organism: Homo sapiens

assay_conditions_summary: pH 8; 298.15 K; cofactor NADH

proof_lines: isozyme GDH1, in the presence of 1 mM ADP, in 50 mM triethanolamine, pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0, at 25°C

proof_lines: isozyme GDH2, in the presence of 1 mM ADP, in 50 mM triethanolamine, pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0, at 25°C


enzyme_display_name: glutamate dehydrogenase [NAD(P)+]

source_db: brenda

verification_status: unverified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

source_license: CC BY 4.0

km_unit: mM

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

enzyme: glutamate dehydrogenase [NAD(P)+]

status: unverified

source: brenda


enzyme_display_name: glutamate dehydrogenase

organism: Cucurbita pepo

enzyme: glutamate dehydrogenase


enzyme_display_name: glutamate dehydrogenase (NADP+)

organism: Lachancea kluyveri

enzyme: glutamate dehydrogenase (NADP+)


substrate_name: NADPH

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH

substrate: NADPH


smiles: N


organism: Aeropyrum pernix K1

proof_lines:
reductive amination
reductive amination at 50°C


proof_lines:
reductive amination
reductive amination at 70°C


organism: Leptolyngbya laminosa

assay_conditions_summary: cofactor NADPH


enzyme_display_name: serine 2-dehydrogenase

organism: Petroselinum crispum

substrate_name: Hydroxypyruvate

enzyme: serine 2-dehydrogenase

substrate: Hydroxypyruvate


enzyme_display_name: L-amino-acid dehydrogenase

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)

enzyme: L-amino-acid dehydrogenase

substrate: L-glutamine


substrate_name: L-methionine

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

substrate: L-methionine


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

substrate: L-glutamate


substrate_name: NADP+

assay_conditions_summary: 323.15 K; cofactor NADP+

proof_lines:
oxidative deamination
oxidative deamination at 50°C

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


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


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

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

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


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)


organism: Pseudomonas aeruginosa

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+

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

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.


substrate_name: NAD+


assay_conditions_summary: pH 8

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


substrate_name: L-glutamate


organism: Homo sapiens

substrate_name: NADH

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


substrate_name: NADPH

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

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

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

substrate: NADPH


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


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


organism: Homo sapiens

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+


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


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)(+)]

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.

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.


organism: Escherichia coli

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


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

assay_conditions_summary: pH 7.6; 343.15 K; cofactor NADP+

column_label: Table 3 (Kinetic parameters determined for glutamate dehydrogenase from Pyrococcus sp. KOD1), row '2-Oxoglutarate'; column 'Km (mM)' = 0.25; column 'kcat (x10^3/min)' = 11.7; column 'kcat/Km (x10^3/min per mM)' = 47.0.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.25 mM; the printed Km column is already in mM, so no unit conversion applies and the exported value is 0.25 mM. kcat: printed Table 3 cell 11.7 x 10^3 min^-1; 11700 / 60 = 195.0 s^-1, which is the exported kcat. kcat/Km: printed Table 3 cell 47.0 x 10^3 min^-1 mM^-1; one min^-1 mM^-1 is 1 / 60 s^-1 mM^-1, so 47000 / 60 = 783.3333333333334 s^-1 mM^-1, and 783.3333333333334 s^(-1)*mM^(-1) is the value this record installs.

raw_value_unit_evidence: Table 3, row 2-Oxoglutarate: Km = 0.25 mM; kcat = 11.7 x 10^3 min^-1; printed kcat/Km = 47.0 x 10^3 min^-1 mM^-1.

row_label: Table 3, row 2-Oxoglutarate

table_label: Table 3: Kinetic parameters determined for glutamate dehydrogenase from Pyrococcus sp. KOD1 (Mol Gen Genet 1998, 257:338-347)


proof_lines:
glutamate production bias
KOD1 GDH


assay_conditions_summary: pH 7.6; 343.15 K; cofactor NADPH

column_label: Table 3 (Kinetic parameters determined for glutamate dehydrogenase from Pyrococcus sp. KOD1), row 'NADH'; column 'Km (mM)' = 0.09; column 'kcat (x10^3/min)' = 5.4; column 'kcat/Km (x10^3/min per mM)' = 60.3.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.09 mM; the printed Km column is already in mM, so no unit conversion applies and the exported value is 0.09 mM. kcat: printed Table 3 cell 5.4 x 10^3 min^-1; 5400 / 60 = 90.0 s^-1, which is the exported kcat. kcat/Km: printed Table 3 cell 60.3 x 10^3 min^-1 mM^-1; one min^-1 mM^-1 is 1 / 60 s^-1 mM^-1, so 60300 / 60 = 1005.0 s^-1 mM^-1, and 1005.0 s^(-1)*mM^(-1) is the value this record installs.

raw_value_unit_evidence: Table 3, row NADH: Km = 0.09 mM; kcat = 5.4 x 10^3 min^-1; printed kcat/Km = 60.3 x 10^3 min^-1 mM^-1.

row_label: Table 3, row NADH


assay_conditions_summary: pH 7.6; 353.15 K; cofactor NADP+

column_label: Table 3 (Kinetic parameters determined for glutamate dehydrogenase from Pyrococcus sp. KOD1), row 'NADP+'; column 'Km (mM)' = 0.08; column 'kcat (x10^3/min)' = 6.1; column 'kcat/Km (x10^3/min per mM)' = 75.7.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.08 mM; the printed Km column is already in mM, so no unit conversion applies and the exported value is 0.08 mM. kcat: printed Table 3 cell 6.1 x 10^3 min^-1; 6100 / 60 = 101.66666666666667 s^-1, carried here at the exported precision as 101.667 s^-1. kcat/Km: printed Table 3 cell 75.7 x 10^3 min^-1 mM^-1; one min^-1 mM^-1 is 1 / 60 s^-1 mM^-1, so 75700 / 60 = 1261.6666666666667 s^-1 mM^-1, and 1261.6666666666667 s^(-1)*mM^(-1) is the value this record installs.

raw_value_unit_evidence: Table 3, row NADP+: Km = 0.08 mM; kcat = 6.1 x 10^3 min^-1; printed kcat/Km = 75.7 x 10^3 min^-1 mM^-1.

row_label: Table 3, row NADP+


column_label: Table 3 (Kinetic parameters determined for glutamate dehydrogenase from Pyrococcus sp. KOD1), row 'NADPH'; column 'Km (mM)' = 0.04; column 'kcat (x10^3/min)' = 6.7; column 'kcat/Km (x10^3/min per mM)' = 167.2.

normalized_value_unit_evidence: Km: printed Table 3 cell 0.04 mM; the printed Km column is already in mM, so no unit conversion applies and the exported value is 0.04 mM. kcat: printed Table 3 cell 6.7 x 10^3 min^-1; 6700 / 60 = 111.66666666666667 s^-1, carried here at the exported precision as 111.667 s^-1. kcat/Km: printed Table 3 cell 167.2 x 10^3 min^-1 mM^-1; one min^-1 mM^-1 is 1 / 60 s^-1 mM^-1, so 167200 / 60 = 2786.6666666666665 s^-1 mM^-1, and 2786.6666666666665 s^(-1)*mM^(-1) is the value this record installs.

raw_value_unit_evidence: Table 3, row NADPH: Km = 0.04 mM; kcat = 6.7 x 10^3 min^-1; printed kcat/Km = 167.2 x 10^3 min^-1 mM^-1.

row_label: Table 3, row NADPH


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


smiles: N


enzyme_display_name: 2,4-diaminopentanoate dehydrogenase

organism: Acetoanaerobium sticklandii

enzyme: 2,4-diaminopentanoate dehydrogenase