1 | Km 186 ± 6.1 uM | V/Km (kcat/Km) 717 M^-1 s^-1

raw_value_unit_evidence: Journal page 67, Table 2 (Steady-state kinetic parameters of mutant SynGCL), mutant row T117S, substrate Cysteine: V/Etot = 8.0 ± 1.3 min^-1 (the turnover cell, kcat); Km = 186 ± 6.1 uM; printed V/Km = 717 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 2, mutant row T117S, substrate Cysteine


column_label: Table 1 (Steady-state kinetic parameters of SynGCL), printed column heads Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 66, PDF page 4. substrate row Cysteine (wild-type SynGCL); column V/Etot (min^-1) = 25.2 ± 1.7; column Km (uM) = 59 ± 0.5; column V/Km (M^-1·s^-1) = 7120. captured primary segment: Table 1 | wild-type SynGCL | substrate Cysteine | V/Etot (kcat) 25.2 ± 1.7 min^-1 | Km 59 ± 0.5 uM | V/Km (kcat/Km) 7120 M^-1 s^-1

raw_value_unit_evidence: Journal page 66, Table 1 (Steady-state kinetic parameters of SynGCL), substrate row Cysteine (wild-type SynGCL): V/Etot = 25.2 ± 1.7 min^-1 (the turnover cell, kcat); Km = 59 ± 0.5 uM; printed V/Km = 7120 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km).

row_label: Table 1, substrate row Cysteine (wild-type SynGCL)


substrate_name: L-Cys

column_label: The abstract reports apparent Km values for L-aminobutyrate, L-cysteine and L-glutamate of 0.31, 0.41 and 0.94 mM, respectively.

raw_value_unit_evidence: Km raw_value=0.41 mM raw_unit=mM

row_label: Prose segment: L-cysteine Km

table_label: PubMed PMID 8538700 abstract

substrate: L-Cys


substrate_name: L-Glu

raw_value_unit_evidence: Km raw_value=0.94 mM raw_unit=mM

row_label: Prose segment: L-glutamate Km

substrate: L-Glu


assay_conditions_summary: pH 8; cofactor ATP

column_label: Printed page 61, Section 3.5 states that the apparent Km values for L-aminobutyrate, L-cysteine, L-glutamate and ATP were 0.31 +/- 0.07, 0.41, 0.94 +/- 0.05 and 1.41 +/- 0.01 mM, respectively; ATP n=3.

normalized_value_unit_evidence: ATP apparent Km normalized_value=1.41 normalized_unit=mM

raw_value_unit_evidence: ATP apparent Km raw_value=1.41 +/- 0.01 raw_unit=mM (n=3)

row_label: Apparent Km prose sequence: L-aminobutyrate, L-cysteine, L-glutamate and ATP

table_label: Primary article printed page 61, Section 3.5 Kinetic properties of the enzyme


assay_conditions_summary: pH 8.2; 298.15 K; cofactor ATP

raw_value_unit_evidence: - Pm gamma-ECL / ATP: Km 250 +/- 24 uM; kcat 22.4 +/- 2.6 s^-1; kcat/Km 8.96 x 10^4 s^-1 M^-1. The central cells are retained with their printed uncertainty and units.

row_label: Pm gamma-ECL / ATP

table_label: Table 2. Steady-state kinetic constants of the individually assayed gamma-ECL and GS activities of the bifunctional GshF glutathione synthetase of P. multocida (Pm)


assay_conditions_summary: pH 8.2; 298.15 K; cofactor NADH

raw_value_unit_evidence: - Pm gamma-ECL / L-Cys: Km 220 +/- 32 uM; kcat 25.3 +/- 2.3 s^-1; kcat/Km 1.15 x 10^5 s^-1 M^-1. The central cells are retained with their printed uncertainty and units.

row_label: Pm gamma-ECL / L-Cys


substrate_name: L-Glutamate

raw_value_unit_evidence: - Pm gamma-ECL / L-Glu: Km 5,300 +/- 330 uM; kcat 24.3 +/- 1.3 s^-1; kcat/Km 4.58 x 10^3 s^-1 M^-1. The central cells are retained with their printed uncertainty and units.

row_label: Pm gamma-ECL / L-Glu

substrate: L-Glutamate


substrate_name: ATP

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

substrate: ATP


substrate_name: glutamate

column_label: Abstract reports recombinant AtGCL forms gamma-glutamylcysteine from glutamate with Km = 9.1 mm.

raw_value_unit_evidence: Km raw_value=9.1 mm raw_unit=mM

row_label: Recombinant AtGCL / glutamate

table_label: PubMed XML abstract PMID 15180996

substrate: glutamate


substrate_name: cysteine

substrate: cysteine


column_label: PubMed abstract maps L-glutamate/L-cysteine/L-gamma-aminobutyrate/ATP to 1.8/0.1/1.3/0.4 mM respectively

normalized_value_unit_evidence: km=1.8 mM

raw_value_unit_evidence: Km 1.8 mM for L-glutamate

row_label: Km values respectively list: L-glutamate, L-cysteine, L-gamma-aminobutyrate, ATP


substrate_name: L-cysteine

normalized_value_unit_evidence: km=0.1 mM

raw_value_unit_evidence: Km 0.1 mM for L-cysteine

substrate: L-cysteine


normalized_value_unit_evidence: km=0.4 mM

raw_value_unit_evidence: Km 0.4 mM for ATP


column_label: Primary-paper abstract reports ATP apparent Km as 0.07 mM.

raw_value_unit_evidence: ATP apparent Km 0.07 mM

row_label: ATP apparent Km statement


column_label: Primary-paper abstract reports L-Glu apparent Km as 0.24 mM.

raw_value_unit_evidence: L-Glu apparent Km 0.24 mM

row_label: L-Glu apparent Km statement


column_label: Primary-paper abstract reports L-Cys apparent Km as 0.69 mM.

raw_value_unit_evidence: L-Cys apparent Km 0.69 mM

row_label: L-Cys apparent Km statement


organism: Schizosaccharomyces pombe

substrate_name: gamma-Glu-Cys

substrate: gamma-Glu-Cys


substrate_name: Gly

substrate: Gly


organism: Escherichia coli (strain K12)

substrate_name: UDP-N-acetyl-alpha-D-muramate

substrate: UDP-N-acetyl-alpha-D-muramate


substrate_name: L-alanine

column_label: PubMed abstract reports L-alanine Km = 20 microM; this normalizes to 0.02 mM.

raw_value_unit_evidence: Km raw_value=20 microM raw_unit=microM

row_label: Prose segment: L-alanine Km

table_label: PubMed PMID 7601127 abstract

substrate: L-alanine


column_label: PubMed abstract reports ATP/Mg2+ Km = 450 microM; this normalizes to 0.45 mM.

raw_value_unit_evidence: Km raw_value=450 microM raw_unit=microM

row_label: Prose segment: ATP/Mg2+ Km


organism: Staphylococcus aureus

substrate_name: L-lysine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D406A to reconstruct the assayed variant sequence.

substrate: L-lysine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P408A to reconstruct the assayed variant sequence.


organism: Staphylococcus aureus (strain NCTC 8325 / PS 47)

substrate_name: UDP-MurNAc

column_label: Table 2; row Km, UM / UDP-MurNAc; column MurC Sa Km (mM); raw 0.28 mM; normalized 0.28 mM.

raw_value_unit_evidence: Table 2 row Km, UM / UDP-MurNAc gives MurC Sa Km 0.28 mM.

row_label: Km, UM / UDP-MurNAc (MurC Sa; UniProt Q2FXJ0)

table_label: PMID 20659527, Table 2: kinetic parameters of MurC Sa ligase from Staphylococcus aureus

substrate: UDP-MurNAc


column_label: Table 2; row Km, L-Ala; column MurC Sa Km (mM); raw 0.44 mM; normalized 0.44 mM.

raw_value_unit_evidence: Table 2 row Km, L-Ala gives MurC Sa Km 0.44 mM.

row_label: Km, L-Ala (MurC Sa; UniProt Q2FXJ0)


column_label: Table 2; row Km, ATP; column MurC Sa Km (mM); raw 2.0 mM; normalized 2.0 mM.

normalized_value_unit_evidence: Km 2.0 mM.

raw_value_unit_evidence: Table 2 row Km, ATP gives MurC Sa Km 2.0 mM.

row_label: Km, ATP (MurC Sa; UniProt Q2FXJ0)


column_label: Table 3 (Steady-state kinetic parameters of SynGS), printed column heads Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. substrate row ATP (wild-type SynGS); column V/Etot (min^-1) = 324 ± 18; column Km (uM) = 136 ± 12; column V/Km (M^-1·s^-1) = 39 710. captured primary segment: Table 3 | wild-type SynGS | substrate ATP | V/Etot (kcat) 324 ± 18 min^-1 | Km 136 ± 12 uM | V/Km (kcat/Km) 39 710 M^-1 s^-1 (plain numeral 39710 M^-1 s^-1)

raw_value_unit_evidence: Journal page 67, Table 3 (Steady-state kinetic parameters of SynGS), substrate row ATP (wild-type SynGS): V/Etot = 324 ± 18 min^-1 (the turnover cell, kcat); Km = 136 ± 12 uM; printed V/Km = 39 710 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km, printed with a thousands space; plain numeral 39710).

row_label: Table 3, substrate row ATP (wild-type SynGS)


substrate_name: gamma-L-glutamyl-L-cysteine

column_label: Table 3 (Steady-state kinetic parameters of SynGS), printed column heads Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. substrate row γ-Glutamylcysteine (wild-type SynGS); column V/Etot (min^-1) = 277 ± 29; column Km (uM) = 99 ± 14; column V/Km (M^-1·s^-1) = 46 630. captured primary segment: Table 3 | wild-type SynGS | substrate γ-Glutamylcysteine | V/Etot (kcat) 277 ± 29 min^-1 | Km 99 ± 14 uM | V/Km (kcat/Km) 46 630 M^-1 s^-1 (plain numeral 46630 M^-1 s^-1)

raw_value_unit_evidence: Journal page 67, Table 3 (Steady-state kinetic parameters of SynGS), substrate row γ-Glutamylcysteine (wild-type SynGS): V/Etot = 277 ± 29 min^-1 (the turnover cell, kcat); Km = 99 ± 14 uM; printed V/Km = 46 630 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km, printed with a thousands space; plain numeral 46630).

row_label: Table 3, substrate row γ-Glutamylcysteine (wild-type SynGS)

substrate: gamma-L-glutamyl-L-cysteine


substrate_name: glycine

column_label: Table 3 (Steady-state kinetic parameters of SynGS), printed column heads Substrate | V/Etot (min^-1) | Km (uM) | V/Km (M^-1 s^-1); journal page 67, PDF page 5. substrate row Glycine (wild-type SynGS); column V/Etot (min^-1) = 253 ± 35; column Km (uM) = 407 ± 90; column V/Km (M^-1·s^-1) = 10 360. captured primary segment: Table 3 | wild-type SynGS | substrate Glycine | V/Etot (kcat) 253 ± 35 min^-1 | Km 407 ± 90 uM | V/Km (kcat/Km) 10 360 M^-1 s^-1 (plain numeral 10360 M^-1 s^-1)

raw_value_unit_evidence: Journal page 67, Table 3 (Steady-state kinetic parameters of SynGS), substrate row Glycine (wild-type SynGS): V/Etot = 253 ± 35 min^-1 (the turnover cell, kcat); Km = 407 ± 90 uM; printed V/Km = 10 360 M^-1 s^-1 (the catalytic-efficiency cell, kcat/Km, printed with a thousands space; plain numeral 10360).

row_label: Table 3, substrate row Glycine (wild-type SynGS)

substrate: glycine


substrate_name: magnesium

smiles: [Mg]

substrate: magnesium


substrate_name: manganese

smiles: [Mn]

substrate: manganese


substrate_name: Asp

sequence_variant_note: Sequence identity was resolved, but no explicit wild-type or mutant call was captured.

substrate: Asp


organism: Brucella abortus

substrate_name: beta-Alanine

column_label: ScienceDirect abstract reports the Michaelis constant for beta-alanine as 4 x 10^-5 M.

raw_value_unit_evidence: Km raw_value=4 x 10^-5 raw_unit=M

row_label: cell-free sonic extracts of Brucella abortus strain 19 / beta-alanine

table_label: ScienceDirect article abstract PMID 14377603

substrate: beta-Alanine


substrate_name: (R)-pantoate

substrate: (R)-pantoate


substrate_name: ATP

column_label: Table 2 Pm row under variable substrates for GS activity, ATP column: Km 530 +/- 65 uM, kcat 26.5 +/- 3.0 s^-1, kcat/km 5.00 x 10^4 s^-1 M^-1; footnote a apparent values.

raw_value_unit_evidence: ATP column for GS activity: Km 530 +/- 65 uM; kcat 26.5 +/- 3.0 s^-1; kcat/km 5.00 x 10^4 s^-1 M^-1; apparent values.

row_label: GS activity variable substrate ATP

table_label: Table 2

substrate: ATP


substrate_name: gamma-L-Glutamyl-L-cysteine

column_label: Table 2 Pm row under variable substrates for GS activity, gamma-Glu-Cys column: Km 90 +/- 9 uM, kcat 26.9 +/- 2.6 s^-1, kcat/km 2.74 x 10^5 s^-1 M^-1; footnote a apparent values.

raw_value_unit_evidence: gamma-Glu-Cys column: Km 90 +/- 9 uM; kcat 26.9 +/- 2.6 s^-1; kcat/km 2.74 x 10^5 s^-1 M^-1; apparent values.

row_label: GS activity variable substrate gamma-Glu-Cys

substrate: gamma-L-Glutamyl-L-cysteine


column_label: Table 2 Pm row under variable substrates for GS activity, Gly column: Km 81,000 +/- 12,300 uM, kcat 36.3 +/- 5.2 s^-1, kcat/km 4.48 x 10^2 s^-1 M^-1; footnote a apparent values.

row_label: GS activity variable substrate Gly


substrate_name: L-alpha-aminobutyrate

substrate: L-alpha-aminobutyrate


organism: Thermus thermophilus

substrate_name: D-Alanine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S293D to reconstruct the assayed variant sequence.

substrate: D-Alanine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S293E to reconstruct the assayed variant sequence.


organism: Mycobacterium leprae


organism: Pseudoalteromonas haloplanktis

assay_conditions_summary: pH 7.8; 283.15 K; cofactor ATP


proof_lines:
Raw SKiD Env: Temp=37°C, pH=8.6
Raw SKiD Env: Temp=37°C, pH=-----


organism: Homo sapiens

substrate_name: CTP

column_label: Table 1 rows KmA and kcat under Human (A = CTP); Table 2 row CTP column Km; no printed kcat/Km column

raw_value_unit_evidence: Table 1 Human (A = CTP): KmA 265 +/- 20 uM and kcat 0.53 +/- 0.02 s^-1; Table 2 CTP: Km 265 +/- 20 uM

row_label: Table 1 column Human (A = CTP); Table 2 row CTP

table_label: ScienceDirect Table 1; ScienceDirect Table 2

substrate: CTP


assay_conditions_summary: pH 7.6; cofactor ATP

column_label: Table 1 rows KmA and kcat under Human (A = ATP); Table 2 row ATP column Km; no printed kcat/Km column

raw_value_unit_evidence: Table 1 Human (A = ATP): KmA 269 +/- 14 uM and kcat 0.56 +/- 0.01 s^-1; Table 2 ATP: Km 269 +/- 14 uM

row_label: Table 1 column Human (A = ATP); Table 2 row ATP


substrate_name: L-ornithine

smiles: C(CC(C(=O)O)N)CN

substrate: L-ornithine


organism: Streptococcus agalactiae

sequence_variant_note: Mutation context is present, but no sequence was resolved for this record.

mutation_type: truncation

assay_conditions_summary: pH 8.4; 310.15 K; cofactor ATP


substrate_name: L-Cys

smiles: C(C(C(=O)O)N)S

substrate: L-Cys


substrate_name: L-Glu

smiles: C(CC(=O)O)C(C(=O)O)N

substrate: L-Glu


substrate_name: Unknown

substrate: Unknown


sequence_variant_note: No sequence was resolved for this record, so variant-aware sequence handling could not be applied.


assay_conditions_summary: pH 8.4; buffer 150 mM Tris-HCl; cofactor ATP

proof_lines: mutant enzyme D448A, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA


substrate_name: gamma-Glu-L-Cys

assay_conditions_summary: pH 8.4; buffer 150 mM Tris-HCl

proof_lines: wild type enzyme, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA

substrate: gamma-Glu-L-Cys


substrate_name: Gly

smiles: C(C(=O)O)N

substrate: Gly


proof_lines: mutant enzyme K526A, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA


proof_lines: mutant enzyme K489A, in 150 mM Tris-HCl buffer, pH 8.4, 100 mM KCl, 40 mM MgCl2, 0.3 mM EDTA


organism: Escherichia coli

assay_conditions_summary: 298.15 K; cofactor ATP


smiles: CC(C)(COP(=O)(O)O)C(C(=O)NCCC(=O)O)O

assay_conditions_summary: pH 7.6; 310.15 K; cofactor ATP

proof_lines:
co-substrate ATP, pH 7.6, 37°C
co-substrate CTP, pH 7.6, 37°C


organism: Arabidopsis thaliana

proof_lines: wild type enzyme, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kinase


organism: Myxococcus xanthus

assay_conditions_summary: pH 7; 310.15 K; cofactor ATP


substrate_name: gamma-L-glutamyl-L-cysteine

smiles: C(CC(=O)NC(CS)C(=O)O)C(C(=O)O)N

substrate: gamma-L-glutamyl-L-cysteine


substrate_name: glycine

substrate: glycine


assay_conditions_summary: pH 9; 310.15 K; cofactor ATP

proof_lines: noncompetitive inhibition with respect to glycine, at pH 9.0 and 37°C

proof_lines: noncompetitive inhibition with respect to ATP, at pH 9.0 and 37°C

proof_lines: competitive inhibition with respect to gamma-L-glutamyl-L-cysteine, at pH 9.0 and 37°C


assay_conditions_summary: pH 7


assay_conditions_summary: pH 7; cofactor ATP


proof_lines: wild type enzyme, at pH 7.0, temperature not specified in the publication


substrate_name: L-cysteine

substrate: L-cysteine


substrate_name: L-glutamate

substrate: L-glutamate


proof_lines: competitive inhibition with respect to L-Glu, at pH 7.0 and 37°C

proof_lines: noncompetitive inhibition with respect to ATP, at pH 7.0 and 37°C


proof_lines: pH 8.0, 25°C, wild-type enzyme, in presence of DTT


proof_lines: pH 8.0, 25°C, mutant C106S,C164S,C205S,C223S,C357S,C433S,C439S, in presence of DTT


assay_conditions_summary: pH 8; 298.15 K; cofactor ATP


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

proof_lines: mutant enzyme R132K, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kin


assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP


proof_lines: mutant enzyme E371Q, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kin


proof_lines: mutant enzyme Q226A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kin


proof_lines: mutant enzyme E220A, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kin


proof_lines: mutant enzyme Q226N, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kin


proof_lines: mutant enzyme E220Q, at 25°C in 100 mM HEPES (pH 7.5), 150 mM NaCl, 20 mM MgCl2, 2.5 mM gamma-glutamylcysteine, 10 mM glycine, 2.5 mM disodium ATP, 2 mM sodium phosphoenolpyruvate, 0.2 mM NADH, 5 units of type III rabbit muscle pyruvate kin


assay_conditions_summary: cofactor ATP