organism: Proteus sp. (in: enterobacteria)

substrate_name: L-glutamine

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

assay_conditions_summary: pH 10.4; buffer 100 mM glycine-KCl-KOH

proof_lines: in 100 mM glycine-KCl-KOH buffer (pH 10.4)

substrate: L-glutamine


enzyme_display_name: L-amino-acid dehydrogenase

substrate_name: L-methionine

source_db: brenda

verification_status: unverified

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

source_license: CC BY 4.0

km_unit: mM

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

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

enzyme: L-amino-acid dehydrogenase

substrate: L-methionine

status: unverified

source: brenda


enzyme_display_name: glutamate dehydrogenase

organism: Arabidopsis thaliana

substrate_name: L-glutamate

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

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+

proof_lines: with NAD+, recombinant enzyme, pH and temperature not specified in the publication

enzyme: glutamate dehydrogenase

substrate: L-glutamate


enzyme_display_name: glutamate dehydrogenase (NADP+)

organism: Aeropyrum pernix K1

substrate_name: NADP+

kcat_display: Not reported

assay_conditions_summary: 323.15 K; cofactor NADP+

proof_lines:
oxidative deamination
oxidative deamination at 50°C

enzyme: glutamate dehydrogenase (NADP+)

substrate: NADP+


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

mutation_type: substitution

proof_lines:
reductive amination at 0.6 M NH4Cl
reductive amination at 1 M NH4Cl


enzyme_display_name: glutamate dehydrogenase [NAD(P)+]

organism: Homo sapiens

assay_conditions_summary: pH 8; 298.15 K; buffer 50 mM triethanolamine; cofactor NADP+

proof_lines:
pH 8.0, 25°C, wild-type enzyme hGDH1
hGDH1, wild-type
pH 8.0, 25°C, wild-type enzyme hGDH2

enzyme: glutamate dehydrogenase [NAD(P)+]


smiles: N

assay_conditions_summary: pH 8; buffer 50 mM triethanolamine; cofactor NADP+

proof_lines: wild type isozyme GDH1, in 50 mM triethanolamine buffer (pH 8.0), 2.6 mM EDTA, 1.4 mM NADP+, and 1 mM ADP

proof_lines: wild type isozyme GDH2, in 50 mM triethanolamine buffer (pH 8.0), 2.6 mM EDTA, 1.4 mM NADP+, and 1 mM ADP


organism: Pyrobaculum islandicum

substrate_name: NAD+

protein_accession_database: UniProt

sequence_source: multiple

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

assay_conditions_summary: cofactor NAD+

proof_lines:
recombinant, urea-activated enzyme
native enzyme
recombinant, heat-activated enzyme

data_origin: experimental

substrate: NAD+


proof_lines:
native enzyme
recombinant, heat-activated enzyme
recombinant, urea-activated enzyme


assay_conditions_summary: pH 9.5; 298.15 K; buffer 50 mM triethanolamine; cofactor NADP+

proof_lines:
pH 9.5, 25°C, wild-type enzyme hGDH1
pH 9.5, 25°C, wild-type enzyme hGDH2
pH 9.5, 25°C, wild-type enzyme


organism: Squalus acanthias

substrate_name: H2O; L-Glutamate; NADP+

km_display: Not reported

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

assay_conditions_summary: cofactor NADP+

substrate: H2O; L-Glutamate; NADP+


substrate_name: NADH

assay_conditions_summary: pH 8; 298.15 K; cofactor NADH

proof_lines:
25°C, wild-type enzyme
pH 8.0, 25°C, wild-type enzyme hGDH1
wild-type, hGDH1

substrate: NADH


organism: Archaeoglobus fulgidus

assay_conditions_summary: 333.15 K; cofactor NADP+


organism: Benjaminiella poitrasii

substrate_name: Unknown

ki_unit: mM

proof_lines: recombinant isozyme BpNADPGDH II, pH 8.0, 22°C

proof_lines: recombinant isozyme BpNADPGDH I, pH 8.0, 22°C

substrate: Unknown


organism: Synechocystis sp. PCC 6803

proof_lines: pH and temperature not specified in the publication


organism: Thermus thermophilus

assay_conditions_summary: pH 8; 310.15 K; buffer and 2 mM EDTA, pH 8, at 37°C; cofactor NADP+

proof_lines: in situ activity in 50 mM Tris-HCl buffer and 2 mM EDTA, pH 8, at 37°C


organism: Spermophilus richardsonii

substrate_name: H+; NH3; NADH; 2-Oxoglutarate

assay_conditions_summary: cofactor NADH

substrate: H+; NH3; NADH; 2-Oxoglutarate


organism: Citrobacter sp.

substrate_name: L-isoleucine

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

substrate: L-isoleucine


organism: Synechocystis sp.

substrate_name: L-arginine

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

substrate: L-arginine


organism: Chlorella sorokiniana

assay_conditions_summary: pH 7; 311.65 K; cofactor NADPH

proof_lines: reductive amination alpha-isoenzyme, depending on NADPH-concentration


organism: Peptoniphilus asaccharolyticus

substrate_name: NADPH

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E243R to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; buffer 100 mM potassium phosphate; cofactor NADPH

proof_lines: mutant enzyme E243R, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride

substrate: NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W244S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W244S, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E243D to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E243D, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D245K with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D245K, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride


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

proof_lines: wild type enzyme, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride


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

proof_lines: mutant enzyme E243K, in 100 mM potassium phosphate buffer at pH 7 with 20 mM oxoglutarate and 100 mM ammonium chloride


organism: Pseudomonas sp.

substrate_name: L-valine

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

proof_lines: in 100 mM glycine-KCl-KOH buffer (pH 10.4)

substrate: L-valine


enzyme_display_name: Alanine dehydrogenase

organism: Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16)

substrate_name: L-alanine (at pH 8.5 and 82 degrees Celsius)

source_db: uniprot

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

proof_lines: kcat is 6.1 sec(-1) and 9.6 sec(-1) for the oxidative deamination of L-alanine and L-2-aminobutyrate, respectively (at pH 8.5 and 82 degrees Celsius). kcat is 118 sec(-1), 143 sec(-1) and 113 sec(-1) for the reductive amination of pyruvate,

enzyme: Alanine dehydrogenase

source: uniprot


substrate_name: L-2-aminobutyrate (at pH 8.5 and 82 degrees Celsius)


substrate_name: NAD(+) (at pH 8.5 and 82 degrees Celsius)

assay_conditions_summary: pH 8.5; cofactor NAD+


substrate_name: pyruvate (at pH 8.5 and 82 degrees Celsius)


substrate_name: 2-oxobutyrate (at pH 8.5 and 82 degrees Celsius)

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


substrate_name: oxaloacetate (at pH 8.5 and 82 degrees Celsius)


substrate_name: NADH (at pH 8.5 and 82 degrees Celsius)

substrate: NADH (at pH 8.5 and 82 degrees Celsius)


substrate_name: NH4(+) (at pH 8.5 and 82 degrees Celsius)


enzyme_display_name: serine 2-dehydrogenase

organism: Pseudomonas aeruginosa

substrate_name: NAD+

verification_status: corrected

assay_conditions_summary: pH 11; cofactor NAD+

column_label: Table 1. Kinetic properties of PA0743 wild type and mutants, Table 1 / Wild type / NAD+: Km=3.4 mM; Vmax=2.8 umol/min/mg protein; kcat=1.6 s^-1; kcat/Km=0.5 x 10^3 M^-1 s^-1.

normalized_value_unit_evidence: Km=3.4 mM; Vmax=2.8 umol/min/mg protein; kcat=1.6 s^-1; kcat/Km=0.5 s^-1 mM^-1

row_label: Table 1 / Wild type / NAD+

enzyme: serine 2-dehydrogenase

status: corrected


verification_status: verified

column_label: Table 1. Kinetic properties of PA0743 wild type and mutants, Table 1 / Wild type / MDHP: kcat=11.6 s^-1.

row_label: Table 1 / Wild type / MDHP

status: verified


column_label: Table 1. Kinetic properties of PA0743 wild type and mutants, Table 1 / Wild type / Methyl-DL-serine: Km=2.4 mM.

normalized_value_unit_evidence: Km=2.4 mM

raw_value_unit_evidence: Km=2.4 mM

row_label: Table 1 / Wild type / Methyl-DL-serine


substrate_name: L-serine

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

assay_conditions_summary: pH 11

column_label: Table 1. Kinetic properties of PA0743 wild type and mutants, Table 1 / Wild type / L-serine: Km=2.5 mM; Vmax=18.7 umol/min/mg protein; kcat=10.4 s^-1; kcat/Km=0.4 x 10^4 M^-1 s^-1.

normalized_value_unit_evidence: Km=2.5 mM; Vmax=18.7 umol/min/mg protein; kcat=10.4 s^-1; kcat/Km=4.0 s^-1 mM^-1

row_label: Table 1 / Wild type / L-serine

substrate: L-serine


organism: [Clostridium] symbiosum

substrate_name: NADH

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D165N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 8

proof_lines: wild-type CsGDH, Vmax: 546 micromol/min/mg, pH 8.0, 25°C


substrate_name: L-glutamate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K333L with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature G446D with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K344L with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 7; buffer 0.1 M potassium phosphate; cofactor NAD+

proof_lines: wild type enzyme, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C

proof_lines: wild-type CsGDH, Vmax: 40.6 micromol/min/mg, pH 8.0, 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W393F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W393F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W449F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W449F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W64F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W64F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W310F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W310F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature W243F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W243F, in 0.1 M potassium phosphate buffer, at pH 7.0 and 25°C


assay_conditions_summary: pH 7; buffer 0.1 M potassium phosphate


organism: Halobacterium salinarum

kcat_over_km_origin: calculated

assay_conditions_summary: pH 9; cofactor NAD+

proof_lines: pH 9.0, 40°C, recombinant enzyme in presence of DMSO

proof_lines: kcat is 24 sec(-1) for glutamate in the presence of 3.2 M NaCl. kcat is 16 sec(-1) for NAD(+) in the presence of 3.2 M NaCl. kcat is 56 sec(-1) for 2-oxoglutarate in the presence of 3.2 M NaCl. kcat is 85 sec(-1) for NH(4)(+) in the presenc

source_databases_merged: brenda uniprot


assay_conditions_summary: pH 9; cofactor NADH


assay_conditions_summary: pH 8.5; cofactor NADH

proof_lines: pH 8.5, 40°C, recombinant enzyme in presence of DMSO


substrate_name: NADP+

assay_conditions_summary: pH 8; cofactor NADP+

proof_lines: chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, Vmax: 80.8 micromol/min/mg, pH 8.0, 25°C


assay_conditions_summary: pH 8; cofactor NADPH

proof_lines: chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, Vmax: 2180 micromol/min/mg, pH 8.0, 25°C


assay_conditions_summary: pH 8; buffer 0.1 M potassium phosphate

proof_lines: wild-type CsGDH, Vmax: 47.1 micromol/min/mg, pH 8.0, 25°C


proof_lines: wild-type CsGDH, Vmax: 307 micromol/min/mg, pH 8.0, 25°C


sequence_variant_note: Mutation signature H4C could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, 781 mM NH4Cl, Vmax: 2260 micromol/min/mg, pH 8.0, 25°C

proof_lines: chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, 1800 mM NH4Cl, Vmax: 200 micromol/min/mg, pH 8.0, 25°C


assay_conditions_summary: pH 7

proof_lines: chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, Vmax: 1960 micromol/min/mg, pH 8.0, 25°C


proof_lines: chimeric protein CEC consisting of the substrate-binding domain of CsGDH and the coenzyme-binding domain of Escherichia coli GDH, Vmax: 121.9 micromol/min/mg, pH 8.0, 25°C


organism: Bryopsis maxima

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

assay_conditions_summary: cofactor NADP+


assay_conditions_summary: cofactor NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature A242G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6; cofactor NADH

proof_lines:
pH 6.0, 25°C, mutant A242G
pH 7.0, 25°C, mutant A242G
pH 8.0, 25°C, mutant A242G


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F238S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines:
pH 6.0, 25°C, mutant F238S
pH 7.0, 25°C, mutant F238S
pH 8.0, 25°C, mutant F238S


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F238S/P262S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines:
pH 6.0, 25°C, mutant F238S/P262S
pH 7.0, 25°C, mutant F238S/P262S
pH 8.0, 25°C, mutant F238S/P262S


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -1, so it is treated as a source-provided variant sequence.

proof_lines:
pH 6.0, 25°C, mutant P262S
pH 7.0, 25°C, mutant P262S
pH 8.0, 25°C, mutant P262S


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D263K with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

proof_lines:
pH 6.0, 25°C, mutant D263K
pH 7.0, 25°C, mutant D263K
pH 8.0, 25°C, mutant D263K


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

assay_conditions_summary: pH 8; cofactor NADH

proof_lines: pH 6.0, 25°C, recombinant wild-type enzyme

proof_lines: pH 7.0, 25°C, recombinant wild-type enzyme

proof_lines: pH 8.0, 25°C, recombinant wild-type enzyme


organism: Agaricus bisporus

assay_conditions_summary: 306.15 K; cofactor NADPH

column_label: Primary abstract kinetic prose; substrate NADPH; Km value 0.074 mM

raw_value_unit_evidence: Abstract Km-value list reports 0.074 mM for NADPH

row_label: NADPH

table_label: PMID 7765894 primary abstract kinetic prose


assay_conditions_summary: 306.15 K; cofactor NADP+

column_label: Primary abstract kinetic prose; substrate NADP; Km value 0.117 mM

raw_value_unit_evidence: Abstract Km-value list reports 0.117 mM for NADP

row_label: NADP


column_label: Primary abstract kinetic prose; substrate ammonia; Km value 2.1 mM

raw_value_unit_evidence: Abstract Km-value list reports 2.1 mM for ammonia

row_label: ammonia


column_label: Primary abstract kinetic prose; substrate 2-oxoglutarate; Km value 3.2 mM

raw_value_unit_evidence: Abstract Km-value list reports 3.2 mM for 2-oxoglutarate


column_label: Primary abstract kinetic prose; substrate L-glutamate; Km value 27.0 mM

raw_value_unit_evidence: Abstract Km-value list reports 27.0 mM for L-glutamate

row_label: L-glutamate


organism: Saccharolobus solfataricus

assay_conditions_summary: pH 7.6; cofactor NADH

proof_lines:
+ 2-oxoglutarate
pH 7.6, 50°C


assay_conditions_summary: pH 7.6; cofactor NADPH

proof_lines:
+ 2-oxoglutarate
pH 7.6, 60°C


assay_conditions_summary: cofactor NAD+


proof_lines:
cosubstrate NADPH
cosubstrate NADH
pH 7.6, 60°C


assay_conditions_summary: pH 7.6; cofactor NADP+

proof_lines:
cosubstrate NAD+
cosubstrate NADP+
pH 7.6, 60°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A40N to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; cofactor NADP+


assay_conditions_summary: pH 7; cofactor NADPH


organism: Streptomyces fradiae


organism: Pyrobaculum calidifontis

assay_conditions_summary: pH 10.5; 323.15 K; cofactor NAD+

column_label: Table 4: Kinetic constants (Extremophiles 2013, volume 17, pages 379-389); printed column heads Enzyme | Substrate | Km (mM) | kcat (s-1) | kcat/Km (mM-1 s-1). Table 4, Pcal_1031 oxidative deamination block, row NAD+; column Km (mM) = 0.028; column kcat (s-1) = 14; column kcat/Km (mM-1 s-1) = 500. captured primary segment: Pcal_1031 | Oxidative deamination | NAD+ | Km 0.028 ± 0.0025 mM | kcat 14 ± 0.54 s^-1 | kcat/Km 500 mM^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 4 cell 14 s^-1; the printed unit s^-1 is already the export unit, so no unit conversion applies and the paper value is 14.0 s^(-1); the exported value is 14.0 s^(-1). Km: printed Table 4 cell 0.028 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.028 mM; the exported value is 0.028 mM. kcat/Km: printed Table 4 cell 500 mM^-1 s^-1; the printed unit mM^-1 s^-1 is already the export unit, so no unit conversion applies and the paper value is 500.0 s^(-1)*mM^(-1); the exported value is 500.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 14.0 / 0.028 = 500.0 s^-1 mM^-1, which is the same number as the printed efficiency cell, so this row closes on itself.

raw_value_unit_evidence: Table 4, Table 4, Pcal_1031 oxidative deamination block, row NAD+: Km = 0.028 mM; kcat = 14 s^-1; printed kcat/Km = 500 mM^-1 s^-1.


column_label: Table 4: Kinetic constants (Extremophiles 2013, volume 17, pages 379-389); printed column heads Enzyme | Substrate | Km (mM) | kcat (s-1) | kcat/Km (mM-1 s-1). Table 4, Pcal_1031 oxidative deamination block, row L-Glutamate; column Km (mM) = 5.3; column kcat (s-1) = 17; column kcat/Km (mM-1 s-1) = 3.2. captured primary segment: Pcal_1031 | Oxidative deamination | L-Glutamate | Km 5.3 ± 0.49 mM | kcat 17 ± 0.94 s^-1 | kcat/Km 3.2 mM^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 4 cell 17 s^-1; the printed unit s^-1 is already the export unit, so no unit conversion applies and the paper value is 17.0 s^(-1); the exported value is 17.0 s^(-1). Km: printed Table 4 cell 5.3 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 5.3 mM; the exported value is 5.3 mM. kcat/Km: printed Table 4 cell 3.2 mM^-1 s^-1; the printed unit mM^-1 s^-1 is already the export unit, so no unit conversion applies and the printed cell is 3.2 s^(-1)*mM^(-1). Quotient disclosure for this row: 17.0 / 5.3 = 3.207547169811321 s^-1 mM^-1, the exported value, and the printed efficiency cell is that quotient written to the two significant figures the table uses.

raw_value_unit_evidence: Table 4, Table 4, Pcal_1031 oxidative deamination block, row L-Glutamate: Km = 5.3 mM; kcat = 17 s^-1; printed kcat/Km = 3.2 mM^-1 s^-1.


assay_conditions_summary: pH 9.5; 323.15 K; cofactor NADH

column_label: Table 4: Kinetic constants (Extremophiles 2013, volume 17, pages 379-389); printed column heads Enzyme | Substrate | Km (mM) | kcat (s-1) | kcat/Km (mM-1 s-1). Table 4, Pcal_1031 reductive amination block, row NADH; column Km (mM) = 0.010; column kcat (s-1) = 58; column kcat/Km (mM-1 s-1) = 5,800. captured primary segment: Pcal_1031 | Reductive amination | NADH | Km 0.010 ± 0.0013 mM | kcat 58 ± 2.4 s^-1 | kcat/Km 5,800 mM^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 4 cell 58 s^-1; the printed unit s^-1 is already the export unit, so no unit conversion applies and the paper value is 58.0 s^(-1); the exported value is 58.0 s^(-1). Km: printed Table 4 cell 0.010 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.01 mM; the exported value is 0.01 mM. kcat/Km: printed Table 4 cell 5,800 mM^-1 s^-1; the printed unit mM^-1 s^-1 is already the export unit, so no unit conversion applies and the paper value is 5800.0 s^(-1)*mM^(-1); the exported value is 5800.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 58.0 / 0.01 = 5800.0 s^-1 mM^-1, which is the same number as the printed efficiency cell, so this row closes on itself.

raw_value_unit_evidence: Table 4, Table 4, Pcal_1031 reductive amination block, row NADH: Km = 0.010 mM; kcat = 58 s^-1; printed kcat/Km = 5,800 mM^-1 s^-1.


column_label: Table 4: Kinetic constants (Extremophiles 2013, volume 17, pages 379-389); printed column heads Enzyme | Substrate | Km (mM) | kcat (s-1) | kcat/Km (mM-1 s-1). Table 4, Pcal_1031 reductive amination block, row Ammonia; column Km (mM) = 9.8; column kcat (s-1) = 58; column kcat/Km (mM-1 s-1) = 5.9. captured primary segment: Pcal_1031 | Reductive amination | Ammonia | Km 9.8 ± 0.36 mM | kcat 58 ± 1.9 s^-1 | kcat/Km 5.9 mM^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 4 cell 58 s^-1; the printed unit s^-1 is already the export unit, so no unit conversion applies and the paper value is 58.0 s^(-1); the exported value is 58.0 s^(-1). Km: printed Table 4 cell 9.8 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 9.8 mM; the exported value is 9.8 mM. kcat/Km: printed Table 4 cell 5.9 mM^-1 s^-1; the printed unit mM^-1 s^-1 is already the export unit, so no unit conversion applies and the printed cell is 5.9 s^(-1)*mM^(-1). Quotient disclosure for this row: 58.0 / 9.8 = 5.918367346938775 s^-1 mM^-1, the exported value, and the printed efficiency cell is that quotient written to the two significant figures the table uses.

raw_value_unit_evidence: Table 4, Table 4, Pcal_1031 reductive amination block, row Ammonia: Km = 9.8 mM; kcat = 58 s^-1; printed kcat/Km = 5.9 mM^-1 s^-1.


column_label: Table 4: Kinetic constants (Extremophiles 2013, volume 17, pages 379-389); printed column heads Enzyme | Substrate | Km (mM) | kcat (s-1) | kcat/Km (mM-1 s-1). Table 4, Pcal_1031 reductive amination block, row 2-Oxoglutarate; column Km (mM) = 0.92; column kcat (s-1) = 65; column kcat/Km (mM-1 s-1) = 71. captured primary segment: Pcal_1031 | Reductive amination | 2-Oxoglutarate | Km 0.92 ± 0.0078 mM | kcat 65 ± 1.1 s^-1 | kcat/Km 71 mM^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 4 cell 65 s^-1; the printed unit s^-1 is already the export unit, so no unit conversion applies and the paper value is 65.0 s^(-1); the exported value is 65.0 s^(-1). Km: printed Table 4 cell 0.92 mM; the printed unit mM is already the export unit, so no unit conversion applies and the paper value is 0.92 mM; the exported value is 0.92 mM. kcat/Km: printed Table 4 cell 71 mM^-1 s^-1; the printed unit mM^-1 s^-1 is already the export unit, so no unit conversion applies and the printed cell is 71.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 65.0 / 0.92 = 70.65217391304347 s^-1 mM^-1, the exported value, and the printed efficiency cell is that quotient written to the two significant figures the table uses.

raw_value_unit_evidence: Table 4, Table 4, Pcal_1031 reductive amination block, row 2-Oxoglutarate: Km = 0.92 mM; kcat = 65 s^-1; printed kcat/Km = 71 mM^-1 s^-1.


organism: Psychrobacter sp.

assay_conditions_summary: pH 8; cofactor NAD+

proof_lines:
NAD+-dependent enzyme
pH 8.0, 20°C


enzyme_display_name: alanine dehydrogenase

organism: Aphanothece halophytica

substrate_name: pyruvate

assay_conditions_summary: pH 9

proof_lines: pH 9.0, temperature not specified in the publication

enzyme: alanine dehydrogenase

substrate: pyruvate


substrate_name: L-alanine

assay_conditions_summary: pH 10

proof_lines: pH 10.0, temperature not specified in the publication

substrate: L-alanine


substrate_name: glyoxylate

proof_lines: pH 8.5, temperature not specified in the publication

substrate: glyoxylate


organism: Dictyostelium discoideum

assay_conditions_summary: cofactor NADH

proof_lines:
non-activated NAD-GDH
activated NAD-GDH


proof_lines:
activated NAD-GDH
non-activated NAD-GDH


organism: Thermococcus kodakarensis

substrate_name: NADPH

proof_lines: pH 7.6, 70°C, recombinent enzyme (heated)

proof_lines: pH 7.6, 70°C, recombinent enzyme (unheated)


organism: Halobacterium sp.

assay_conditions_summary: cofactor NADPH


assay_conditions_summary: cofactor NADP+


organism: Synechocystis sp.


organism: Phormidium lapideum

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature I198R with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


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


organism: Nitrobacter hamburgensis


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M415L/R443S/G456A with inferred residue-numbering offset -39 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; cofactor NADH

proof_lines: mutant enzyme M415L/R443S/G456A, 50 mM triethanolamine pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0 at 25°C


organism: Amycolatopsis sulphurea


organism: Trichomonas vaginalis


assay_conditions_summary: pH 9.5; cofactor NADP+

column_label: Table 4 enzyme Pcal_1606, Oxidative deamination row L-Glutamate; columns Km mM, kcat s^-1, kcat/Km mM^-1*s^-1; raw cells 3.4 +/- 0.35, 13 +/- 0.61, 3.8; normalized cells 3.4 mM, 13 s^-1, 3.8 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=3.4 normalized_unit=mM; kcat normalized_value=13 normalized_unit=s^-1; kcat/Km normalized_value=3.8 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=3.4 +/- 0.35 raw_unit=mM; kcat raw_value=13 +/- 0.61 raw_unit=s^-1; kcat/Km raw_value=3.8 raw_unit=mM^-1*s^-1

row_label: Pcal_1606 oxidative deamination / L-Glutamate

table_label: Table 4. Kinetic constants


assay_conditions_summary: pH 9; cofactor NADPH

proof_lines: kcat is 13 sec(-1) for oxidative deamination of L-glutamate, and 95 sec(-1) for reductive amination of 2-oxoglutarate (at 50 degrees Celsius).


assay_conditions_summary: pH 9; cofactor NADP+

column_label: Table 4 enzyme Pcal_1606, Reductive amination row 2-Oxoglutarate; columns Km mM, kcat s^-1, kcat/Km mM^-1*s^-1; raw cells 1.7 +/- 0.45, 95 +/- 13, 56; normalized cells 1.7 mM, 95 s^-1, 56 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=1.7 normalized_unit=mM; kcat normalized_value=95 normalized_unit=s^-1; kcat/Km normalized_value=56 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=1.7 +/- 0.45 raw_unit=mM; kcat raw_value=95 +/- 13 raw_unit=s^-1; kcat/Km raw_value=56 raw_unit=mM^-1*s^-1

row_label: Pcal_1606 reductive amination / 2-Oxoglutarate


column_label: Table 4 enzyme Pcal_1606, Reductive amination row Ammonia; columns Km mM, kcat s^-1, kcat/Km mM^-1*s^-1; raw cells 2.2 +/- 0.071, 100 +/- 3.0, 45; normalized cells 2.2 mM, 100 s^-1, 45 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=2.2 normalized_unit=mM; kcat normalized_value=100 normalized_unit=s^-1; kcat/Km normalized_value=45 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=2.2 +/- 0.071 raw_unit=mM; kcat raw_value=100 +/- 3.0 raw_unit=s^-1; kcat/Km raw_value=45 raw_unit=mM^-1*s^-1

row_label: Pcal_1606 reductive amination / Ammonia


organism: Peptoniphilus asaccharolyticus

proof_lines: These values indicate a 1165-fold discrimination in favor of NADH.


assay_conditions_summary: pH 7; cofactor NADH


organism: Saccharomyces cerevisiae

proof_lines: isoform Gdh3, S0.5 value, Hill coefficient 2.4, pH 5.8, 30°C


assay_conditions_summary: pH 7.5; cofactor NADPH


organism: Bacillus subtilis

substrate_name: NAD+; L-Alanine; H2O

assay_conditions_summary: cofactor NAD+

substrate: NAD+; L-Alanine; H2O


organism: Lysinibacillus sphaericus

substrate_name: oxidative deamination of L-alanine

substrate: oxidative deamination of L-alanine


substrate_name: L-Glutamate; NAD+; H2O

substrate: L-Glutamate; NAD+; H2O


organism: Chlamydomonas reinhardtii

substrate_name: NH3; H+; NADH; 2-Oxoglutarate

substrate: NH3; H+; NADH; 2-Oxoglutarate


organism: Clostridium symbiosum

substrate_name: NAD+; H2O; L-Glutamate

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

substrate: NAD+; H2O; L-Glutamate


enzyme_display_name: Glutamate dehydrogenase 2

substrate_name: ammonium ions

enzyme: Glutamate dehydrogenase 2

substrate: ammonium ions


organism: Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1)

substrate_name: NADP(+) (at 50 degrees Celsius)

substrate: NADP(+) (at 50 degrees Celsius)


organism: Streptomyces clavuligerus

substrate_name: L-Ala

proof_lines:
with respect to NADH
with respect to NH4+
with respect to pyruvate

substrate: L-Ala


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


organism: Mustela vison

substrate_name: NH3; NADH; H+; 2-Oxoglutarate

substrate: NH3; NADH; H+; 2-Oxoglutarate


organism: Pyrococcus furiosus


organism: Pyrococcus horikoshii

substrate_name: NADP+; L-Glutamate; H2O

substrate: NADP+; L-Glutamate; H2O


organism: Rattus norvegicus


organism: Thermococcus kodakaraensis

substrate_name: NADPH; H+; NH3; 2-Oxoglutarate

substrate: NADPH; H+; NH3; 2-Oxoglutarate


organism: Dictyostelium discoideum

substrate_name: 2-Oxoglutarate; NADH; NH3

substrate: 2-Oxoglutarate; NADH; NH3


organism: Escherichia coli


organism: Mycobacterium smegmatis

substrate_name: NAD+; L-Glutamate; H2O

substrate: NAD+; L-Glutamate; H2O


organism: Pyrobaculum islandicum


organism: Bos taurus

substrate_name: NH3; NADH; 2-Oxoglutarate; H+

substrate: NH3; NADH; 2-Oxoglutarate; H+


organism: Homo sapiens

substrate_name: L-Glutamate; H2O; NAD+

substrate: L-Glutamate; H2O; NAD+


organism: Schizosaccharomyces pombe


organism: Bilophila wadsworthia

substrate_name: Unknown

substrate: Unknown


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


organism: Rhizobium sp.


organism: Streptomyces coelicolor

substrate_name: L-serine

proof_lines: pH 9.0, 30°C, reductive amination reaction

substrate: L-serine


smiles: CCC(=O)CC(=O)O


substrate_name: pyruvate

substrate: pyruvate


organism: Chlamydomonas reinhardtii

substrate_name: NH3; H+; NADPH; 2-Oxoglutarate

substrate: NH3; H+; NADPH; 2-Oxoglutarate


substrate_name: L-Glutamate; NADP+; H2O

substrate: L-Glutamate; NADP+; H2O


organism: Salmonella typhimurium

substrate_name: NADPH; 2-Oxoglutarate; H+; NH3

assay_conditions_summary: pH 7; cofactor NADP+

substrate: NADPH; 2-Oxoglutarate; H+; NH3


enzyme_display_name: glutamate dehydrogenase (NADP(+))

organism: Thermococcus waiotapuensis

substrate_name: NADPH

source_db: oed

assay_conditions_summary: pH 8; 353.15 K; cofactor NADPH

enzyme: glutamate dehydrogenase (NADP(+))

substrate: NADPH

source: oed


organism: Trichomonas vaginalis


substrate_name: L-glutamate

substrate: L-glutamate


substrate_name: L-alanine

substrate: L-alanine


substrate_name: L-norvaline

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

substrate: L-norvaline


substrate_name: glyoxylate

substrate: glyoxylate


substrate_name: L-valine

substrate: L-valine


organism: [Clostridium] symbiosum

substrate_name: NADH

sequence_variant_note: Mutation signature F232S/P262S/D263K could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant F232S/P262S/D263K , pH and temperature not specified in the publication

substrate: NADH


substrate_name: NAD+

substrate: NAD+


organism: Halobacterium salinarum

substrate_name: NH(4)(+) (for the recombinant enzyme, in the presence of 3.2 M NaCl)

assay_conditions_summary: pH 8; 313.15 K; cofactor NAD+

proof_lines: pH 8.0, 40°C, Ki(slope), at 120 mM L-glutamate

proof_lines: pH 8.0, 40°C, Ki(intercept), at 2.5 mM NAD+


organism: Sulfolobus solfataricus

substrate_name: 2-Oxoglutarate; NADH; H+; NH3

proof_lines:
vs. 2-oxoglutarate
vs. NADH

substrate: 2-Oxoglutarate; NADH; H+; NH3


organism: Escherichia coli

substrate_name: H2O; NADP+; L-Glutamate

substrate: H2O; NADP+; L-Glutamate


enzyme_display_name: UniProt P39633

organism: Bacillus subtilis

source_db: skid

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

assay_conditions_summary: pH 7.7; buffer pH 7; cofactor NAD+

column_label: PDF text lines 212-218 report deamination Km 0.34 mM for L-glutamate and kcat 18.1 s^-1; methods lines 147-151 define deamination assay with L-glutamate and NAD+ at 37 C pH 7.7

normalized_value_unit_evidence: kcat normalized_value=18.1 normalized_unit=s^-1; Km normalized_value=0.34 normalized_unit=mM; kcat/Km normalized_value=53.23529411764706 normalized_unit=s^-1*mM^-1 from same-row 18.1/0.34

raw_value_unit_evidence: kcat raw_value=18.1 raw_unit=s^-1 for deamination; Km raw_value=0.34 raw_unit=mM for L-glutamate

row_label: Wild-Type / L-glutamate

table_label: Results prose and enzyme assay methods for wild-type Bs-GluDH deamination reaction

source_databases_merged: skid uniprot

enzyme: UniProt P39633

source: skid


assay_conditions_summary: pH 7.3; buffer pH 7; cofactor NADH

column_label: PDF Table 3 row Wild-Type has 342 and 0.65; row Q144R has 435 and 1.22; current export row stores 435 and 0.65 without mutation label

normalized_value_unit_evidence: Export combines kcat 435 with Km 0.65; no single Table 3 row supports that tuple

raw_value_unit_evidence: Wild-type row has kcat raw_value=342 s^-1 and Km raw_value=0.65 mM for 2-OG; Q144R row has kcat raw_value=435 s^-1 and Km raw_value=1.22 mM for 2-OG

row_label: Unlabelled export row compared to Wild-Type / 2-OG

table_label: Table 3 Steady-State Kinetic Parameters of Wild-Type Q144R and E27F Mutant Enzymes in Their Amination Reactions


column_label: PDF text lines 212-218 report deamination Km 0.08 mM for NAD+; methods lines 147-151 define deamination assay with L-glutamate and NAD+ at 37 C pH 7.7

raw_value_unit_evidence: Km raw_value=0.08 raw_unit=mM for NAD+

row_label: Wild-Type / NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E27F to reconstruct the assayed variant sequence.

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

assay_conditions_summary: pH 7.3; 310.15 K; cofactor NADH


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39633 and applied mutation signature Q144R to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.3; 310.15 K; buffer pH 7; cofactor NADH

column_label: PDF Table 3 row Q144R; columns kcat 435; Km 2-OG 1.22; kcat/Km 2-OG 356

normalized_value_unit_evidence: kcat normalized_value=435 s^-1; Km normalized_value=1.22 mM; kcat/Km normalized_value=356.55737704918033 s^-1*mM^-1 from same-row 435/1.22

raw_value_unit_evidence: Q144R kcat raw_value=435 s^-1; Km raw_value=1.22 mM for 2-OG; printed kcat/Km 2-OG=356


column_label: PDF Table 3 row Wild-Type; columns kcat s^-1 342; Km mM 2-OG 0.65; kcat/Km s^-1 mM^-1 2-OG printed 535; exact calculated export efficiency 342/0.65=526.1538461538462

normalized_value_unit_evidence: kcat normalized_value=342 normalized_unit=s^-1; Km normalized_value=0.65 normalized_unit=mM; kcat/Km normalized_value=526.1538461538462 normalized_unit=s^-1*mM^-1 from same-row 342/0.65

raw_value_unit_evidence: kcat raw_value=342 raw_unit=s^-1; Km raw_value=0.65 raw_unit=mM for 2-OG; printed kcat/Km for 2-OG=535 s^-1 mM^-1

row_label: Wild-Type / 2-OG


substrate_name: L-Glutamate

assay_conditions_summary: pH 7.7; 310.15 K; buffer pH 7; cofactor NAD+

substrate: L-Glutamate


column_label: PDF text lines 212-218 report deamination Km 0.08 mM for NAD+ and kcat 18.1 s^-1; methods lines 147-151 define deamination assay with L-glutamate and NAD+ at 37 C pH 7.7

normalized_value_unit_evidence: kcat normalized_value=18.1 normalized_unit=s^-1; Km normalized_value=0.08 normalized_unit=mM; kcat/Km normalized_value=226.25 normalized_unit=s^-1*mM^-1 from same-row 18.1/0.08

raw_value_unit_evidence: kcat raw_value=18.1 raw_unit=s^-1 for deamination; Km raw_value=0.08 raw_unit=mM for NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39633 and applied mutation signature E27F to reconstruct the assayed variant sequence.

column_label: PDF Table 3 row E27F; columns kcat 344; Km NADH 0.16; kcat/Km NADH 2150

normalized_value_unit_evidence: kcat normalized_value=344 s^-1; Km normalized_value=0.16 mM; kcat/Km normalized_value=2150 s^-1*mM^-1 from same-row 344/0.16

raw_value_unit_evidence: E27F kcat raw_value=344 s^-1; Km raw_value=0.16 mM for NADH; printed kcat/Km NADH=2150

row_label: E27F / NADH


enzyme_display_name: glutamate dehydrogenase [NAD(P)(+)]

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -2, so it is treated as a source-provided variant sequence.

enzyme: glutamate dehydrogenase [NAD(P)(+)]


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G96Y with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K118Y with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +5, so it is treated as a source-provided variant sequence.


sequence_variant_note: Mutation signature K94Y could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +10, so it is treated as a source-provided variant sequence.


assay_conditions_summary: pH 9.5; 298.15 K; cofactor NAD+

column_label: Table 1; row hGDH2 / WT; columns kcat, Km (L-Glutamate), kcat/Km (L-Glutamate)

raw_value_unit_evidence: Table 1 cells for hGDH2 WT, substrate L-Glutamate: kcat=83 s^-1; Km=1.81 mM; kcat/Km=45.9 s^-1 mM^-1

row_label: hGDH2 / WT

table_label: Table 1


organism: Clostridium symbiosum

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P24295 and applied mutation signature A163G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 298.15 K; cofactor NADH

column_label: Table 3: Comparison between the mutants and wild-type GDH with respect to kinetic parameters for substrates glutamate and 2-oxoglutarate (Eur. J. Biochem. 268, 5791-5799 (2001)); the enzyme label runs down the left edge and each enzyme block carries three printed lines, 'Glu' at pH 7.0, 'Glu' at pH 8.0 and '2-og' at pH 7.0, under the column heads 'pH', 'Km (mM)', 'kcat (s^-1)' and 'kcat/Km (s^-1 M^-1)'. Table 3, row A163G with substrate 2-og at pH 7.0: column 'Km (mM)' = 1.1 +/- 0.07; column 'kcat (s^-1)' = 210 +/- 3.4; column 'kcat/Km (s^-1 M^-1)' = 1.94 x 10^5.

normalized_value_unit_evidence: Km: printed cell 1.1 +/- 0.07 in the column head 'Km (mM)'; the unit is already mM, so no unit conversion applies and the paper value is 1.1 mM. kcat: printed cell 210 +/- 3.4 in the column head 'kcat (s^-1)'; the unit is already s^-1, so no unit conversion applies and the paper value is 210.0 s^(-1). kcat/Km: printed cell 1.94 x 10^5 in the column head 'kcat/Km (s^-1 M^-1)'; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.94 x 10^5 / 1000 = 194.0 s^-1 mM^-1. Closure reading: the quotient of the two printed component cells is 210.0 / 1.1 = 190.9090909090909 s^-1 mM^-1, and the paper's own efficiency cell for the same row is printed as 1.94 x 10^5 s^-1 M^-1.

raw_value_unit_evidence: Table 3, row A163G with substrate 2-og at pH 7.0: column 'Km (mM)' prints 1.1 +/- 0.07; column 'kcat (s^-1)' prints 210 +/- 3.4; column 'kcat/Km (s^-1 M^-1)' prints 1.94 x 10^5.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P24295 and applied mutation signature K89L/A163G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3: Comparison between the mutants and wild-type GDH with respect to kinetic parameters for substrates glutamate and 2-oxoglutarate (Eur. J. Biochem. 268, 5791-5799 (2001)); the enzyme label runs down the left edge and each enzyme block carries three printed lines, 'Glu' at pH 7.0, 'Glu' at pH 8.0 and '2-og' at pH 7.0, under the column heads 'pH', 'Km (mM)', 'kcat (s^-1)' and 'kcat/Km (s^-1 M^-1)'. Table 3, row KA/LG (the mutant K89L/A163G) with substrate 2-og at pH 7.0: column 'Km (mM)' = 6.74 +/- 0.16; column 'kcat (s^-1)' = 2.95 +/- 0.04; column 'kcat/Km (s^-1 M^-1)' = 4.4 x 10^2.

normalized_value_unit_evidence: Km: printed cell 6.74 +/- 0.16 in the column head 'Km (mM)'; the unit is already mM, so no unit conversion applies and the paper value is 6.74 mM. kcat: printed cell 2.95 +/- 0.04 in the column head 'kcat (s^-1)'; the unit is already s^-1, so no unit conversion applies and the paper value is 2.95 s^(-1). kcat/Km: printed cell 4.4 x 10^2 in the column head 'kcat/Km (s^-1 M^-1)'; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.4 x 10^2 / 1000 = 0.44 s^-1 mM^-1. Closure reading: the quotient of the two printed component cells is 2.95 / 6.74 = 0.43768545994065283 s^-1 mM^-1, and the paper's own efficiency cell for the same row is printed as 4.4 x 10^2 s^-1 M^-1.

raw_value_unit_evidence: Table 3, row KA/LG (the mutant K89L/A163G) with substrate 2-og at pH 7.0: column 'Km (mM)' prints 6.74 +/- 0.16; column 'kcat (s^-1)' prints 2.95 +/- 0.04; column 'kcat/Km (s^-1 M^-1)' prints 4.4 x 10^2.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P24295 and applied mutation signature S380A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 3: Comparison between the mutants and wild-type GDH with respect to kinetic parameters for substrates glutamate and 2-oxoglutarate (Eur. J. Biochem. 268, 5791-5799 (2001)); the enzyme label runs down the left edge and each enzyme block carries three printed lines, 'Glu' at pH 7.0, 'Glu' at pH 8.0 and '2-og' at pH 7.0, under the column heads 'pH', 'Km (mM)', 'kcat (s^-1)' and 'kcat/Km (s^-1 M^-1)'. Table 3, row S380A with substrate 2-og at pH 7.0: column 'Km (mM)' = 1.7 +/- 0.03; column 'kcat (s^-1)' = 38.3 +/- 0.34; column 'kcat/Km (s^-1 M^-1)' = 2.3 x 10^4.

normalized_value_unit_evidence: Km: printed cell 1.7 +/- 0.03 in the column head 'Km (mM)'; the unit is already mM, so no unit conversion applies and the paper value is 1.7 mM. kcat: printed cell 38.3 +/- 0.34 in the column head 'kcat (s^-1)'; the unit is already s^-1, so no unit conversion applies and the paper value is 38.3 s^(-1). kcat/Km: printed cell 2.3 x 10^4 in the column head 'kcat/Km (s^-1 M^-1)'; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.3 x 10^4 / 1000 = 23.0 s^-1 mM^-1. Closure reading: the quotient of the two printed component cells is 38.3 / 1.7 = 22.52941176470588 s^-1 mM^-1, and the paper's own efficiency cell for the same row is printed as 2.3 x 10^4 s^-1 M^-1.

raw_value_unit_evidence: Table 3, row S380A with substrate 2-og at pH 7.0: column 'Km (mM)' prints 1.7 +/- 0.03; column 'kcat (s^-1)' prints 38.3 +/- 0.34; column 'kcat/Km (s^-1 M^-1)' prints 2.3 x 10^4.


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

normalized_value_unit_evidence: Km 0.22 mM; kcat 179 s^(-1); independently printed kcat/Km 814 s^(-1)*mM^(-1).

raw_value_unit_evidence: WT 2-og row: Km 0.22 +/- 0.05 mM; kcat 179 +/- 2 s^-1; independently printed kcat/Km 8.14 x 10^5 s^-1 M^-1.

table_label: Table 3. Kinetic parameters for glutamate and 2-oxoglutarate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P24295 and applied mutation signature K89L with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

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

column_label: Table 5: Comparison of kinetic parameters for three mutant enzymes with two monocarboxylic 2-oxoacid substrates (Eur. J. Biochem. 268, 5791-5799 (2001)); the enzyme label runs down the left edge and the six data columns form two groups of three, the group '2-Oxocaproic acid' then the group '2-Oxo-g-methiolbutyric acid', each carrying the column heads 'Km (mM)', 'kcat (s^-1)' and 'kcat/Km (s^-1 M^-1)'. Table 5, row K89L with substrate 2-Oxocaproic acid at pH 7.0: column 'Km (mM) in the '2-Oxocaproic acid' column group' = 39.4 +/- 4.4; column 'kcat (s^-1) in the '2-Oxocaproic acid' column group' = 13.8 +/- 1; column 'kcat/Km (s^-1 M^-1) in the '2-Oxocaproic acid' column group' = 3.5 x 10^2.

normalized_value_unit_evidence: Km: printed cell 39.4 +/- 4.4 in the column head 'Km (mM) in the '2-Oxocaproic acid' column group'; the unit is already mM, so no unit conversion applies and the paper value is 39.4 mM. kcat: printed cell 13.8 +/- 1 in the column head 'kcat (s^-1) in the '2-Oxocaproic acid' column group'; the unit is already s^-1, so no unit conversion applies and the paper value is 13.8 s^(-1). kcat/Km: printed cell 3.5 x 10^2 in the column head 'kcat/Km (s^-1 M^-1) in the '2-Oxocaproic acid' column group'; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.5 x 10^2 / 1000 = 0.35 s^-1 mM^-1. Closure reading: the quotient of the two printed component cells is 13.8 / 39.4 = 0.35025380710659904 s^-1 mM^-1, and the paper's own efficiency cell for the same row is printed as 3.5 x 10^2 s^-1 M^-1.

raw_value_unit_evidence: Table 5, row K89L with substrate 2-Oxocaproic acid at pH 7.0: column 'Km (mM) in the '2-Oxocaproic acid' column group' prints 39.4 +/- 4.4; column 'kcat (s^-1) in the '2-Oxocaproic acid' column group' prints 13.8 +/- 1; column 'kcat/Km (s^-1 M^-1) in the '2-Oxocaproic acid' column group' prints 3.5 x 10^2.


column_label: Table 5: Comparison of kinetic parameters for three mutant enzymes with two monocarboxylic 2-oxoacid substrates (Eur. J. Biochem. 268, 5791-5799 (2001)); the enzyme label runs down the left edge and the six data columns form two groups of three, the group '2-Oxocaproic acid' then the group '2-Oxo-g-methiolbutyric acid', each carrying the column heads 'Km (mM)', 'kcat (s^-1)' and 'kcat/Km (s^-1 M^-1)'. Table 5, row K89L/A163G with substrate 2-Oxocaproic acid at pH 7.0: column 'Km (mM) in the '2-Oxocaproic acid' column group' = 5.97 +/- 0.37; column 'kcat (s^-1) in the '2-Oxocaproic acid' column group' = 13.9 +/- 0.5; column 'kcat/Km (s^-1 M^-1) in the '2-Oxocaproic acid' column group' = 2.33 x 10^3.

normalized_value_unit_evidence: Km: printed cell 5.97 +/- 0.37 in the column head 'Km (mM) in the '2-Oxocaproic acid' column group'; the unit is already mM, so no unit conversion applies and the paper value is 5.97 mM. kcat: printed cell 13.9 +/- 0.5 in the column head 'kcat (s^-1) in the '2-Oxocaproic acid' column group'; the unit is already s^-1, so no unit conversion applies and the paper value is 13.9 s^(-1). kcat/Km: printed cell 2.33 x 10^3 in the column head 'kcat/Km (s^-1 M^-1) in the '2-Oxocaproic acid' column group'; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.33 x 10^3 / 1000 = 2.33 s^-1 mM^-1. Closure reading: the quotient of the two printed component cells is 13.9 / 5.97 = 2.328308207705193 s^-1 mM^-1, and the paper's own efficiency cell for the same row is printed as 2.33 x 10^3 s^-1 M^-1.

raw_value_unit_evidence: Table 5, row K89L/A163G with substrate 2-Oxocaproic acid at pH 7.0: column 'Km (mM) in the '2-Oxocaproic acid' column group' prints 5.97 +/- 0.37; column 'kcat (s^-1) in the '2-Oxocaproic acid' column group' prints 13.9 +/- 0.5; column 'kcat/Km (s^-1 M^-1) in the '2-Oxocaproic acid' column group' prints 2.33 x 10^3.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P24295 and applied mutation signature K89L/S380A/A163G with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Table 5: Comparison of kinetic parameters for three mutant enzymes with two monocarboxylic 2-oxoacid substrates (Eur. J. Biochem. 268, 5791-5799 (2001)); the enzyme label runs down the left edge and the six data columns form two groups of three, the group '2-Oxocaproic acid' then the group '2-Oxo-g-methiolbutyric acid', each carrying the column heads 'Km (mM)', 'kcat (s^-1)' and 'kcat/Km (s^-1 M^-1)'. Table 5, row KSA/LAG (the triple mutant K89L/S380A/A163G) with substrate 2-Oxocaproic acid at pH 7.0: column 'Km (mM) in the '2-Oxocaproic acid' column group' = 5.5 +/- 0.18; column 'kcat (s^-1) in the '2-Oxocaproic acid' column group' = 11.2 +/- 0.2; column 'kcat/Km (s^-1 M^-1) in the '2-Oxocaproic acid' column group' = 2.04 x 10^3.

normalized_value_unit_evidence: Km: printed cell 5.5 +/- 0.18 in the column head 'Km (mM) in the '2-Oxocaproic acid' column group'; the unit is already mM, so no unit conversion applies and the paper value is 5.5 mM. kcat: printed cell 11.2 +/- 0.2 in the column head 'kcat (s^-1) in the '2-Oxocaproic acid' column group'; the unit is already s^-1, so no unit conversion applies and the paper value is 11.2 s^(-1). kcat/Km: printed cell 2.04 x 10^3 in the column head 'kcat/Km (s^-1 M^-1) in the '2-Oxocaproic acid' column group'; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.04 x 10^3 / 1000 = 2.04 s^-1 mM^-1. Closure reading: the quotient of the two printed component cells is 11.2 / 5.5 = 2.036363636363636 s^-1 mM^-1, and the paper's own efficiency cell for the same row is printed as 2.04 x 10^3 s^-1 M^-1.

raw_value_unit_evidence: Table 5, row KSA/LAG (the triple mutant K89L/S380A/A163G) with substrate 2-Oxocaproic acid at pH 7.0: column 'Km (mM) in the '2-Oxocaproic acid' column group' prints 5.5 +/- 0.18; column 'kcat (s^-1) in the '2-Oxocaproic acid' column group' prints 11.2 +/- 0.2; column 'kcat/Km (s^-1 M^-1) in the '2-Oxocaproic acid' column group' prints 2.04 x 10^3.


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

column_label: Table 5: Comparison of kinetic parameters for three mutant enzymes with two monocarboxylic 2-oxoacid substrates (Eur. J. Biochem. 268, 5791-5799 (2001)); the enzyme label runs down the left edge and the six data columns form two groups of three, the group '2-Oxocaproic acid' then the group '2-Oxo-g-methiolbutyric acid', each carrying the column heads 'Km (mM)', 'kcat (s^-1)' and 'kcat/Km (s^-1 M^-1)'. Table 5, row K89L with substrate 2-Oxo-g-methiolbutyric acid at pH 7.0: column 'Km (mM) in the '2-Oxo-g-methiolbutyric acid' column group' = 53.5 +/- 2.5; column 'kcat (s^-1) in the '2-Oxo-g-methiolbutyric acid' column group' = 8.82 +/- 0.25; column 'kcat/Km (s^-1 M^-1) in the '2-Oxo-g-methiolbutyric acid' column group' = 1.65 x 10^2.

normalized_value_unit_evidence: Km: printed cell 53.5 +/- 2.5 in the column head 'Km (mM) in the '2-Oxo-g-methiolbutyric acid' column group'; the unit is already mM, so no unit conversion applies and the paper value is 53.5 mM. kcat: printed cell 8.82 +/- 0.25 in the column head 'kcat (s^-1) in the '2-Oxo-g-methiolbutyric acid' column group'; the unit is already s^-1, so no unit conversion applies and the paper value is 8.82 s^(-1). kcat/Km: printed cell 1.65 x 10^2 in the column head 'kcat/Km (s^-1 M^-1) in the '2-Oxo-g-methiolbutyric acid' column group'; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.65 x 10^2 / 1000 = 0.165 s^-1 mM^-1. Closure reading: the quotient of the two printed component cells is 8.82 / 53.5 = 0.16485981308411216 s^-1 mM^-1, and the paper's own efficiency cell for the same row is printed as 1.65 x 10^2 s^-1 M^-1.

raw_value_unit_evidence: Table 5, row K89L with substrate 2-Oxo-g-methiolbutyric acid at pH 7.0: column 'Km (mM) in the '2-Oxo-g-methiolbutyric acid' column group' prints 53.5 +/- 2.5; column 'kcat (s^-1) in the '2-Oxo-g-methiolbutyric acid' column group' prints 8.82 +/- 0.25; column 'kcat/Km (s^-1 M^-1) in the '2-Oxo-g-methiolbutyric acid' column group' prints 1.65 x 10^2.


column_label: Table 5: Comparison of kinetic parameters for three mutant enzymes with two monocarboxylic 2-oxoacid substrates (Eur. J. Biochem. 268, 5791-5799 (2001)); the enzyme label runs down the left edge and the six data columns form two groups of three, the group '2-Oxocaproic acid' then the group '2-Oxo-g-methiolbutyric acid', each carrying the column heads 'Km (mM)', 'kcat (s^-1)' and 'kcat/Km (s^-1 M^-1)'. Table 5, row K89L/A163G with substrate 2-Oxo-g-methiolbutyric acid at pH 7.0: column 'Km (mM) in the '2-Oxo-g-methiolbutyric acid' column group' = 6.6 +/- 0.36; column 'kcat (s^-1) in the '2-Oxo-g-methiolbutyric acid' column group' = 9.6 +/- 0.3; column 'kcat/Km (s^-1 M^-1) in the '2-Oxo-g-methiolbutyric acid' column group' = 1.45 x 10^3.

normalized_value_unit_evidence: Km: printed cell 6.6 +/- 0.36 in the column head 'Km (mM) in the '2-Oxo-g-methiolbutyric acid' column group'; the unit is already mM, so no unit conversion applies and the paper value is 6.6 mM. kcat: printed cell 9.6 +/- 0.3 in the column head 'kcat (s^-1) in the '2-Oxo-g-methiolbutyric acid' column group'; the unit is already s^-1, so no unit conversion applies and the paper value is 9.6 s^(-1). kcat/Km: printed cell 1.45 x 10^3 in the column head 'kcat/Km (s^-1 M^-1) in the '2-Oxo-g-methiolbutyric acid' column group'; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.45 x 10^3 / 1000 = 1.45 s^-1 mM^-1. Closure reading: the quotient of the two printed component cells is 9.6 / 6.6 = 1.4545454545454546 s^-1 mM^-1, and the paper's own efficiency cell for the same row is printed as 1.45 x 10^3 s^-1 M^-1.

raw_value_unit_evidence: Table 5, row K89L/A163G with substrate 2-Oxo-g-methiolbutyric acid at pH 7.0: column 'Km (mM) in the '2-Oxo-g-methiolbutyric acid' column group' prints 6.6 +/- 0.36; column 'kcat (s^-1) in the '2-Oxo-g-methiolbutyric acid' column group' prints 9.6 +/- 0.3; column 'kcat/Km (s^-1 M^-1) in the '2-Oxo-g-methiolbutyric acid' column group' prints 1.45 x 10^3.


column_label: Table 5: Comparison of kinetic parameters for three mutant enzymes with two monocarboxylic 2-oxoacid substrates (Eur. J. Biochem. 268, 5791-5799 (2001)); the enzyme label runs down the left edge and the six data columns form two groups of three, the group '2-Oxocaproic acid' then the group '2-Oxo-g-methiolbutyric acid', each carrying the column heads 'Km (mM)', 'kcat (s^-1)' and 'kcat/Km (s^-1 M^-1)'. Table 5, row KSA/LAG (the triple mutant K89L/S380A/A163G) with substrate 2-Oxo-g-methiolbutyric acid at pH 7.0: column 'Km (mM) in the '2-Oxo-g-methiolbutyric acid' column group' = 5.9 +/- 0.25; column 'kcat (s^-1) in the '2-Oxo-g-methiolbutyric acid' column group' = 6.6 +/- 0.15; column 'kcat/Km (s^-1 M^-1) in the '2-Oxo-g-methiolbutyric acid' column group' = 1.12 x 10^3.

normalized_value_unit_evidence: Km: printed cell 5.9 +/- 0.25 in the column head 'Km (mM) in the '2-Oxo-g-methiolbutyric acid' column group'; the unit is already mM, so no unit conversion applies and the paper value is 5.9 mM. kcat: printed cell 6.6 +/- 0.15 in the column head 'kcat (s^-1) in the '2-Oxo-g-methiolbutyric acid' column group'; the unit is already s^-1, so no unit conversion applies and the paper value is 6.6 s^(-1). kcat/Km: printed cell 1.12 x 10^3 in the column head 'kcat/Km (s^-1 M^-1) in the '2-Oxo-g-methiolbutyric acid' column group'; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.12 x 10^3 / 1000 = 1.12 s^-1 mM^-1. Closure reading: the quotient of the two printed component cells is 6.6 / 5.9 = 1.11864406779661 s^-1 mM^-1, and the paper's own efficiency cell for the same row is printed as 1.12 x 10^3 s^-1 M^-1.

raw_value_unit_evidence: Table 5, row KSA/LAG (the triple mutant K89L/S380A/A163G) with substrate 2-Oxo-g-methiolbutyric acid at pH 7.0: column 'Km (mM) in the '2-Oxo-g-methiolbutyric acid' column group' prints 5.9 +/- 0.25; column 'kcat (s^-1) in the '2-Oxo-g-methiolbutyric acid' column group' prints 6.6 +/- 0.15; column 'kcat/Km (s^-1 M^-1) in the '2-Oxo-g-methiolbutyric acid' column group' prints 1.12 x 10^3.


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


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +14, so it is treated as a source-provided variant sequence.


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.


sequence_variant_note: Mutation signature E279R could not be applied safely because the resolved sequence does not match the expected reference residue(s).


column_label: Table III; row Wild-type; column kcat. Table IV; row Wild-type; columns Km-Glu and kcat/Km.

normalized_value_unit_evidence: normalized paper cells: kcat=65 s^-1; Km(L-Glutamate)=3.44 mM; kcat/Km(L-Glutamate)=18.90 s^-1 mM^-1. Export/sheet values: kcat=65 s^(-1); Km=3.44 mM; kcat/Km=18.8953488372093 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table III row Wild-type: kcat=65 s^-1. Table IV row Wild-type: Km-Glu=3.44 mM; kcat/Km=18.90 s^-1 mM^-1.

row_label: Wild-type

table_label: Table IV plus Table III kcat column


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

assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH


column_label: Table III (Michaelis Constants for a-Ketoglutarate and NH4Cl of Wild-Type and Mutant Glutamate Dehydrogenases), row 'wild type'; column 'Km-aKG (uM)' = 270; the turnover number is the same enzyme's Table II (Km-NADPH and kcat for Wild-Type and Mutant Enzymes) row 'wild type', column 'kcat (min^-1)', sub-column 'av' = 11.4 x 10^3; neither table prints a kcat/Km cell for a-ketoglutarate.

normalized_value_unit_evidence: Km: printed Table III Km-aKG cell 270 uM; 270 / 1000 = 0.27 mM. kcat: printed Table II kcat(av) cell 11.4 x 10^3 min^-1; 1 min^-1 is 1/60 s^-1, so 11400 / 60 = 190.0 s^(-1). kcat/Km: no cell is printed for a-ketoglutarate, so the paper value 703.7037037037037 s^(-1)*mM^(-1) is the quotient 190.0 / 0.27 of the two printed cells above and is typed derived_same_measurement.

raw_value_unit_evidence: Table III, row 'wild type': Km-aKG = 270 uM; Table II, row 'wild type': kcat(av) = 11.4 x 10^3 min^-1; no kcat/Km cell is printed for a-ketoglutarate in either table.

row_label: Table III, row 'wild type'

table_label: Table III: Michaelis Constants for a-Ketoglutarate and NH4Cl of Wild-Type and Mutant Glutamate Dehydrogenases (Biochemistry 1992, 31(34):7807-7814)


column_label: Table IV (Comparison of NADPH and NADH as Coenzymes for Wild-Type and Mutant Glutamate Dehydrogenases), row 'wild type', NADH columns; column 'Km (uM)', NADH = 2000; column 'kcat (min^-1) x 10^-3', NADH = 1.22 (i.e. 1.22 x 10^3 min^-1); column 'kcat/Km (min^-1 uM^-1)', NADH = 0.62.

raw_value_unit_evidence: Table IV, row 'wild type', NADH columns: Km = 2000 uM; kcat = 1.22 x 10^3 min^-1 (printed 1.22 under the head kcat (min^-1) x 10^-3); printed kcat/Km = 0.62 min^-1 uM^-1.

row_label: Table IV, row 'wild type', NADH columns

table_label: Table IV: Comparison of NADPH and NADH as Coenzymes for Wild-Type and Mutant Glutamate Dehydrogenases (Biochemistry 1992, 31(34):7807-7814)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K286Q to reconstruct the assayed variant sequence.


organism: Alkalihalophilus pseudofirmus

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K73A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K73E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K73Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K73Y to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 10.5; 313.15 K; cofactor NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K73F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K73R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K73S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00370 and applied mutation signature C321A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 295.15 K; buffer 50 mM Tris-HCl; cofactor NADP+

column_label: Table 1 (Kinetic constants of wild-type GDH and mutants) is transposed relative to the usual layout: the enzyme forms run across its columns and the metrics run down its lines, in two blocks of Vmax / Km / Kcat, the first block measured with NADP+ as the varied substrate and the second with Glu. This export row reads the column headed 'C321A' of the Glu block: line 'Glu Km (mM)' = 0.6; line 'Kcat (s^-1)' of that block = 6.7; line 'Vmax (uM min^-1)' of that block = 1.6, which the export schema does not carry in these units. There is no kcat/Km line in the table.

normalized_value_unit_evidence: kcat: printed Table 1 cell 6.7 s^-1; already in s^-1, so no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 6.7 s^(-1). Km: printed Table 1 cell 0.6 mM; the 'Glu Km (mM)' head is set entirely in the article's Latin text font and prints milli-molar, so no unit conversion applies; the paper value is 0.6 mM. kcat/Km: Table 1 has no catalytic-efficiency line, so the paper value 11.166666666666668 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 6.7 / 0.6 of this column's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1 (Kinetic constants of wild-type GDH and mutants), column 'C321A': the 'Glu Km (mM)' line reads 0.6 and the 'Kcat (s^-1)' line of the same Glu block reads 6.7. Table 1 carries no catalytic-efficiency line, so it prints no kcat/Km cell for this column.

row_label: Table 1, column 'C321A', varied-substrate block Glu

table_label: Table 1: Kinetic constants of wild-type GDH and mutants (Biochem Biophys Res Commun 2019, 509(1):262-267)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00370 and applied mutation signature K341L to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic constants of wild-type GDH and mutants) is transposed relative to the usual layout: the enzyme forms run across its columns and the metrics run down its lines, in two blocks of Vmax / Km / Kcat, the first block measured with NADP+ as the varied substrate and the second with Glu. This export row reads the column headed 'K341L' of the Glu block: line 'Glu Km (mM)' = 0.24; line 'Kcat (s^-1)' of that block = 19.6; line 'Vmax (uM min^-1)' of that block = 4.7, which the export schema does not carry in these units. There is no kcat/Km line in the table.

normalized_value_unit_evidence: kcat: printed Table 1 cell 19.6 s^-1; already in s^-1, so no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 19.6 s^(-1). Km: printed Table 1 cell 0.24 mM; the 'Glu Km (mM)' head is set entirely in the article's Latin text font and prints milli-molar, so no unit conversion applies; the paper value is 0.24 mM. kcat/Km: Table 1 has no catalytic-efficiency line, so the paper value 81.66666666666667 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 19.6 / 0.24 of this column's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1 (Kinetic constants of wild-type GDH and mutants), column 'K341L': the 'Glu Km (mM)' line reads 0.24 and the 'Kcat (s^-1)' line of the same Glu block reads 19.6. Table 1 carries no catalytic-efficiency line, so it prints no kcat/Km cell for this column.

row_label: Table 1, column 'K341L', varied-substrate block Glu


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00370 and applied mutation signature P320A to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic constants of wild-type GDH and mutants) is transposed relative to the usual layout: the enzyme forms run across its columns and the metrics run down its lines, in two blocks of Vmax / Km / Kcat, the first block measured with NADP+ as the varied substrate and the second with Glu. This export row reads the column headed 'P320A' of the Glu block: line 'Glu Km (mM)' = 0.9; line 'Kcat (s^-1)' of that block = 9.6; line 'Vmax (uM min^-1)' of that block = 2.3, which the export schema does not carry in these units. There is no kcat/Km line in the table.

normalized_value_unit_evidence: kcat: printed Table 1 cell 9.6 s^-1; already in s^-1, so no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 9.6 s^(-1). Km: printed Table 1 cell 0.9 mM; the 'Glu Km (mM)' head is set entirely in the article's Latin text font and prints milli-molar, so no unit conversion applies; the paper value is 0.9 mM. kcat/Km: Table 1 has no catalytic-efficiency line, so the paper value 10.666666666666666 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 9.6 / 0.9 of this column's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1 (Kinetic constants of wild-type GDH and mutants), column 'P320A': the 'Glu Km (mM)' line reads 0.9 and the 'Kcat (s^-1)' line of the same Glu block reads 9.6. Table 1 carries no catalytic-efficiency line, so it prints no kcat/Km cell for this column.

row_label: Table 1, column 'P320A', varied-substrate block Glu


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

assay_conditions_summary: pH 8; 295.15 K; cofactor NADP+

column_label: Wild GDH column; L-glutamate block Vmax, Km, and kcat cells

normalized_value_unit_evidence: Wild GDH / L-glutamate has kcat 17.1 s^-1, Km 0.45 mM, and exact same-measurement quotient 38.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 Wild GDH / L-glutamate block: Vmax 4.1 micromolar min^-1; Km 0.45 mM; kcat 17.1 s^-1; no kcat/Km ratio cell was printed.

row_label: Wild GDH / L-glutamate block

table_label: Table 1. Kinetic constants of wild-type GDH and mutants.


substrate_name: NADP+

column_label: Table 1 (Kinetic constants of wild-type GDH and mutants) is transposed relative to the usual layout: the enzyme forms run across its columns and the metrics run down its lines, in two blocks of Vmax / Km / Kcat, the first block measured with NADP+ as the varied substrate and the second with Glu. This export row reads the column headed 'C321A' of the NADP+ block: line 'NADP+ Km (mM)' = 0.15; line 'Kcat (s^-1)' of that block = 8.8; line 'Vmax (uM min^-1)' of that block = 2.1, which the export schema does not carry in these units. There is no kcat/Km line in the table.

normalized_value_unit_evidence: kcat: printed Table 1 cell 8.8 s^-1; already in s^-1, so no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 8.8 s^(-1). Km: printed Table 1 cell 0.15 mM; the 'NADP+ Km (mM)' head is set entirely in the article's Latin text font and prints milli-molar, so no unit conversion applies; the paper value is 0.15 mM. kcat/Km: Table 1 has no catalytic-efficiency line, so the paper value 58.66666666666667 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 8.8 / 0.15 of this column's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1 (Kinetic constants of wild-type GDH and mutants), column 'C321A': the 'NADP+ Km (mM)' line reads 0.15 and the 'Kcat (s^-1)' line of the same NADP+ block reads 8.8. Table 1 carries no catalytic-efficiency line, so it prints no kcat/Km cell for this column.

row_label: Table 1, column 'C321A', varied-substrate block NADP+

substrate: NADP+


column_label: Table 1 (Kinetic constants of wild-type GDH and mutants) is transposed relative to the usual layout: the enzyme forms run across its columns and the metrics run down its lines, in two blocks of Vmax / Km / Kcat, the first block measured with NADP+ as the varied substrate and the second with Glu. This export row reads the column headed 'K341L' of the NADP+ block: line 'NADP+ Km (mM)' = 0.13; line 'Kcat (s^-1)' of that block = 20.4; line 'Vmax (uM min^-1)' of that block = 4.9, which the export schema does not carry in these units. There is no kcat/Km line in the table.

normalized_value_unit_evidence: kcat: printed Table 1 cell 20.4 s^-1; already in s^-1, so no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 20.4 s^(-1). Km: printed Table 1 cell 0.13 mM; the 'NADP+ Km (mM)' head is set entirely in the article's Latin text font and prints milli-molar, so no unit conversion applies; the paper value is 0.13 mM. kcat/Km: Table 1 has no catalytic-efficiency line, so the paper value 156.9230769230769 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 20.4 / 0.13 of this column's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1 (Kinetic constants of wild-type GDH and mutants), column 'K341L': the 'NADP+ Km (mM)' line reads 0.13 and the 'Kcat (s^-1)' line of the same NADP+ block reads 20.4. Table 1 carries no catalytic-efficiency line, so it prints no kcat/Km cell for this column.

row_label: Table 1, column 'K341L', varied-substrate block NADP+


column_label: Table 1 (Kinetic constants of wild-type GDH and mutants) is transposed relative to the usual layout: the enzyme forms run across its columns and the metrics run down its lines, in two blocks of Vmax / Km / Kcat, the first block measured with NADP+ as the varied substrate and the second with Glu. This export row reads the column headed 'P320A' of the NADP+ block: line 'NADP+ Km (mM)' = 0.3; line 'Kcat (s^-1)' of that block = 9.2; line 'Vmax (uM min^-1)' of that block = 2.2, which the export schema does not carry in these units. There is no kcat/Km line in the table.

normalized_value_unit_evidence: kcat: printed Table 1 cell 9.2 s^-1; already in s^-1, so no unit conversion applies (this paper prints no min^-1 kinetic cell); the paper value is 9.2 s^(-1). Km: printed Table 1 cell 0.3 mM; the 'NADP+ Km (mM)' head is set entirely in the article's Latin text font and prints milli-molar, so no unit conversion applies; the paper value is 0.3 mM. kcat/Km: Table 1 has no catalytic-efficiency line, so the paper value 30.666666666666664 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 9.2 / 0.3 of this column's own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1 (Kinetic constants of wild-type GDH and mutants), column 'P320A': the 'NADP+ Km (mM)' line reads 0.3 and the 'Kcat (s^-1)' line of the same NADP+ block reads 9.2. Table 1 carries no catalytic-efficiency line, so it prints no kcat/Km cell for this column.

row_label: Table 1, column 'P320A', varied-substrate block NADP+


column_label: Wild GDH column; NADP+ block Vmax, Km, and kcat cells

normalized_value_unit_evidence: Wild GDH / NADP+ has kcat 16.7 s^-1, Km 0.07 mM, and exact same-measurement quotient 238.57142857142853 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 Wild GDH / NADP+ block: Vmax 4.0 micromolar min^-1; Km 0.07 mM; kcat 16.7 s^-1; no kcat/Km ratio cell was printed.

row_label: Wild GDH / NADP+ block


organism: Pyrococcus horikoshii

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


assay_conditions_summary: pH 7.6; cofactor NADH


assay_conditions_summary: pH 7.6; cofactor NADPH


assay_conditions_summary: pH 7.6; cofactor NADP+


column_label: Table 1; 2-Oxoglutarate row; Apparent Km (mM) column = 0.53 +/- 0.019; kcat (s^-1) column = 165.3 +/- 5.15; no separate kcat/Km column is printed.

raw_value_unit_evidence: Table 1 2-Oxoglutarate row reports Apparent Km = 0.53 +/- 0.019 mM and kcat = 165.3 +/- 5.15 s^-1.

row_label: 2-Oxoglutarate row; Apparent Km and kcat columns

table_label: PMID 12590923, Table 1: Km values of Pho-GDH for various substrates


column_label: Table 1; L-Glutamate row; Apparent Km (mM) column = 0.60 +/- 0.032; kcat (s^-1) column = 121.2 +/- 3.63; no separate kcat/Km column is printed.

raw_value_unit_evidence: Table 1 L-Glutamate row reports Apparent Km = 0.60 +/- 0.032 mM and kcat = 121.2 +/- 3.63 s^-1.

row_label: L-Glutamate row; Apparent Km and kcat columns


assay_conditions_summary: pH 7.6; 363.15 K; buffer pH 7; cofactor NADH

column_label: Table 1; NADH row; Apparent Km (mM) column = 0.083 +/- 0.004; kcat (s^-1) column = 374.5 +/- 17.74; no separate kcat/Km column is printed.

raw_value_unit_evidence: Table 1 NADH row reports Apparent Km = 0.083 +/- 0.004 mM and kcat = 374.5 +/- 17.74 s^-1.

row_label: NADH row; Apparent Km and kcat columns


assay_conditions_summary: pH 7.6; 363.15 K; buffer pH 7; cofactor NADP+

column_label: Table 1; NADP row; Apparent Km (mM) column = 0.025 +/- 0.003; kcat (s^-1) column = 399.6 +/- 31.20; no separate kcat/Km column is printed.

raw_value_unit_evidence: Table 1 NADP row reports Apparent Km = 0.025 +/- 0.003 mM and kcat = 399.6 +/- 31.20 s^-1.

row_label: NADP row; Apparent Km and kcat columns


organism: Homo sapiens

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -2, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G96Y with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature K94Y could not be applied safely because the resolved sequence does not match the expected reference residue(s).


assay_conditions_summary: pH 9.5; 298.15 K; cofactor ADP


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K118Y with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +5, so it is treated as a source-provided variant sequence.


column_label: Table 1; row hGDH2 / WT; columns kcat, Km (NAD+), kcat/Km (NAD+)

raw_value_unit_evidence: Table 1 cells for hGDH2 WT, substrate NAD+: kcat=83 s^-1; Km=0.59 mM; kcat/Km=140.7 s^-1 mM^-1


assay_conditions_summary: pH 8; 298.15 K; cofactor NADH

column_label: FEBS Letters Table 1; row hGDH1 (wild type); columns kcat, Km-alpha-KG, kcat/Km-alpha-KG

normalized_value_unit_evidence: kcat normalized_value=104.0 normalized_unit=s^-1; kcat/Km normalized_value=81.3 normalized_unit=s^-1*mM^-1; KM normalized_value=1.25 normalized_unit=mM; current_export_kcat=104.0 s^-1; current_export_kcat_over_km=85.9504132231405 s^-1*mM^-1; current_export_km=1.21 mM

raw_value_unit_evidence: kcat raw_value=104 raw_unit=s^-1; kcat/Km raw_value=81.3 raw_unit=s^-1 mM^-1; KM raw_value=1.25 raw_unit=mM

row_label: hGDH1 (wild type)

table_label: ScienceDirect / FEBS Letters Table 1 - Kinetic properties of hGDH1, hGDH2, and hGDH2 S443R mutant


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +10, so it is treated as a source-provided variant sequence.


column_label: FEBS Letters Table 1; row hGDH2 (wild type); columns kcat, Km-alpha-KG, kcat/Km-alpha-KG

normalized_value_unit_evidence: kcat normalized_value=130.0 normalized_unit=s^-1; kcat/Km normalized_value=93.5 normalized_unit=s^-1*mM^-1; KM normalized_value=1.39 normalized_unit=mM; current_export_kcat=130.0 s^-1; current_export_kcat_over_km=93.52517985611512 s^-1*mM^-1; current_export_km=1.39 mM

raw_value_unit_evidence: kcat raw_value=130 raw_unit=s^-1; kcat/Km raw_value=93.5 raw_unit=s^-1 mM^-1; KM raw_value=1.39 raw_unit=mM

row_label: hGDH2 (wild type)


column_label: FEBS Letters Table 1; row hGDH1 (wild type); columns kcat, Km-NADH, kcat/Km-NADH

normalized_value_unit_evidence: kcat normalized_value=104.0 normalized_unit=s^-1; kcat/Km normalized_value=1280.0 normalized_unit=s^-1*mM^-1; KM normalized_value=0.081 normalized_unit=mM; current_export_kcat=104.0 s^-1; current_export_kcat_over_km=1283.9506172839506 s^-1*mM^-1; current_export_km=0.081 mM

raw_value_unit_evidence: kcat raw_value=104 raw_unit=s^-1; kcat/Km raw_value=1.28 raw_unit=s^-1 uM^-1; KM raw_value=81 raw_unit=uM


column_label: FEBS Letters Table 1; row hGDH2 (wild type); columns kcat, Km-NADH, kcat/Km-NADH

normalized_value_unit_evidence: kcat normalized_value=130.0 normalized_unit=s^-1; kcat/Km normalized_value=1510.0 normalized_unit=s^-1*mM^-1; KM normalized_value=0.086 normalized_unit=mM; current_export_kcat=130.0 s^-1; current_export_kcat_over_km=1511.6279069767443 s^-1*mM^-1; current_export_km=0.086 mM

raw_value_unit_evidence: kcat raw_value=130 raw_unit=s^-1; kcat/Km raw_value=1.51 raw_unit=s^-1 uM^-1; KM raw_value=86 raw_unit=uM


organism: Bilophila wadsworthia

assay_conditions_summary: pH 9; cofactor NAD+

column_label: Abstract prose; row label: NADH; column label: apparent Km values; metric: Km; raw value: 0.04; raw unit: mM; normalized value: 0.04; normalized unit: mM; captured paper segment maps substrate order alanine, NAD+, pyruvate, ammonia, NADH to values 1.6, 0.15, 1.1, 31, 0.04 mM.

normalized_value_unit_evidence: Km 0.04 mM

raw_value_unit_evidence: Primary abstract prose: The apparent Km values for alanine, NAD+, pyruvate, ammonia and NADH were 1.6, 0.15, 1.1, 31 and 0.04 mM, respectively.

row_label: NADH

table_label: PMID 11041346 PubMed/Springer abstract kinetic-parameter prose


column_label: Abstract prose; row label: NAD+; column label: apparent Km values; metric: Km; raw value: 0.15; raw unit: mM; normalized value: 0.15; normalized unit: mM; captured paper segment maps substrate order alanine, NAD+, pyruvate, ammonia, NADH to values 1.6, 0.15, 1.1, 31, 0.04 mM.

normalized_value_unit_evidence: Km 0.15 mM

row_label: NAD+


substrate_name: pyruvate

column_label: Abstract prose; row label: pyruvate; column label: apparent Km values; metric: Km; raw value: 1.1; raw unit: mM; normalized value: 1.1; normalized unit: mM; captured paper segment maps substrate order alanine, NAD+, pyruvate, ammonia, NADH to values 1.6, 0.15, 1.1, 31, 0.04 mM.

normalized_value_unit_evidence: Km 1.1 mM

row_label: pyruvate


substrate_name: L-Ala

column_label: Abstract prose; row label: alanine / L-Ala synonym; column label: apparent Km values; metric: Km; raw value: 1.6; raw unit: mM; normalized value: 1.6; normalized unit: mM; captured paper segment maps substrate order alanine, NAD+, pyruvate, ammonia, NADH to values 1.6, 0.15, 1.1, 31, 0.04 mM.

normalized_value_unit_evidence: Km 1.6 mM

row_label: alanine / L-Ala synonym

substrate: L-Ala


column_label: Abstract prose; row label: ammonia / NH4+ synonym; column label: apparent Km values; metric: Km; raw value: 31; raw unit: mM; normalized value: 31; normalized unit: mM; captured paper segment maps substrate order alanine, NAD+, pyruvate, ammonia, NADH to values 1.6, 0.15, 1.1, 31, 0.04 mM.

normalized_value_unit_evidence: Km 31 mM

row_label: ammonia / NH4+ synonym


substrate_name: ammonia (at pH 9 and 35 degrees Celsius)

column_label: Abstract reports apparent Km values for alanine, NAD+, pyruvate, ammonia and NADH were 1.6, 0.15, 1.1, 31 and 0.04 mM, respectively.

raw_value_unit_evidence: Km raw_value=31 mM raw_unit=mM

row_label: Bilophila wadsworthia alanine dehydrogenase / ammonia

table_label: PubMed XML abstract PMID 11041346


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K286E with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K286Q with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K286R with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


column_label: Table II (Km-NADPH and kcat for Wild-Type and Mutant Enzymes), row 'wild type'; column 'Km (uM)' = 9.8; column 'kcat (min^-1)', sub-column 'av' = 11.4 x 10^3; column 'kcat(av)/Km (min^-1 uM^-1)' = 1.20 x 10^3.

raw_value_unit_evidence: Table II, row 'wild type': Km = 9.8 uM; kcat(av) = 11.4 x 10^3 min^-1; printed kcat(av)/Km = 1.20 x 10^3 min^-1 uM^-1.

row_label: Table II, row 'wild type'

table_label: Table II: Km-NADPH and kcat for Wild-Type and Mutant Enzymes (Biochemistry 1992, 31(34):7807-7814)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K278Q with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.


column_label: Table III (Michaelis Constants for a-Ketoglutarate and NH4Cl of Wild-Type and Mutant Glutamate Dehydrogenases), row 'wild type'; column 'Km-NH4Cl (mM)' = 3.6; the turnover number is the same enzyme's Table II (Km-NADPH and kcat for Wild-Type and Mutant Enzymes) row 'wild type', column 'kcat (min^-1)', sub-column 'av' = 11.4 x 10^3; neither table prints a kcat/Km cell for NH4Cl.

normalized_value_unit_evidence: Km: printed Table III Km-NH4Cl cell 3.6 mM; already in mM, no conversion; the paper value is 3.6 mM. kcat: printed Table II kcat(av) cell 11.4 x 10^3 min^-1; 1 min^-1 is 1/60 s^-1, so 11400 / 60 = 190.0 s^(-1). kcat/Km: no cell is printed for NH4Cl, so the paper value 52.77777777777778 s^(-1)*mM^(-1) is the quotient 190.0 / 3.6 of the two printed cells above and is typed derived_same_measurement.

raw_value_unit_evidence: Table III, row 'wild type': Km-NH4Cl = 3.6 mM; Table II, row 'wild type': kcat(av) = 11.4 x 10^3 min^-1; no kcat/Km cell is printed for NH4Cl in either table.

row_label: Table III, row 'wild type'


organism: Streptomyces fradiae

assay_conditions_summary: cofactor NADH

column_label: PMID 2917562 / DOI 10.1111/j.1432-1033.1989.tb14544.x, Wiley/PubMed abstract prose, reductive amination sentence, NADH Km metric.

raw_value_unit_evidence: Primary abstract prose reports reductive amination Km values of 0.23 mM for pyruvate, 11.6 mM for NH4+, and 0.05 mM for NADH.

row_label: reductive amination / NADH

table_label: Wiley/PubMed abstract prose


assay_conditions_summary: cofactor NAD+

column_label: PMID 2917562 / DOI 10.1111/j.1432-1033.1989.tb14544.x, Wiley/PubMed abstract prose, oxidative deamination sentence, NAD+ Km metric.

raw_value_unit_evidence: Primary abstract prose reports Km values of 10.0 mM for L-alanine and 0.18 mM for NAD+.

row_label: oxidative deamination / NAD+


column_label: PMID 2917562 / DOI 10.1111/j.1432-1033.1989.tb14544.x, Wiley/PubMed abstract prose, reductive amination sentence, pyruvate Km metric.

row_label: reductive amination / pyruvate

substrate: pyruvate


proof_lines:
alanine dehydrogenase
pyruvate
L-alanine


substrate_name: oxaloacetate

proof_lines:
alanine dehydrogenase
pyruvate
NADH

substrate: oxaloacetate


column_label: PMID 2917562 / DOI 10.1111/j.1432-1033.1989.tb14544.x, Wiley/PubMed abstract prose, oxidative deamination sentence, L-alanine Km metric.

row_label: oxidative deamination / L-alanine


column_label: PMID 2917562 / DOI 10.1111/j.1432-1033.1989.tb14544.x, Wiley/PubMed abstract prose, reductive amination sentence, NH4+ Km metric.

row_label: reductive amination / NH4+


organism: Phormidium lapideum

column_label: PDF page 997: substrate order L-alanine, NAD+, pyruvate, NH4+, NADH maps to Km values 5.0, 0.04, 0.33, 111, 0.02 mM

raw_value_unit_evidence: NADH apparent Km = 0.02 mM

row_label: NADH in apparent Km substrate list

table_label: Results - Substrate Specificity paragraph


assay_conditions_summary: 318.15 K; cofactor NAD+

source_databases_merged: brenda skid


raw_value_unit_evidence: pyruvate apparent Km = 0.33 mM

row_label: pyruvate in apparent Km substrate list


normalized_value_unit_evidence: km=5.0 mM

raw_value_unit_evidence: L-alanine apparent Km = 5.0 mM

row_label: L-alanine in apparent Km substrate list


normalized_value_unit_evidence: km=111 mM

raw_value_unit_evidence: NH4+ apparent Km = 111 mM

row_label: NH4+ in apparent Km substrate list


organism: Pyrobaculum calidifontis

assay_conditions_summary: pH 9.5; cofactor NADP+

column_label: Table 4 enzyme Pcal_1606, Oxidative deamination row NADP+; columns Km mM, kcat s^-1, kcat/Km mM^-1*s^-1; raw cells 0.035 +/- 0.0022, 9.9 +/- 0.33, 280; normalized cells 0.035 mM, 9.9 s^-1, 280 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.035 normalized_unit=mM; kcat normalized_value=9.9 normalized_unit=s^-1; kcat/Km normalized_value=280 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=0.035 +/- 0.0022 raw_unit=mM; kcat raw_value=9.9 +/- 0.33 raw_unit=s^-1; kcat/Km raw_value=280 raw_unit=mM^-1*s^-1

row_label: Pcal_1606 oxidative deamination / NADP+

table_label: Table 4. Kinetic constants


assay_conditions_summary: pH 9.5; 323.15 K; cofactor NADP+

column_label: Table 4 enzyme Pcal_1606, Oxidative deamination row L-Glutamate; columns Km mM, kcat s^-1, kcat/Km mM^-1*s^-1; raw cells 3.4 +/- 0.35, 13 +/- 0.61, 3.8; normalized cells 3.4 mM, 13 s^-1, 3.8 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=3.4 normalized_unit=mM; kcat normalized_value=13 normalized_unit=s^-1; kcat/Km normalized_value=3.8 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=3.4 +/- 0.35 raw_unit=mM; kcat raw_value=13 +/- 0.61 raw_unit=s^-1; kcat/Km raw_value=3.8 raw_unit=mM^-1*s^-1

row_label: Pcal_1606 oxidative deamination / L-Glutamate


substrate_name: NADPH

assay_conditions_summary: pH 9; 323.15 K; cofactor NADPH

column_label: Table 4 enzyme Pcal_1606, Reductive amination row NADPH; columns Km mM, kcat s^-1, kcat/Km mM^-1*s^-1; raw cells 0.017 +/- 0.0028, 92 +/- 5.6, 5400; normalized cells 0.017 mM, 92 s^-1, 5400 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.017 normalized_unit=mM; kcat normalized_value=92 normalized_unit=s^-1; kcat/Km normalized_value=5400 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=0.017 +/- 0.0028 raw_unit=mM; kcat raw_value=92 +/- 5.6 raw_unit=s^-1; kcat/Km raw_value=5400 raw_unit=mM^-1*s^-1

row_label: Pcal_1606 reductive amination / NADPH


assay_conditions_summary: pH 9; 323.15 K; cofactor NADP+

column_label: Table 4 enzyme Pcal_1606, Reductive amination row Ammonia; columns Km mM, kcat s^-1, kcat/Km mM^-1*s^-1; raw cells 2.2 +/- 0.071, 100 +/- 3.0, 45; normalized cells 2.2 mM, 100 s^-1, 45 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=2.2 normalized_unit=mM; kcat normalized_value=100 normalized_unit=s^-1; kcat/Km normalized_value=45 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=2.2 +/- 0.071 raw_unit=mM; kcat raw_value=100 +/- 3.0 raw_unit=s^-1; kcat/Km raw_value=45 raw_unit=mM^-1*s^-1

row_label: Pcal_1606 reductive amination / Ammonia


column_label: Table 4 enzyme Pcal_1606, Reductive amination row 2-Oxoglutarate; columns Km mM, kcat s^-1, kcat/Km mM^-1*s^-1; raw cells 1.7 +/- 0.45, 95 +/- 13, 56; normalized cells 1.7 mM, 95 s^-1, 56 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=1.7 normalized_unit=mM; kcat normalized_value=95 normalized_unit=s^-1; kcat/Km normalized_value=56 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=1.7 +/- 0.45 raw_unit=mM; kcat raw_value=95 +/- 13 raw_unit=s^-1; kcat/Km raw_value=56 raw_unit=mM^-1*s^-1

row_label: Pcal_1606 reductive amination / 2-Oxoglutarate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39633 and applied mutation signature Q144R to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.3; 310.15 K; buffer pH 7; cofactor NAD+

column_label: PDF Table 3 row Q144R; columns kcat 435; Km NADH 0.41; kcat/Km NADH 1060

normalized_value_unit_evidence: kcat normalized_value=435 s^-1; Km normalized_value=0.41 mM; kcat/Km normalized_value=1060.9756097560976 s^-1*mM^-1 from same-row 435/0.41

raw_value_unit_evidence: Q144R kcat raw_value=435 s^-1; Km raw_value=0.41 mM for NADH; printed kcat/Km NADH=1060

row_label: Q144R / NADH


column_label: PDF Table 3 row Wild-Type; columns kcat s^-1 342; Km mM NADH 0.07; kcat/Km s^-1 mM^-1 NADH printed 4890; exact calculated export efficiency 342/0.07=4885.714285714285

normalized_value_unit_evidence: kcat normalized_value=342 normalized_unit=s^-1; Km normalized_value=0.07 normalized_unit=mM; kcat/Km normalized_value=4885.714285714285 normalized_unit=s^-1*mM^-1 from same-row 342/0.07

raw_value_unit_evidence: kcat raw_value=342 raw_unit=s^-1; Km raw_value=0.07 raw_unit=mM; printed kcat/Km for NADH=4890 s^-1 mM^-1

row_label: Wild-Type / NADH


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P39633 and applied mutation signature E27F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.3; 310.15 K; buffer pH 7; cofactor NADH

column_label: PDF Table 3 row E27F; columns kcat 344 and Km NH4Cl 52.3

normalized_value_unit_evidence: kcat normalized_value=344 s^-1; Km normalized_value=52.3 mM; kcat/Km normalized_value=6.577437858508604 s^-1*mM^-1 from same-row 344/52.3

raw_value_unit_evidence: E27F kcat raw_value=344 s^-1; Km raw_value=52.3 mM for NH4Cl

row_label: E27F / NH4Cl


column_label: PDF Table 3 row Q144R; columns kcat 435 and Km NH4Cl 56.8

normalized_value_unit_evidence: kcat normalized_value=435 s^-1; Km normalized_value=56.8 mM; kcat/Km normalized_value=7.658450704225353 s^-1*mM^-1 from same-row 435/56.8

raw_value_unit_evidence: Q144R kcat raw_value=435 s^-1; Km raw_value=56.8 mM for NH4Cl

row_label: Q144R / NH4Cl


column_label: PDF Table 3 row Wild-Type; columns kcat s^-1 342; Km mM NH4Cl 55.6; exact calculated export efficiency 342/55.6=6.151079136690647

normalized_value_unit_evidence: kcat normalized_value=342 normalized_unit=s^-1; Km normalized_value=55.6 normalized_unit=mM; kcat/Km normalized_value=6.151079136690647 normalized_unit=s^-1*mM^-1 from same-row 342/55.6

raw_value_unit_evidence: kcat raw_value=342 raw_unit=s^-1; Km raw_value=55.6 raw_unit=mM for NH4Cl

row_label: Wild-Type / NH4Cl


substrate_name: L-glutamate


assay_conditions_summary: pH 9; 313.15 K; cofactor NAD+


assay_conditions_summary: pH 8.5; 313.15 K; cofactor NADH


organism: Thermococcus kodakaraensis

proof_lines:
glutamate production bias
KOD1 GDH


assay_conditions_summary: pH 7.6; 343.15 K; cofactor NADPH


assay_conditions_summary: pH 7.6; 353.15 K; cofactor NADP+

proof_lines:
NADH/NADPH coenzyme use
KOD1 GDH


proof_lines:
glutamate production bias
NADH/NADPH coenzyme use


organism: Benjaminiella poitrasii

assay_conditions_summary: pH 8; cofactor NADH

proof_lines:
NAD-dependent glutamate dehydrogenase
2-oxoglutarate
L-glutamate


assay_conditions_summary: pH 8; cofactor NAD+


assay_conditions_summary: pH 8


organism: Kitasatospora aureofaciens

assay_conditions_summary: pH 8.5; cofactor NADP+

column_label: Prose states Km values for reductive amination: NADH 0.029 mM.

raw_value_unit_evidence: Km value for NADH 0.029 mM.

row_label: NADH

table_label: Abstract/prose kinetic summary


assay_conditions_summary: pH 10; cofactor NADP+

column_label: Prose states oxidative deamination Km: NAD+ 0.11 mM.

raw_value_unit_evidence: Km value for NAD+ 0.11 mM.

row_label: NAD+


column_label: Prose states Km values for reductive amination: pyruvate 0.56 mM.

raw_value_unit_evidence: Km value for pyruvate was 0.56 mM.

row_label: pyruvate


column_label: Prose states oxidative deamination Km: L-alanine 5.0 mM.

normalized_value_unit_evidence: Km 5.0 mM.

raw_value_unit_evidence: Km value for L-alanine was 5.0 mM.

row_label: L-alanine


column_label: Prose states Km values for reductive amination: NH4Cl 6.67 mM.

raw_value_unit_evidence: Km value for NH4Cl 6.67 mM.

row_label: NH4Cl / NH4+


enzyme_display_name: leucine dehydrogenase

organism: Natrialba magadii

enzyme: leucine dehydrogenase


substrate_name: L-Leu

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

substrate: L-Leu


organism: Bacillus sp. (in: firmicutes)


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


enzyme_display_name: 2,4-diaminopentanoate dehydrogenase

organism: Acetoanaerobium sticklandii

enzyme: 2,4-diaminopentanoate dehydrogenase


enzyme_display_name: Amine dehydrogenase

organism: Petrotoga mobilis (strain DSM 10674 / SJ95)

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

enzyme: Amine dehydrogenase


enzyme_display_name: glutamate synthase (NADPH)

organism: [Brevibacterium] flavum

substrate_name: alpha-ketoglutarate

enzyme: glutamate synthase (NADPH)

substrate: alpha-ketoglutarate


substrate: NADPH


substrate_name: L-glutamine

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

substrate: L-glutamine


enzyme_display_name: UniProt Q05756

organism: Azospirillum brasilense

source_license: CC BY-NC-ND 4.0

enzyme: UniProt Q05756


enzyme_display_name: glutamate synthase (NADH)

organism: Chlamydomonas reinhardtii

enzyme: glutamate synthase (NADH)


organism: Prosthecochloris vibrioformis f. thiosulfatophilum


assay_conditions_summary: pH 10.5; 323.15 K; cofactor NAD+

column_label: Table label: Table 4 Kinetic constants. Row: Pcal_1031 | Oxidative deamination | L-Glutamate. Enzyme block: Pcal_1031, section Oxidative deamination. Columns read: Km (mM)a cell 5.3, kcat (s-1)a cell 17, kcat/Km (mM-1 s-1) cell 3.2. metric: kcat; raw value: 17; raw unit: s^-1; normalized value: 17.0 s^(-1); metric: Km; raw value: 5.3; raw unit: mM; normalized value: 5.3 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 3.207547169811321 s^-1 mM^-1; assay condition: Recombinant Pcal_1031, the NAD+-dependent glutamate dehydrogenase (EC 1.4.1.2) of Pyrobaculum calidifontis; the standard assay mixture for oxidative deamination (1 ml, pH 10.5 for Pcal_1031) contained 200 mM Gly-KOH, 50 mM L-glutamate, 1.25 mM NAD(P)+ and 60 nM protein; the standard assays were performed at 50 °C; per Table 4 footnote a, assays were performed at 50 °C, the enzyme was mixed with various concentrations of substrate, and Km and kcat were determined through nonlinear regression analysis of the assay data. Export row conditions: pH 10.5; 323.15 K.

normalized_value_unit_evidence: Pcal_1031 Oxidative deamination row L-Glutamate of Table 4: kcat 17 s^-1 = 17.0 s^(-1) (no conversion, table already in s^-1); Km 5.3 mM = 5.3 mM (no conversion, table already in mM); kcat/Km 3.207547169811321 s^-1 mM^-1 (the table's mM^-1 s^-1 is the same unit as s^-1 mM^-1). In the PDF text extract the superscript plus of NAD+ renders as ?, so the printed row label `NAD?` is the paper's NAD+; the kcat column header `kcat (s-1)a` is the flattened kcat (s^-1) with footnote marker a, the Km header `Km (mM)a` likewise carries footnote marker a, the plus-minus error terms render as ±, and the thousands separator renders as a comma, so the printed cell `5,800` is the paper's 5800.

raw_value_unit_evidence: Table 4 Kinetic constants | header row of Table 4: Enzyme Substrate Km (mM)a kcat (s-1)a kcat/Km (mM-1 s-1); enzyme block anchor rows: Pcal_1031 Oxidative deamination / Reductive amination | row: L-Glutamate 5.3 ± 0.49 17 ± 0.94 3.2 | Pcal_1031 Oxidative deamination cells read: kcat = 17 s^-1; Km = 5.3 mM; kcat/Km = 3.2 mM^-1 s^-1. Table 4 footnote a: Assays were performed at 50 °C as described in Materials and methods. In these assays, the enzyme was mixed with various concentrations of substrate. Km and kcat were determined through nonlinear regression analysis of the assay data.

table_label: Table 4 Kinetic constants

substrate: L-glutamate