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'


enzyme_display_name: glutamate--cysteine ligase

organism: Trypanosoma brucei

substrate_name: L-glutamate

source_db: brenda

verification_status: corrected

ki_display: Not reported

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

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

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

mutation_type: substitution

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

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'

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

data_origin: experimental

enzyme: glutamate--cysteine ligase

substrate: L-glutamate

status: corrected

source: brenda


verification_status: verified

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'

status: verified


mutation_signature: Unknown

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

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 Mg2+


substrate_name: ATP

kcat_display: Not reported

kcat_over_km_display: Not reported

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.


substrate_name: L-alpha-aminobutyrate

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

substrate: L-alpha-aminobutyrate


enzyme_display_name: glutathione synthase

organism: Synechocystis sp.

substrate_name: glycine

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

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)

enzyme: glutathione synthase

substrate: glycine


substrate_name: gamma-L-glutamyl-L-cysteine

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

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)

substrate: gamma-L-glutamyl-L-cysteine


assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

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)

source_db: uniprot

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)

source: uniprot


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.

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

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


substrate_name: L-Glu

substrate: L-Glu


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

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

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


enzyme_display_name: D-alanine--D-alanine ligase

organism: Enterococcus faecalis

substrate_name: D-Alanine; ATP

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

enzyme: D-alanine--D-alanine ligase

substrate: D-Alanine; ATP


organism: Enterococcus faecium

substrate_name: ATP; D-Alanine

substrate: ATP; D-Alanine


organism: Escherichia coli


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

km_display: Not reported

ki_unit: mM

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

source_db: skid

source_license: CC BY-NC-ND 4.0

substrate: L-cysteine

source: skid


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: 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

sequence_source: multiple


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

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

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

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


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


organism: Pseudoalteromonas haloplanktis


organism: Synechocystis sp.

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


assay_conditions_summary: 310.15 K; cofactor ATP

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


organism: Trypanosoma brucei

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: Homo sapiens

verification_status: unverified

status: unverified


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

smiles: CCN

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


organism: Escherichia coli

substrate_name: D-Alanine

source_db: oed

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

source: oed


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

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)


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 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


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

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


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

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)

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)


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

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 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

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)


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

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

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


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

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

source_databases_merged: skid uniprot


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

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


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


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


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

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


substrate_name: beta-Alanine

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

substrate: beta-Alanine


substrate_name: L-Ile

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

substrate: L-Ile


substrate_name: L-Vinylglycine

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

substrate: L-Vinylglycine


substrate_name: DL-propargylglycine

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

substrate: DL-propargylglycine


substrate_name: L-Val

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

substrate: L-Val


substrate_name: L-Thr

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

substrate: L-Thr


substrate_name: 2-amino-n-butyric acid

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

substrate: 2-amino-n-butyric acid


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

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


substrate_name: benzyl L-alaninate

substrate: benzyl L-alaninate


substrate_name: methyl L-alaninate

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

substrate: methyl L-alaninate


substrate_name: ethyl L-alaninate

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

substrate: ethyl L-alaninate


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


substrate_name: ATP

substrate: ATP


substrate_name: D-Ala

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

proof_lines: N-terminal Ala, mutant enzyme E15Q, mutant enzyme Y216K

substrate: D-Ala


proof_lines:
N-terminal Ala, mutant enzyme L282R
C-terminal Ala, mutant enzyme L282R


proof_lines:
N-terminal Ala, mutant enzyme H63Q
C-terminal Ala, mutant enzyme H63Q


substrate_name: D-Phe

substrate: D-Phe


substrate_name: D-Met

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

substrate: D-Met


substrate_name: D-norleucine

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

substrate: D-norleucine


proof_lines: C-terminal Ala, mutant enzyme K144A, reaction with 5 mM ATP

proof_lines: C-terminal Ala, mutant enzyme K144A, reaction with 15 mM ATP


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


proof_lines: C-terminal Ala, mutant enzyme K144T, reaction with 5 mM ATP

proof_lines: C-terminal Ala, mutant enzyme K144T, reaction with 15 mM ATP


organism: Mus musculus


substrate_name: L-threonine

substrate: L-threonine


substrate_name: L-alanine

substrate: L-alanine


substrate_name: L-serine

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

substrate: L-serine


substrate_name: L-methionine

substrate: L-methionine


substrate_name: glycine

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

substrate: glycine


substrate_name: L-valine

substrate: L-valine


substrate_name: L-taurine

substrate: L-taurine


substrate_name: gamma-L-Glu-L-Cys

proof_lines: mutant E144K and mutant N146D, pH 8.2, 37°C

substrate: gamma-L-Glu-L-Cys


proof_lines: wild-type, 37°C, pH not specified in the publication


assay_conditions_summary: pH 8.2; 310.15 K; cofactor ATP


enzyme_display_name: ribose-5-phosphate isomerase

substrate_name: D-ribose 5-phosphate

enzyme: ribose-5-phosphate isomerase

substrate: D-ribose 5-phosphate


substrate_name: L-cysteine

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

proof_lines: recombinant mutant C553G holoenzyme, pH 8.0, 37°C

substrate: L-cysteine


substrate_name: L-Glu

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

substrate: L-Glu


proof_lines: recombinant wild-type holoenzyme, pH 8.0, 37°C


substrate_name: gamma-Glu-Cys

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

substrate: gamma-Glu-Cys


substrate_name: L-Cys

proof_lines: mutant R127C, catalytic subunit, pH 8.0, 37°C

proof_lines: mutant R127C, CGL holoenzyme, pH 8.0, 37°C

substrate: L-Cys


proof_lines: wild-type, catalytic subunit, pH 8.0, 37°C


proof_lines: mutant H370L, CGL holoenzyme, pH 8.0, 37°C


proof_lines: mutant P414L, catalytic subunit, pH 8.0, 37°C


substrate_name: ATP

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

substrate: ATP


substrate_name: Gly

proof_lines: mutant G370V, 37°C, pH not specified in the publication

substrate: Gly


proof_lines: mutant G369V, 37°C, pH not specified in the publication


proof_lines: mutant G371V, 37°C, pH not specified in the publication


substrate_name: gamma-L-Glu-aminobutanoate

substrate: gamma-L-Glu-aminobutanoate


assay_conditions_summary: 310.15 K; cofactor ATP


organism: Actinobacillus pleuropneumoniae

assay_conditions_summary: pH 8.5; 313.15 K; cofactor ATP

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


substrate_name: L-glutamate

substrate: L-glutamate


substrate_name: Unknown

substrate: Unknown


substrate_name: gamma-L-glutamyl-L-cysteine

substrate: gamma-L-glutamyl-L-cysteine


substrate_name: UDP-N-acetylmuramate

substrate: UDP-N-acetylmuramate


substrate_name: L-alanine

substrate: L-alanine


organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 8; cofactor ATP


assay_conditions_summary: pH 8


organism: Pasteurella multocida

assay_conditions_summary: pH 8.2; 298.15 K; cofactor ATP


assay_conditions_summary: pH 8.2; 298.15 K; buffer 200 mM; cofactor ATP

proof_lines:
pH 8.2, 25°C
inTris-HCl buffer (200 mM, pH 8.2)


substrate_name: gamma-Glu-L-Cys

substrate: gamma-Glu-L-Cys


substrate_name: glycine

substrate: glycine


organism: Streptococcus thermophilus


substrate_name: L-alpha-aminobutyrate

substrate: L-alpha-aminobutyrate


organism: Escherichia coli


proof_lines:
mutant with a nicked loop
loopless mutant


proof_lines:
loopless mutant
mutant with a nicked loop


organism: Enterococcus faecalis

substrate_name: D-Ala

proof_lines: C-terminal Ala, reaction with D-Ala + ATP, VanB

substrate: D-Ala


smiles: CCCC(C(=O)[O-])O


substrate_name: D-lactate

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

substrate: D-lactate


organism: Staphylococcus aureus

substrate_name: L-lysine

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

substrate: L-lysine


proof_lines: pH 8.6, 37°C, recombinant wild-type enzyme


proof_lines: above, pH 8.6, 37°C, recombinant mutant A409R


proof_lines: above, pH.6, 37°C, recombinant mutant E460A


substrate_name: (R)-pantoate

substrate: (R)-pantoate


substrate_name: beta-Alanine

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

substrate: beta-Alanine


enzyme_display_name: alanine racemase

organism: Streptomyces lavendulae

enzyme: alanine racemase


substrate_name: D-alanine

substrate: D-alanine


substrate_name: ATP

substrate: ATP


substrate_name: D-cycloserine

substrate: D-cycloserine


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 8.5; 310.15 K; cofactor ATP

proof_lines:
pH 8.5, 37°C, recombinant enzyme
pH 8.6


substrate_name: L-serine

substrate: L-serine


proof_lines:
at pH 7.6 and 25°C
pH 7.6


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


substrate_name: cysteine

proof_lines:
pH 7.6
at pH 7.6 and 25°C

substrate: cysteine


substrate_name: CTP

assay_conditions_summary: pH 7.6; 298.15 K; cofactor ATP

substrate: CTP


substrate_name: L-Cys

proof_lines:
strain B
strain W
strain KM

substrate: L-Cys


substrate_name: L-Glu

substrate: L-Glu


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


substrate_name: L-Ala

substrate: L-Ala


substrate_name: beta-chloro-L-Ala

assay_conditions_summary: 298.15 K; cofactor ATP

proof_lines: pH not specified in the publication, 25°C

substrate: beta-chloro-L-Ala


substrate_name: L-Ser

substrate: L-Ser


substrate_name: Gly

substrate: Gly


proof_lines:
37°C, mutant enzyme S150A, pH 6.0
37°C, mutant enzyme S150A, pH 7.5
37°C, mutant enzyme S150A, pH 9.2


proof_lines:
37°C, mutant enzyme E15Q, pH 6.0
37°C, mutant enzyme E15Q, pH 7.5
37°C, mutant enzyme E15Q, pH 9.2


proof_lines:
37°C, mutant enzyme Y216F, pH 6.0
37°C, mutant enzyme Y216F, pH 7.5
37°C, mutant enzyme Y216F, pH 9.2


proof_lines:
37°C, wild-type enzyme, pH 6.0
37°C, wild-type enzyme, pH 7.5
37°C, wild-type enzyme, pH 9.2


substrate_name: L-cysteine

proof_lines:
37°C, pH 7.2, catalytic subunit GCLC
37°C, pH 7.2, holoenzyme
at pH 8.2 and 37°C

substrate: L-cysteine


substrate_name: L-glutamate

substrate: L-glutamate


assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP

proof_lines:
37°C, pH 7.2,catalytic subunit GCLC
37°C, pH 7.2, holoenzyme
37°C, pH 7.2, catalytic subunit GCLC


substrate_name: Unknown

proof_lines: Kis, 37°C, pH 7.2, catalytic subunit GCLC, versus L-glutamate

proof_lines: Kii, 37°C, pH 7.2, catalytic subunit GCLC, versus ATP

proof_lines: Kii, 37°C, pH 7.2, catalytic subunit GCLC, versus L-glutamate

substrate: Unknown


organism: Nostoc sp.

assay_conditions_summary: pH 8.4; 298.15 K; cofactor ATP


organism: Plasmodium berghei


assay_conditions_summary: pH 8.2; cofactor ATP


organism: [Candida] boidinii


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

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


assay_conditions_summary: pH 8.6; 310.15 K; cofactor ATP


substrate_name: L-Lys

substrate: L-Lys


substrate_name: gamma-L-Glu-L-Cys

substrate: gamma-L-Glu-L-Cys


organism: Agrobacterium tumefaciens


substrate_name: ATP

substrate: ATP


organism: Thermus thermophilus

substrate_name: D-alanine

substrate: D-alanine


smiles: N


organism: Arabidopsis thaliana

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP


substrate_name: gamma-Glu-L-Cys

proof_lines: 25°C, pH 7.5, with glycine as varied substrate

proof_lines: 25°C, pH 7.5, with ATP as varied substrate

substrate: gamma-Glu-L-Cys


organism: Chlamydia trachomatis

substrate_name: L-alanine

substrate: L-alanine


substrate_name: L-serine

substrate: L-serine


substrate_name: glycine

substrate: glycine


organism: Brassica juncea


assay_conditions_summary: cofactor ATP


substrate_name: cysteine

mutation_type: deletion

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

substrate: cysteine


substrate_name: glutamate

substrate: glutamate


proof_lines: pH 7.0, 25°C, versus glutamate, mutant DELTA85

proof_lines: pH 7.0, 25°C, versus cysteine, mutant DELTA85


substrate_name: beta-Alanine

substrate: beta-Alanine


substrate_name: (R)-pantoate

substrate: (R)-pantoate


substrate_name: D-cycloserine

substrate: D-cycloserine


organism: Glycine max

proof_lines: pH 8.0, 30°C, with beta-Ala as cosubstrate


substrate_name: beta-Ala

substrate: beta-Ala


organism: Homo sapiens

substrate_name: gamma-glutamyl-alpha-aminobutyrate

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

substrate: gamma-glutamyl-alpha-aminobutyrate


assay_conditions_summary: pH 8.2; 310.15 K; cofactor ATP


substrate_name: Gly

substrate: Gly


substrate_name: D-pantoate

assay_conditions_summary: pH 7.8; 298.15 K; cofactor ATP

proof_lines: pH and temperature not specified in the publication

substrate: D-pantoate


substrate_name: L-cysteine

proof_lines:
pH 8.2, 37°C
holoenzyme
heavy subunit

substrate: L-cysteine


proof_lines:
pH 8.2, 37°C
holoenzyme


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


organism: Rattus norvegicus

substrate_name: gamma-L-Glu-L-alpha-aminobutyrate

substrate: gamma-L-Glu-L-alpha-aminobutyrate


substrate_name: ATP

substrate: ATP


substrate_name: CTP

substrate: CTP


substrate_name: L-Cys

proof_lines:
pH 7.6, 37°C
substrate CTP, pH 7.6, 37°C

substrate: L-Cys


organism: Proteus mirabilis


substrate_name: L-Glu

substrate: L-Glu


organism: Streptococcus pyogenes

assay_conditions_summary: 296.15 K; cofactor ATP


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

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


substrate_name: L-Lys

substrate: L-Lys


organism: Saccharomyces cerevisiae

proof_lines: reaction with Glu-alpha-aminobutyrate + hydroxylamine


organism: Staphylococcus aureus

substrate_name: UDP-N-acetylmuramate

substrate: UDP-N-acetylmuramate


substrate_name: L-Ala

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

substrate: L-Ala


organism: Xanthomonas campestris


substrate_name: L-glutamate

substrate: L-glutamate


organism: Zea mays

substrate_name: gamma-Glu-L-Cys

substrate: gamma-Glu-L-Cys


organism: Triticum aestivum

substrate_name: glycine

substrate: glycine


proof_lines:
pH 8.0, 30°C, with Gly as cosubstrate
pH 8.0, 30°C


substrate_name: beta-Ala

substrate: beta-Ala


organism: Bacillus thuringiensis

substrate_name: (R)-pantoate

substrate: (R)-pantoate


substrate_name: beta-Alanine

substrate: beta-Alanine


organism: Acinetobacter baumannii

substrate_name: D-alanine

proof_lines:
pH 7.8, 45°C
pH 7.8, 45°C, first D-Ala
pH 7.8, 45°C, second D-Ala

substrate: D-alanine


assay_conditions_summary: pH 7.8; 318.15 K; cofactor ATP


organism: Escherichia coli


substrate_name: Gly

substrate: Gly


substrate_name: gamma-Glu-Cys

substrate: gamma-Glu-Cys


organism: Bacillus subtilis


organism: Corynebacterium glutamicum


organism: Helicobacter pylori


substrate_name: ATP

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

substrate: ATP


enzyme_display_name: sulfoquinovose mutarotase

organism: Herbaspirillum seropedicae

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

enzyme: sulfoquinovose mutarotase


organism: Lotus japonicus


proof_lines:
25°C, pH 8.0, at 20 mM pantoate
25°C, pH 8.0, at 0.5 mM pantoate


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 8; 310.15 K; cofactor ATP

proof_lines: pH 8.0, 37°C, recombinant His-tagged enzyme


enzyme_display_name: mannose 2-epimerase

organism: Runella slithyformis

substrate_name: beta-D-mannopyranose

enzyme: mannose 2-epimerase

substrate: beta-D-mannopyranose


enzyme_display_name: D-tagatose 6-phosphate 4-epimerase

organism: Agrobacterium fabrum

substrate_name: D-tagatose 6-phosphate

source_databases_merged: brenda uniprot

enzyme: D-tagatose 6-phosphate 4-epimerase

substrate: D-tagatose 6-phosphate


enzyme_display_name: mannuronan 5-epimerase

organism: Azotobacter vinelandii

substrate_name: Unknown

enzyme: mannuronan 5-epimerase

substrate: Unknown


enzyme_display_name: tRNA pseudouridine(55) synthase

organism: Thermotoga maritima

substrate_name: tRNA uridine55

enzyme: tRNA pseudouridine(55) synthase

substrate: tRNA uridine55


enzyme_display_name: fructoselysine 3-epimerase

organism: Escherichia coli (strain K12)

substrate_name: D-fructosyl-L-lysine

enzyme: fructoselysine 3-epimerase

substrate: D-fructosyl-L-lysine


proof_lines: pH 7.5, 37°C, Escherichia coli tRNAPhe, wild-type enzyme

proof_lines: pH 7.5, 37°C, substrate: Escherichia coli tRNAPhe. wild-type enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature K19M to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, Escherichia coli tRNAPhe, mutant enzyme K19M


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature P20L to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, Escherichia coli tRNAPhe, mutant enzyme P20L


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature P20G to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, Escherichia coli tRNAPhe, mutant enzyme P20G


mutation_signature: pseudouridine synthase TruB with an 10-amino acid N-terminal truncation

sequence_variant_note: Mutation context was captured, but the signature could not be translated into an exact residue substitution safely.


organism: Nicotiana tabacum

substrate_name: L-Cys

substrate: L-Cys


organism: Lathyrus oleraceus


organism: Rattus norvegicus


substrate_name: L-alpha-aminobutyrate

substrate: L-alpha-aminobutyrate


organism: Staphylococcus aureus


organism: Thermus thermophilus

proof_lines: in the presence of 100 mM K+, at pH 7.3 and 30°C

proof_lines: in the presence of 50 mM K+, at pH 7.3 and 30°C

proof_lines: in the presence of less than 1 mM Na+, at pH 7.3 and 30°C


assay_conditions_summary: pH 7.3; 303.15 K; cofactor ATP


organism: Dyadobacter fermentans

protein_accession_database: NCBI Protein

sequence_source: GenBank: ACT96842.1

assay_conditions_summary: pH 8

column_label: Hokkaido repository PDF Table 2 row Dfer_5652 has the exact Km cell and the paper kcat/kcat/Km cells needed to explain the rounded/computed export values.

table_label: Hokkaido repository PDF Table 2: Kinetic parameters of Runsl_4512 and Dfer_5652 for D-mannose


proof_lines: co-substrate: beta-alanine, pH 8.0, 30°C


proof_lines: co-substrate: (R)-pantoate, pH 8.0, 30°C


organism: Bos taurus

substrate_name: (R)-beta-amino-iso-butyrate

substrate: (R)-beta-amino-iso-butyrate


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature C58A/C174A/C193A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, substrate: Escherichia coli tRNAPhe, mutant enzyme C58A/C174A/C193A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature C58A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, substrate: Escherichia coli tRNAPhe, mutant enzyme C58A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature C174A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, substrate: Escherichia coli tRNAPhe, mutant enzyme C174A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature C193V to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, substrate: Escherichia coli tRNAPhe, mutant enzyme C193V


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature K19R to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, Escherichia coli tRNAPhe, mutant enzyme K19R


organism: Bacillus subtilis

substrate_name: L-Ala

substrate: L-Ala


organism: Onchocerca volvulus

substrate_name: L-glutamate

substrate: L-glutamate


substrate_name: [alginate]-beta-D-mannuronate

proof_lines:
pH 6.8, 37°C
pH 6.8, 30°C, presence of 8.6 mM Ca2+
pH 6.8, 30°C, presence of 0.68 mM Ca2+

substrate: [alginate]-beta-D-mannuronate


organism: Enterococcus faecium

substrate_name: D-Ala

proof_lines:
N-terminal Ala
C-terminal Ala

substrate: D-Ala


assay_conditions_summary: pH 7.4; 298.15 K; cofactor ATP

proof_lines:
pH 7.4, 25°C, versus ATP
pH 7.4, 25°C, versus D-Ala


proof_lines:
strain W
strain KM
pH 7.5, 37°C


enzyme_display_name: Muconate cycloisomerase

organism: Rhodococcus opacus

substrate_name: cis,cis-muconate

enzyme: Muconate cycloisomerase

substrate: cis,cis-muconate


enzyme_display_name: inositol-3-phosphate synthase

organism: Cyberlindnera jadinii

substrate_name: glucose 6-phosphate

enzyme: inositol-3-phosphate synthase

substrate: glucose 6-phosphate


enzyme_display_name: Inositol-3-phosphate synthase

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: NAD (at 37 degrees Celsius and pH 7.2)

enzyme: Inositol-3-phosphate synthase

substrate: NAD (at 37 degrees Celsius and pH 7.2)


enzyme_display_name: chalcone isomerase

organism: Citrus sinensis

enzyme: chalcone isomerase


organism: Phaseolus vulgaris


enzyme_display_name: UniProt G4U3G8

organism: Deschampsia antarctica

substrate_name: isoliquiritigenin

enzyme: UniProt G4U3G8

substrate: isoliquiritigenin


substrate_name: naringenin chalcone

substrate: naringenin chalcone


enzyme_display_name: Chloromuconate cycloisomerase

organism: Delftia acidovorans

enzyme: Chloromuconate cycloisomerase


enzyme_display_name: 23S rRNA pseudouridine(2457) synthase

substrate_name: 23S rRNA uridine2457

enzyme: 23S rRNA pseudouridine(2457) synthase

substrate: 23S rRNA uridine2457


enzyme_display_name: phosphoribosylanthranilate isomerase

proof_lines:
25°C, monomeric domain PRAI[ML256-452]
pH 7.5
pH 7.5, 20°C

enzyme: phosphoribosylanthranilate isomerase


enzyme_display_name: D-alanine--D-alanine ligase

proof_lines:
ligase A
ligase B
N-terminal Ala, ligase B

enzyme: D-alanine--D-alanine ligase


enzyme_display_name: glutathione synthase

substrate_name: ATP

proof_lines:
glutathione synthetase
ATP

enzyme: glutathione synthase

substrate: ATP


substrate_name: D-pantoate

substrate: D-pantoate


organism: Cephalocereus senilis

substrate_name: liquiritigenin

substrate: liquiritigenin


proof_lines:
isoenzyme II
isoenzyme I


enzyme_display_name: muconate cycloisomerase

enzyme: muconate cycloisomerase


enzyme_display_name: D-lyxose ketol-isomerase

substrate_name: D-Lyxose

enzyme: D-lyxose ketol-isomerase

substrate: D-Lyxose


organism: Limnospira platensis

substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


organism: Synechocystis sp.

substrate_name: D-glucose 6-phosphate

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

proof_lines:
pH 7.5, recombinant refolded enzyme
pH 7.5, native enzyme

substrate: D-glucose 6-phosphate


assay_conditions_summary: pH 7.5; cofactor NAD+


organism: Gleichenia glauca


organism: Pinus ponderosa

substrate_name: D-Glucose 6-phosphate

substrate: D-Glucose 6-phosphate


organism: Physcomitrella appendiculatum


organism: Euglena gracilis


substrate_name: 1D-myo-Inositol 3-phosphate

substrate: 1D-myo-Inositol 3-phosphate


proof_lines:
chloroplastic enzyme
cytosolic enzyme from green cells
cytosolic enzyme from dark-grown cells


proof_lines: cytosolic enzyme from streptomycin-bleached cells, and chloroplastidic enzyme


organism: Cicer arietinum

proof_lines:
isozyme MIPS1
isozyme MIPS2


organism: Bacillus sp. (in: firmicutes)


organism: Arthrospira platensis


organism: Taxus baccata


organism: Rhodococcus rhodochrous


organism: Lemna gibba


organism: Eubacterium ramulus

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H33Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H33Q, at pH 6.4, temperature not specified in the publication


sequence_variant_note: Mutation signature H33E could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme H33E, at pH 6.4, temperature not specified in the publication


sequence_variant_note: Mutation signature H33A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme H33A, at pH 6.4, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y48F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y48F, at pH 6.4, temperature not specified in the publication


sequence_variant_note: Resolved sequence already matches the mutant residue(s), so it is treated as a source-provided variant sequence.

proof_lines: wild type enzyme, at pH 6.4, temperature not specified in the publication


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -6, so it is treated as a source-provided variant sequence.

proof_lines: mutant enzyme H73A, at pH 6.4, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R125A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R125A, at pH 6.4, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature R34A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.6; 298.15 K; buffer DMSO in 50 mM potassium phosphate

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row R34A, isoliquiritigenin column group; column kcat (min^-1) = 0.1 ± 0.03; column Km (uM) = 5.3 ± 7.8; column kcat/Km (M^-1 s^-1) = 314.

raw_value_unit_evidence: Table 4, enzyme row R34A, isoliquiritigenin column group: kcat = 0.1 ± 0.03 min^-1; Km = 5.3 ± 7.8 uM; printed kcat/Km = 314 M^-1 s^-1.

row_label: Table 4, row R34A, isoliquiritigenin column group

table_label: Table 4: Steady-state kinetic parameters of wild-type and mutant DaCHI1 (PLoS ONE 2018, 13(2): e0192415)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature R34M to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row R34M, isoliquiritigenin column group; column kcat (min^-1) = 0.1 ± 0.08; column Km (uM) = 24.3 ± 28.2; column kcat/Km (M^-1 s^-1) = 69.

raw_value_unit_evidence: Table 4, enzyme row R34M, isoliquiritigenin column group: kcat = 0.1 ± 0.08 min^-1; Km = 24.3 ± 28.2 uM; printed kcat/Km = 69 M^-1 s^-1.

row_label: Table 4, row R34M, isoliquiritigenin column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature K108A to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row K108A, isoliquiritigenin column group; column kcat (min^-1) = 0.2 ± 0.11; column Km (uM) = 11.2 ± 15.9; column kcat/Km (M^-1 s^-1) = 298.

raw_value_unit_evidence: Table 4, enzyme row K108A, isoliquiritigenin column group: kcat = 0.2 ± 0.11 min^-1; Km = 11.2 ± 15.9 uM; printed kcat/Km = 298 M^-1 s^-1.

row_label: Table 4, row K108A, isoliquiritigenin column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature S189A to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row S189A, isoliquiritigenin column group; column kcat (min^-1) = 0.2 ± 0.03; column Km (uM) = 18.5 ± 6.9; column kcat/Km (M^-1 s^-1) = 180.

raw_value_unit_evidence: Table 4, enzyme row S189A, isoliquiritigenin column group: kcat = 0.2 ± 0.03 min^-1; Km = 18.5 ± 6.9 uM; printed kcat/Km = 180 M^-1 s^-1.

row_label: Table 4, row S189A, isoliquiritigenin column group


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I190M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature Y116A to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row Y116A, isoliquiritigenin column group; column kcat (min^-1) = 0.4 ± 0.04; column Km (uM) = 27.6 ± 5.4; column kcat/Km (M^-1 s^-1) = 242.

raw_value_unit_evidence: Table 4, enzyme row Y116A, isoliquiritigenin column group: kcat = 0.4 ± 0.04 min^-1; Km = 27.6 ± 5.4 uM; printed kcat/Km = 242 M^-1 s^-1.

row_label: Table 4, row Y116A, isoliquiritigenin column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature M36A to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row M36A, isoliquiritigenin column group; column kcat (min^-1) = 0.5 ± 0.15; column Km (uM) = 16.4 ± 10.1; column kcat/Km (M^-1 s^-1) = 508.

raw_value_unit_evidence: Table 4, enzyme row M36A, isoliquiritigenin column group: kcat = 0.5 ± 0.15 min^-1; Km = 16.4 ± 10.1 uM; printed kcat/Km = 508 M^-1 s^-1.

row_label: Table 4, row M36A, isoliquiritigenin column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature S189T to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row S189T, isoliquiritigenin column group; column kcat (min^-1) = 1.0 ± 0.04; column Km (uM) = 10.8 ± 1.2; column kcat/Km (M^-1 s^-1) = 1543.

raw_value_unit_evidence: Table 4, enzyme row S189T, isoliquiritigenin column group: kcat = 1.0 ± 0.04 min^-1; Km = 10.8 ± 1.2 uM; printed kcat/Km = 1543 M^-1 s^-1.

row_label: Table 4, row S189T, isoliquiritigenin column group


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

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row DaCHI1, isoliquiritigenin column group; column kcat (min^-1) = 1.3 ± 0.1; column Km (uM) = 15.3 ± 1.5; column kcat/Km (M^-1 s^-1) = 1416.

raw_value_unit_evidence: Table 4, enzyme row DaCHI1, isoliquiritigenin column group: kcat = 1.3 ± 0.1 min^-1; Km = 15.3 ± 1.5 uM; printed kcat/Km = 1416 M^-1 s^-1.

row_label: Table 4, row DaCHI1, isoliquiritigenin column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature Q104E to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row Q104E, isoliquiritigenin column group; column kcat (min^-1) = 1.4 ± 0.06; column Km (uM) = 22.5 ± 2.3; column kcat/Km (M^-1 s^-1) = 1011.

raw_value_unit_evidence: Table 4, enzyme row Q104E, isoliquiritigenin column group: kcat = 1.4 ± 0.06 min^-1; Km = 22.5 ± 2.3 uM; printed kcat/Km = 1011 M^-1 s^-1.

row_label: Table 4, row Q104E, isoliquiritigenin column group


column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row S189A, naringenin chalcone column group; column kcat (min^-1) = 299 ± 15; column Km (uM) = 2.4 ± 0.6; column kcat/Km (M^-1 s^-1) = 2.08 x 10^6.

raw_value_unit_evidence: Table 4, enzyme row S189A, naringenin chalcone column group: kcat = 299 ± 15 min^-1; Km = 2.4 ± 0.6 uM; printed kcat/Km = 2.08 x 10^6 M^-1 s^-1.

row_label: Table 4, row S189A, naringenin chalcone column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature M96K to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row M96K, naringenin chalcone column group; column kcat (min^-1) = 468 ± 51; column Km (uM) = 10.5 ± 3.4; column kcat/Km (M^-1 s^-1) = 7.43 x 10^5.

raw_value_unit_evidence: Table 4, enzyme row M96K, naringenin chalcone column group: kcat = 468 ± 51 min^-1; Km = 10.5 ± 3.4 uM; printed kcat/Km = 7.43 x 10^5 M^-1 s^-1.

row_label: Table 4, row M96K, naringenin chalcone column group


column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row Y116A, naringenin chalcone column group; column kcat (min^-1) = 578 ± 68; column Km (uM) = 7.0 ± 2.8; column kcat/Km (M^-1 s^-1) = 1.38 x 10^6.

raw_value_unit_evidence: Table 4, enzyme row Y116A, naringenin chalcone column group: kcat = 578 ± 68 min^-1; Km = 7.0 ± 2.8 uM; printed kcat/Km = 1.38 x 10^6 M^-1 s^-1.

row_label: Table 4, row Y116A, naringenin chalcone column group


column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row M36A, naringenin chalcone column group; column kcat (min^-1) = 2112 ± 239; column Km (uM) = 4.8 ± 2.0; column kcat/Km (M^-1 s^-1) = 7.33 x 10^6.

raw_value_unit_evidence: Table 4, enzyme row M36A, naringenin chalcone column group: kcat = 2112 ± 239 min^-1; Km = 4.8 ± 2.0 uM; printed kcat/Km = 7.33 x 10^6 M^-1 s^-1.

row_label: Table 4, row M36A, naringenin chalcone column group


column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row K108A, naringenin chalcone column group; column kcat (min^-1) = 3416 ± 234; column Km (uM) = 4.8 ± 1.2; column kcat/Km (M^-1 s^-1) = 1.19 x 10^7.

raw_value_unit_evidence: Table 4, enzyme row K108A, naringenin chalcone column group: kcat = 3416 ± 234 min^-1; Km = 4.8 ± 1.2 uM; printed kcat/Km = 1.19 x 10^7 M^-1 s^-1.

row_label: Table 4, row K108A, naringenin chalcone column group


assay_conditions_summary: pH 7.6; buffer potassium phosphate

column_label: table label: Table 4. Steady-state kinetic parameters of wild-type and mutant DaCHI1.; row label: DaCHI1; column label: the Naringenin chalcone kcat (min-1) cell and the Naringenin chalcone Km (uM) cell of this one wild-type row; no cell is taken from the Isoliquiritigenin column group of this row, from any mutant row, or from any other table; raw value: kcat 7819 plus-minus 825 min-1, Km 8.5 plus-minus 3.1 uM; raw unit: min-1 for kcat, uM for Km; normalized value: kcat 130.3 s^-1, Km 0.0085 mM, kcat/Km 15329.411764705883 s^-1 mM^-1; normalized unit: s^-1, mM, s^-1 mM^-1; condition label: Table 4 footnote: Km and kcat were calculated using the Michaelis-Menten equation; reactions were performed in potassium phosphate buffer (pH 7.6) as described in Material and Methods; all Km and kcat values are expressed as the mean plus-minus standard deviation of three parallel experiments. Enzymatic activity assay (Materials and Methods, Block RVM0009-METHODS-VERBATIM): the standard reaction was carried out at 25 C using 50 uM substrate in DMSO, 50 mM potassium phosphate buffer (pH 7.6) containing 1 mg bovine serum albumin. The export row carries pH 7.6 and no stored temperature.

normalized_value_unit_evidence: metric: kcat; raw value: 7819 ± 825; raw unit: min–1; normalized value: 130.3 s^-1; normalized unit: s^-1; metric: Km; raw value: 8.5 ± 3.1; raw unit: μM; normalized value: 0.0085 mM; normalized unit: mM; metric: kcat/Km; normalized value: 15329.411764705883 s^-1 mM^-1; normalized unit: s^-1 mM^-1; assay condition: Table 4 footnote: Km and kcat were calculated using the Michaelis-Menten equation; reactions were performed in potassium phosphate buffer (pH 7.6) as described in Material and Methods; all Km and kcat values are expressed as the mean plus-minus standard deviation of three parallel experiments. Enzymatic activity assay (Materials and Methods, Block RVM0009-METHODS-VERBATIM): the standard reaction was carried out at 25 C using 50 uM substrate in DMSO, 50 mM potassium phosphate buffer (pH 7.6) containing 1 mg bovine serum albumin. The export row carries pH 7.6 and no stored temperature. Conversion note: 7819 min-1 divided by 60 is 130.31666666666666 s^-1, stored at the export's one-decimal precision as 130.3 s^-1; 8.5 uM divided by 1000 is 0.0085 mM exactly; kcat/Km is the quotient of this row's own two cells as stored, 130.3 s^-1 divided by 0.0085 mM giving 15329.411764705883 s^-1 mM^-1, which reproduces the printed ratio cell 1.53 x 10^7 M-1 s-1 exactly at that cell's three-significant-figure precision.

raw_value_unit_evidence: Table 4, row DaCHI1, Naringenin chalcone column group: kcat cell 7819 ± 825 min–1; Km cell 8.5 ± 3.1 μM; printed kcat/Km cell 1.53 × 10^7 M–1 s–1 (superscript 7 rendered on the preceding text-layer line).


column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row Q104E, naringenin chalcone column group; column kcat (min^-1) = 8082 ± 267; column Km (uM) = 6.1 ± 0.7; column kcat/Km (M^-1 s^-1) = 2.208 x 10^7.

raw_value_unit_evidence: Table 4, enzyme row Q104E, naringenin chalcone column group: kcat = 8082 ± 267 min^-1; Km = 6.1 ± 0.7 uM; printed kcat/Km = 2.208 x 10^7 M^-1 s^-1.

row_label: Table 4, row Q104E, naringenin chalcone column group


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:G4U3G8 and applied mutation signature I190M to reconstruct the assayed variant sequence.

column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row I190M, naringenin chalcone column group; column kcat (min^-1) = 11860 ± 539; column Km (uM) = 8.6 ± 1.2; column kcat/Km (M^-1 s^-1) = 2.292 x 10^7.

raw_value_unit_evidence: Table 4, enzyme row I190M, naringenin chalcone column group: kcat = 11860 ± 539 min^-1; Km = 8.6 ± 1.2 uM; printed kcat/Km = 2.292 x 10^7 M^-1 s^-1.

row_label: Table 4, row I190M, naringenin chalcone column group


column_label: Table 4 (Steady-state kinetic parameters of wild-type and mutant DaCHI1), enzyme row S189T, naringenin chalcone column group; column kcat (min^-1) = 13690 ± 556; column Km (uM) = 9.9 ± 1.2; column kcat/Km (M^-1 s^-1) = 2.306 x 10^7.

raw_value_unit_evidence: Table 4, enzyme row S189T, naringenin chalcone column group: kcat = 13690 ± 556 min^-1; Km = 9.9 ± 1.2 uM; printed kcat/Km = 2.306 x 10^7 M^-1 s^-1.

row_label: Table 4, row S189T, naringenin chalcone column group


organism: Vigna radiata


enzyme_display_name: chloromuconate cycloisomerase

organism: Rhodococcus opacus

proof_lines: pH and temperature not specified in the publication

enzyme: chloromuconate cycloisomerase


organism: Pseudomonas reinekei


assay_conditions_summary: buffer air-saturated

column_label: TABLE 2. Substrate specificities of muconate cycloisomerases MCIcatB and MCIsalC from Pseudomonas sp. strain MT1. TABLE 2, MCIsalC row 3-Methylmuconate; column 'Km (uM)' = 26.3; column 'kcat (s^-1)' = 214; column 'kcat/Km (s^-1 uM^-1)' = 8.13.

normalized_value_unit_evidence: Km: printed cell 26.3 uM converts to 0.0263 mM; the exported value is 0.026 mM. kcat: printed cell 214 s^-1 converts to 214.0 s^(-1); the exported value is 214.0 s^(-1). kcat/Km: printed cell 8.13 s^-1 uM^-1 converts to 8130.000000000001 s^(-1)*mM^(-1); the exported value is 8230.76923076923 s^(-1)*mM^(-1).

raw_value_unit_evidence: TABLE 2. Substrate specificities of muconate cycloisomerases MCIcatB and MCIsalC from Pseudomonas sp. strain MT1. TABLE 2, MCIsalC row 3-Methylmuconate: Km = 26.3 uM; kcat = 214 s^-1; printed kcat/Km = 8.13 s^-1 uM^-1.

row_label: TABLE 2, MCIsalC row 3-Methylmuconate


organism: Medicago sativa

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

source_databases_merged: sabio_rk skid uniprot


organism: Delftia acidovorans

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


organism: Arthrobacter sp.

column_label: Table 2. Substrate specificity of the MC from Arthrobacter sp. BA-5-17; row/segment 3-Ethyl-cis,cis-muconate; column/metric Km (uM)

raw_value_unit_evidence: Table 2 reports Km 670 +/- 32 uM for 3-ethyl-cis,cis-muconate.


organism: Homo sapiens


organism: Pseudomonas putida

substrate_name: cis,cis-Muconate

substrate: cis,cis-Muconate


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


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


column_label: PMID 9726873 TABLE 3. Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates; row 2,4-Dichloro-cis,cis-muconate / wild-type enzyme column group (TABLE 3); wild-type enzyme column group, sub-columns Km (uM), kcat (min^-1) and kcat/Km (min^-1 uM^-1); printed cells Km 26 ± 3 uM, kcat 3.3 ± 0.1 min^-1, kcat/Km 0.13 min^-1 uM^-1. The exported kcat/Km is recorded as the quotient of this same row's own two printed cells as stored (0.055 s^-1 / 0.026 mM = 2.1153846153846154 s^-1 mM^-1), not as the paper's rounded printed kcat/Km cell (0.13 min^-1 uM^-1), which agrees with that quotient at the printed cell's precision.

normalized_value_unit_evidence: metric: Km; normalized value: 0.026 mM; metric: kcat; normalized value: 0.055 s^-1; metric: kcat/Km; normalized value: 2.1153846153846154 s^-1 mM^-1; assay condition: Kinetic assay at pH 7.5 in 30 mM Tris-HCl with 1 mM MnSO4 at 25 degrees C, followed spectrophotometrically at 260 nm; purified wild-type P. putida PRS2000 muconate cycloisomerase, the TABLE 3 wild-type enzyme column group; kcat computed for a subunit molecular mass of 40 kDa

raw_value_unit_evidence: Table row as printed: Km 26 ± 3 uM; kcat 3.3 ± 0.1 min^-1; kcat/Km 0.13 min^-1 uM^-1 (wild-type enzyme column group).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08310 and applied mutation signature A271S with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates), substrate row '2,4-Dichloro-cis,cis-muconate', enzyme column group 'A271S'; column 'Km (uM)' = 44; column 'kcat (min^-1)' = 2.9; column 'kcat/Km (min^-1 uM^-1)' = 0.067.

raw_value_unit_evidence: Table 3, substrate row 2,4-Dichloro-cis,cis-muconate, enzyme column A271S: Km = 44 uM; kcat = 2.9 min^-1; printed kcat/Km = 0.067 min^-1 uM^-1.

table_label: Table 3: Kinetic constants of P. putida muconate cycloisomerase and variants with various substrates (Appl. Environ. Microbiol. 1998, 64(9):3290-3299)


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +11, so it is treated as a source-provided variant sequence.


organism: Drosophila melanogaster

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NAD+


organism: Arabidopsis thaliana

proof_lines: kcat is 6.4 min(-1) for D-glucose 6-phosphate. kcat is 5.0 min(-1) for NAD(+).


proof_lines: kcat is 4.0 min(-1) for D-glucose 6-phosphate. kcat is 3.6 min(-1) for NAD(+).


proof_lines: kcat is 5.2 min(-1) for D-glucose 6-phosphate. kcat is 4.8 min(-1) for NAD(+).


substrate_name: NAD(+)

substrate: NAD(+)


organism: Cupriavidus necator

proof_lines:
measurement of substrate consumption
measurement of product formation