sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature M2T/V70K/E212G to reconstruct the assayed variant sequence.

proof_lines: M2T/V70K/E212G mutant protein, pH 9.0, 30°C


enzyme_display_name: pyridoxamine-pyruvate transaminase

organism: Mesorhizobium loti

source_db: brenda

verification_status: unverified

ki_display: Not reported

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y35H/V70K to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 9

data_origin: experimental

enzyme: pyridoxamine-pyruvate transaminase

status: unverified

source: brenda


substrate_name: L-glutamate

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y35H/V70R/F247C to reconstruct the assayed variant sequence.

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

proof_lines: Y35H/V70R/F247C mutant protein, pH 9.0, 30°C

substrate: L-glutamate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V70R/F247C to reconstruct the assayed variant sequence.


enzyme_display_name: UniProt B0F481

organism: Arabidopsis thaliana

substrate_name: S-adenosyl-L-methionine

source_db: skid

mutation_signature: Unknown

source_license: CC BY-NC-ND 4.0

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

enzyme: UniProt B0F481

substrate: S-adenosyl-L-methionine

source: skid


enzyme_display_name: UniProt P12995

organism: Escherichia coli

smiles: CC(C(=O)CCCCCC(=O)[O-])N

enzyme: UniProt P12995


enzyme_display_name: UniProt P9WQ81

organism: Mycobacterium tuberculosis

kcat_display: Not reported

kcat_over_km_display: Not reported

enzyme: UniProt P9WQ81


enzyme_display_name: glycine-oxaloacetate transaminase

organism: Paracoccus denitrificans

substrate_name: glyoxylate

sequence_source: multiple

proof_lines: pH 7.1, 25°C, with substrate L-aspartate

proof_lines: kcat is 58 sec(-1) for the transamination of glyoxylate using L-aspartate. kcat is 0.76 sec(-1) for the transamination of glycine using oxaloacetate. kcat is 8.8 sec(-1) for the transamination of glyoxylate using L-serine. kcat is 5.0 sec(-

source_databases_merged: brenda uniprot

enzyme: glycine-oxaloacetate transaminase

substrate: glyoxylate


substrate_name: L-aspartate

substrate: L-aspartate


organism: Paracoccus denitrificans (strain Pd 1222)

substrate_name: glycine

source_db: uniprot

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

substrate: glycine

source: uniprot


substrate_name: oxaloacetate

substrate: oxaloacetate


substrate_name: L-serine

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

substrate: L-serine


substrate_name: pyridoxamine

verification_status: corrected

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

normalized_value_unit_evidence: kcat normalized_value=28 normalized_unit=s^-1; Km normalized_value=0.044 normalized_unit=mM; kcat/Km ratio normalized_value=636.3636363636364 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 PM cells: kcat raw_value=28 +/- 0.5 raw_unit=s^-1; Km raw_value=0.044 +/- 0.004 raw_unit=mM; kcat/Km raw_value=640000 raw_unit=s^-1 M^-1.

row_label: PM

table_label: Table 1. Kinetic parameters of PPAT.

source_databases_merged: brenda skid uniprot

substrate: pyridoxamine

status: corrected


verification_status: verified

column_label: Official PMC Table 1 row (S)-2-Aminobutyrate: (S)-2-Aminobutyrate | Km 20 +/- 0.9 mM | kcat 9.0 +/- 0.2 s^-1 | kcat/Km 450 s^-1 M^-1.

normalized_value_unit_evidence: kcat normalized_value=9 normalized_unit=s^-1; Km normalized_value=20 normalized_unit=mM; kcat/Km ratio normalized_value=0.45 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 (S)-2-Aminobutyrate cells: kcat raw_value=9.0 +/- 0.2 raw_unit=s^-1; Km raw_value=20 +/- 0.9 raw_unit=mM; kcat/Km raw_value=450 raw_unit=s^-1 M^-1.

status: verified


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

column_label: Official PMC Table 1 row 2-Oxobutyrate: 2-Oxobutyrate | Km 7.1 +/- 0.1 mM | kcat 24 +/- 0.2 s^-1 | kcat/Km 3400 s^-1 M^-1.

normalized_value_unit_evidence: kcat normalized_value=24 normalized_unit=s^-1; Km normalized_value=7.1 normalized_unit=mM; kcat/Km ratio normalized_value=3.3802816901408455 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 2-Oxobutyrate cells: kcat raw_value=24 +/- 0.2 raw_unit=s^-1; Km raw_value=7.1 +/- 0.1 raw_unit=mM; kcat/Km raw_value=3400 raw_unit=s^-1 M^-1.


substrate_name: pyruvate

column_label: Official PMC Table 1 row Pyruvate: Pyruvate | Km 0.34 +/- 0.02 mM | kcat 29 +/- 0.6 s^-1 | kcat/Km 85000 s^-1 M^-1.

normalized_value_unit_evidence: kcat normalized_value=29 normalized_unit=s^-1; Km normalized_value=0.34 normalized_unit=mM; kcat/Km ratio normalized_value=85.29411764705881 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 Pyruvate cells: kcat raw_value=29 +/- 0.6 raw_unit=s^-1; Km raw_value=0.34 +/- 0.02 raw_unit=mM; kcat/Km raw_value=85000 raw_unit=s^-1 M^-1.

row_label: Pyruvate

substrate: pyruvate


substrate_name: pyridoxal

normalized_value_unit_evidence: kcat normalized_value=41 normalized_unit=s^-1; Km normalized_value=0.059 normalized_unit=mM; kcat/Km ratio normalized_value=694.9152542372882 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 PL cells: kcat raw_value=41 +/- 0.8 raw_unit=s^-1; Km raw_value=0.059 +/- 0.005 raw_unit=mM; kcat/Km raw_value=690000 raw_unit=s^-1 M^-1.

row_label: PL

substrate: pyridoxal


substrate_name: L-alanine

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

column_label: Official PMC Table 1 row L-Alanine: L-Alanine | Km 11 +/- 0.6 mM | kcat 41 +/- 0.7 s^-1 | kcat/Km 3700 s^-1 M^-1.

normalized_value_unit_evidence: kcat normalized_value=41 normalized_unit=s^-1; Km normalized_value=11 normalized_unit=mM; kcat/Km ratio normalized_value=3.727272727272727 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 L-Alanine cells: kcat raw_value=41 +/- 0.7 raw_unit=s^-1; Km raw_value=11 +/- 0.6 raw_unit=mM; kcat/Km raw_value=3700 raw_unit=s^-1 M^-1.

row_label: L-Alanine

substrate: L-alanine


enzyme_display_name: UniProt P42588

substrate_name: 2-oxoglutaric acid

enzyme: UniProt P42588

substrate: 2-oxoglutaric acid


enzyme_display_name: UniProt A8IW39

organism: Chlamydomonas reinhardtii

substrate_name: tetrahydrodipicolinate

enzyme: UniProt A8IW39

substrate: tetrahydrodipicolinate


substrate_name: LL-diaminopimelate

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

proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.6
Raw SKiD Env: Temp=-----, pH=7.6

substrate: LL-diaminopimelate


enzyme_display_name: glutamine-phenylpyruvate transaminase

organism: Thermus thermophilus

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

enzyme: glutamine-phenylpyruvate transaminase


substrate_name: phenylpyruvate

substrate: phenylpyruvate


substrate_name: Indolepyruvate

substrate: Indolepyruvate


substrate_name: L-phenylalanine

substrate: L-phenylalanine


substrate_name: L-tyrosine

substrate: L-tyrosine


substrate_name: L-asparagine

substrate: L-asparagine


substrate_name: L-methionine

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

substrate: L-methionine


substrate_name: L-kynurenine

substrate: L-kynurenine


substrate_name: L-glutamine

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

substrate: L-glutamine


substrate_name: L-tryptophan

substrate: L-tryptophan


substrate_name: L-histidine

substrate: L-histidine


substrate_name: L-aspartate

substrate: L-aspartate


substrate_name: L-glutamate

substrate: L-glutamate


substrate_name: L-serine

substrate: L-serine


substrate_name: L-threonine

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

substrate: L-threonine


substrate_name: L-alanine

substrate: L-alanine


substrate_name: L-arginine

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

substrate: L-arginine


substrate_name: L-leucine

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

substrate: L-leucine


source_db: oed

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

source: oed


enzyme_display_name: kynurenine-glyoxylate transaminase

organism: Macaca fuscata

substrate_name: glyoxylate

enzyme: kynurenine-glyoxylate transaminase

substrate: glyoxylate


enzyme_display_name: 4-aminobutyrate--pyruvate transaminase

organism: Malus domestica

smiles: NCCCC(=O)O

enzyme: 4-aminobutyrate--pyruvate transaminase


smiles: O=CC(=O)O


substrate_name: pyruvate

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

substrate: pyruvate


enzyme_display_name: 4-aminobutyrate-pyruvate transaminase

enzyme: 4-aminobutyrate-pyruvate transaminase


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

proof_lines:
cosubstrate pyruvate, pH 9.0, 25°C
cosubstrate glyoxylate, pH 9.0, 25°C


organism: Rattus norvegicus

proof_lines:
cosubstrate L-alanine, 37°C
L-kynurenine, pH 8.0, 37°C


proof_lines:
cosubstrate L-serine, 37°C
cosubstrate L-histidine, 37°C
cosubstrate L-phenylalanine, 37°C


substrate_name: alanine

substrate: alanine


substrate_name: phenylalanine

substrate: phenylalanine


substrate_name: histidine

substrate: histidine


substrate_name: serine

substrate: serine


enzyme_display_name: UniProt F2XBU9

organism: Vibrio fluvialis

enzyme: UniProt F2XBU9


substrate_name: benzylamine

substrate: benzylamine


smiles: CCCCCN


smiles: C(CCC(=O)[O-])CC=O


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


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


enzyme_display_name: N6-acetyl-beta-lysine transaminase

organism: Pseudomonas sp.

enzyme: N6-acetyl-beta-lysine transaminase


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


organism: Nicotiana tabacum

proof_lines: pH 8.2, temperature not specified in the publication


enzyme_display_name: 2-aminohexanoate transaminase

organism: Candida guilliermondii var. membranaefaciens

substrate_name: L-norleucine

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

proof_lines: pH 7.8, 35°C, in the presence of 2-oxoglutarate

enzyme: 2-aminohexanoate transaminase

substrate: L-norleucine


proof_lines: pH 7.8, 35°C, in the presence of L-norleucine or L-leucine


substrate_name: L-kynurenine

substrate: L-kynurenine


enzyme_display_name: L-arginine:2-oxoglutarate transaminase

organism: Pimelobacter simplex

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

enzyme: L-arginine:2-oxoglutarate transaminase


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


substrate_name: spermidine

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

smiles: C(CCNCCCN)CN

mutation_type: substitution

proof_lines: mutant enzyme R797Q, in the presence of 100 mM bicarbonate, at pH 8.6 and 25°C

proof_lines: mutant enzyme R797Q, in the absence of bicarbonate, at pH 8.6 and 25°C

substrate: spermidine


proof_lines: wild type enzyme, in the presence of 100 mM bicarbonate, at pH 8.6 and 25°C

proof_lines: wild type enzyme, in the absence of bicarbonate, at pH 8.6 and 25°C


enzyme_display_name: Kynurenine aminotransferase

organism: Aedes aegypti

substrate_name: cysteine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate)

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

column_label: Table 1, row Cysteine, column Km (mM), cell 1.3 ± 0.6 mM

raw_value_unit_evidence: Table 1 row Cysteine, Km (mM) = 1.3 ± 0.6 mM

row_label: Cysteine

table_label: Table 1. Kinetic parameters of AeKAT towards different amino acids

enzyme: Kynurenine aminotransferase


substrate_name: tyrosine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate)

column_label: Table 1, row Tyrosine, column Km (mM), cell 0.9 ± 0.2 mM

raw_value_unit_evidence: Table 1 row Tyrosine, Km (mM) = 0.9 ± 0.2 mM

row_label: Tyrosine


substrate_name: glutamine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate)

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

column_label: Table 1, row Glutamine, column Km (mM), cell 3.8 ± 0.8 mM

raw_value_unit_evidence: Table 1 row Glutamine, Km (mM) = 3.8 ± 0.8 mM

row_label: Glutamine


substrate_name: methionine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate)

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

column_label: Table 1, row Methionine, column Km (mM), cell 1.4 ± 0.4 mM

raw_value_unit_evidence: Table 1 row Methionine, Km (mM) = 1.4 ± 0.4 mM

row_label: Methionine


substrate_name: histidine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate)

column_label: Table 1, row Histidine, column Km (mM), cell 1.5 ± 0.3 mM

raw_value_unit_evidence: Table 1 row Histidine, Km (mM) = 1.5 ± 0.3 mM

row_label: Histidine


substrate_name: phenylalanine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate)

column_label: Table 1, row Phenylalanine, column Km (mM), cell 3.5 ± 0.3 mM

raw_value_unit_evidence: Table 1 row Phenylalanine, Km (mM) = 3.5 ± 0.3 mM

row_label: Phenylalanine


substrate_name: kynurenine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate)

column_label: Table 1, row Kynurenine, column Km (mM), cell 4.3 ± 0.5 mM

raw_value_unit_evidence: Table 1 row Kynurenine, Km (mM) = 4.3 ± 0.5 mM

row_label: Kynurenine


substrate_name: asparagine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate)

column_label: Table 1, row Asparagine, column Km (mM), cell 6.1 ± 0.8 mM

raw_value_unit_evidence: Table 1 row Asparagine, Km (mM) = 6.1 ± 0.8 mM

row_label: Asparagine


substrate_name: tryptophan (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate)

column_label: Table 1, row Tryptophan, column Km (mM), cell 12.9 ± 4.2 mM

raw_value_unit_evidence: Table 1 row Tryptophan, Km (mM) = 12.9 ± 4.2 mM

row_label: Tryptophan


substrate_name: leucine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate)

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

column_label: Table 1, row Leucine, column Km (mM), cell 34.5 ± 7.5 mM

raw_value_unit_evidence: Table 1 row Leucine, Km (mM) = 34.5 ± 7.5 mM

row_label: Leucine


substrate_name: serine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate)

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

column_label: Table 1, row Serine, column Km (mM), cell 32.7 ± 7.9 mM

raw_value_unit_evidence: Table 1 row Serine, Km (mM) = 32.7 ± 7.9 mM

row_label: Serine


substrate_name: alanine (at 45 degrees Celsius, at pH 8.5 and with ketobutyrate as cosubstrate)

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

column_label: Table 1, row Alanine, column Km (mM), cell 246 ± 164 mM

raw_value_unit_evidence: Table 1 row Alanine, Km (mM) = 246 ± 164 mM

row_label: Alanine


substrate_name: amino-butyrate (at 45 degrees Celsius, at pH 8.5 and with pyruvate as cosubstrate)

smiles: CCCC(=O)ON

column_label: Table 1, row Amino-butyrate, column Km (mM), cell 92.7 ± 15.9 mM

raw_value_unit_evidence: Table 1 row Amino-butyrate, Km (mM) = 92.7 ± 15.9 mM

row_label: Amino-butyrate


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

proof_lines: forward reaction with glyoxylate, pH 9.0, 30°C

proof_lines: forward reaction with pyruvate, pH 9.0, 30°C


substrate_name: glyoxylate

proof_lines: forward reaction with 4-aminobutanoate, pH 9.0, 30°C

proof_lines: reverse reaction with L-alanine, pH 9.0, 30°C


substrate_name: pyruvate

column_label: Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Forward reaction / varied substrate pyruvate / fixed substrate GABA, column kcat s^-1, raw cell 10.6, normalized 10.6 s^-1; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Forward reaction / varied substrate pyruvate / fixed substrate GABA, column Km mM, raw cell 0.14+/-0.01, normalized 0.14 mM; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Forward reaction / varied substrate pyruvate / fixed substrate GABA, column kcat/Km s^-1 mM^-1, raw cell 76, normalized 76 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=10.6 normalized_unit=s^-1; Km normalized_value=0.14 normalized_unit=mM; kcat/Km normalized_value=76 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=10.6 raw_unit=s^-1 raw_cell=10.6; Km raw_value=0.14+/-0.01 raw_unit=mM raw_cell=0.14+/-0.01; kcat/Km raw_value=76 raw_unit=s^-1*mM^-1 raw_cell=76


substrate_name: succinate semialdehyde

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

column_label: Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Reverse reaction / varied substrate SSA (succinate semialdehyde) / fixed substrate alanine, column kcat s^-1, raw cell 10.8, normalized 10.8 s^-1; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Reverse reaction / varied substrate SSA (succinate semialdehyde) / fixed substrate alanine, column Km mM, raw cell 0.014+/-0.002, normalized 0.014 mM; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Reverse reaction / varied substrate SSA (succinate semialdehyde) / fixed substrate alanine, column kcat/Km s^-1 mM^-1, raw cell 770, normalized 770 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=10.8 normalized_unit=s^-1; Km normalized_value=0.014 normalized_unit=mM; kcat/Km normalized_value=770 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=10.8 raw_unit=s^-1 raw_cell=10.8; Km raw_value=0.014+/-0.002 raw_unit=mM raw_cell=0.014+/-0.002; kcat/Km raw_value=770 raw_unit=s^-1*mM^-1 raw_cell=770

substrate: succinate semialdehyde


substrate_name: L-alanine

proof_lines: reverse reaction with glyoxylate, pH 9.0, 30°C

proof_lines: reverse reaction with succinate semialdehyde, pH 9.0, 30°C


organism: Psychrobacter cryohalolentis

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

assay_conditions_summary: pH 8

proof_lines: pH 8.0, 35°C, with (S)-(-)-1-phenylethylamine


proof_lines:
pH 8.0, 35°C, with 2,3-butanedione
pH 8.0, 35°C, with isobutyraldehyde


substrate_name: Isobutyraldehyde

smiles: CC(C)C=O

substrate: Isobutyraldehyde


enzyme_display_name: UniProt Q9A9H3

organism: Caulobacter vibrioides

assay_conditions_summary: pH 7.5; 295.15 K; buffer C pH 7

column_label: Table 3 row GDP-4-keto-6-deoxymannose reaction reports Km sugar, kcat, and kcat/Km sugar in separate metric-labeled columns.

normalized_value_unit_evidence: Km 0.013 mM; kcat 2.7 s^-1; kcat/Km 210000 M^-1 s^-1 = 210 s^-1*mM^-1, consistent with expected 207.6923076923077 by rounding/uncertainty.

row_label: GDP-4-keto-6-deoxymannose reaction

table_label: PMC HTML Table 3, Kinetic Parameters for C. crescentus GDP-perosamine Synthase

source_databases_merged: skid uniprot

enzyme: UniProt Q9A9H3


column_label: Table 3 row GDP-4-keto-3,6-dideoxymannose reaction reports Km sugar, kcat, and kcat/Km sugar in separate metric-labeled columns.

normalized_value_unit_evidence: Km 0.016 mM; kcat 0.015 s^-1; kcat/Km 940 M^-1 s^-1 = 0.94 s^-1*mM^-1, consistent with expected 0.9375 by rounding/uncertainty.

raw_value_unit_evidence: Unnatural substrate row: Km sugar 0.016 +/- 0.003 mM; Km glutamate 0.13 +/- 0.02 mM; Ki sugar N/A; kcat 0.015 +/- 0.001 s^-1; kcat/Km sugar (9.4 +/- 1.8) x 10^2 M^-1 s^-1.

row_label: GDP-4-keto-3,6-dideoxymannose reaction


enzyme_display_name: GDP-perosamine synthase

organism: Vibrio cholerae serotype O1

column_label: Abstract reports His-tag RfbE has a Km of 0.06 mM for GDP-4-keto-6-deoxy-D-mannose.

raw_value_unit_evidence: Km raw_value=0.06 mM raw_unit=mM

row_label: Vibrio cholerae RfbE / GDP-4-keto-6-deoxy-D-mannose

table_label: PubMed XML abstract PMID 11479276

enzyme: GDP-perosamine synthase


substrate_name: L-glutamate

substrate: L-glutamate


enzyme_display_name: UDP-N-acetylbacillosamine transaminase

organism: Campylobacter jejuni subsp. jejuni serotype O:2 (strain ATCC 700819 / NCTC 11168)

enzyme: UDP-N-acetylbacillosamine transaminase


organism: Escherichia coli O157:H7

proof_lines: kcat is 18.98 sec(-1) for GDP-4-keto-6-deoxy-D-mannose. kcat is 10.41 sec(-1) for L-glutamate.


column_label: PMID 17888872, Table 1, row Km (mM), column Sodium-L-glutamate: 2.0 mM. Sodium-L-glutamate is the assayed form of the expected L-glutamate amino donor.

raw_value_unit_evidence: Table 1: Km (mM), Sodium-L-glutamate column, raw value 2.0 mM.

row_label: Km (mM)

table_label: Table 1. Kinetics parameters of GDP-perosamine synthetase


enzyme_display_name: 3-hydroxykynurenine transaminase

substrate_name: 3-hydroxykynurenine (at 50 degrees Celsius and pH 7.0)

assay_conditions_summary: pH 7

proof_lines: kcat is 2424 min(-1) for 3-hydroxykynurenine (at 50 degrees Celsius and pH 7) (PubMed:11880382). kcat is 1640 min(-1) for L-alanine (at 50 degrees Celsius, pH 7.0 and with glyoxylate as cosubstrate) (PubMed:11880382). kcat is 1200 min(-1) f

enzyme: 3-hydroxykynurenine transaminase


substrate_name: L-alanine (at 50 degrees Celsius, pH 7.0 and with glyoxylate as cosubstrate)


substrate_name: L-kynurenine (at 50 degrees Celsius and pH 7.0)


organism: Caulobacter vibrioides (strain ATCC 19089 / CIP 103742 / CB 15)

substrate_name: L-glutamate (with GDP-4-keto-6-deoxy-D-mannose as cosubstrate)

proof_lines: kcat is 2.7 sec(-1) for GDP-4-keto-6-deoxy-D-mannose. kcat is 0.015 sec(-1) for GDP-4-keto-3,6-dideoxymannose.


organism: Helicobacter pylori (strain ATCC 700392 / 26695)

proof_lines: kcat is 43 min(-1) with (2E,6E)-farnesyl UDP-2-acetamido-2,6-dideoxy-beta-L-arabino-4-hexulose as substrate.


substrate_name: glyoxylate (at 50 degrees Celsius, pH 7.0 and with alanine as cosubstrate)


enzyme_display_name: UniProt P19367

organism: Homo sapiens

substrate_name: D-glucose

km_display: Not reported

enzyme: UniProt P19367

substrate: D-glucose


enzyme_display_name: UniProt P04806

organism: Saccharomyces cerevisiae

enzyme: UniProt P04806


substrate_name: D-fructose

substrate: D-fructose


enzyme_display_name: UniProt P33284

organism: Kluyveromyces lactis

enzyme: UniProt P33284


substrate_name: ATP

substrate: ATP


proof_lines:
Raw SKiD Env: Temp=25°C, pH=-----
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=30°C, pH=7.5


enzyme_display_name: UniProt P17709

enzyme: UniProt P17709


organism: Zea mays

substrate_name: fructose

substrate: fructose


substrate_name: UTP

substrate: UTP


organism: Anopheles gambiae

proof_lines: kcat is 988.5 min(-1) for D,L-3-hydroxykynurenine (at 50 degrees Celsius, pH 7 and with glyoxylate as cosubstrate) (PubMed:16262702). kcat is 1077.2 min(-1) for D,L-kynurenine (at 50 degrees Celsius, pH 7 and with glyoxylate as cosubstrate)


substrate_name: glyoxylate (at 50 degrees Celsius, pH 7 and with D,L-3-hydroxykynurenine as cosubstrate)


enzyme_display_name: kynurenine---glyoxylate transaminase

organism: Rattus norvegicus

substrate_name: Glyoxylate; 3-Hydroxy-L-kynurenine

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

enzyme: kynurenine---glyoxylate transaminase

substrate: Glyoxylate; 3-Hydroxy-L-kynurenine


enzyme_display_name: Bifunctional dethiobiotin synthetase/7,8-diamino-pelargonic acid aminotransferase, mitochondrial

organism: Arabidopsis thaliana

substrate_name: Unknown

proof_lines: kcat is 0.072 min(-1) for 7,8-diamino-pelargonic acid aminotransferase + dethiobiotin synthetase activities, and 1.85 min(-1) for 7,8-diamino-pelargonic acid aminotransferase activity only (at pH 7.5 and 30 degrees Celsius).

substrate: Unknown


substrate_name: L,D-alanine (at 50 degrees Celsius, pH 7.0 and with glyoxylate as cosubstrate)


substrate_name: D,L-3-hydroxykynurenine (at 50 degrees Celsius, pH 7 and with glyoxylate as cosubstrate)


enzyme_display_name: Kynurenine--oxoglutarate transaminase 1

enzyme: Kynurenine--oxoglutarate transaminase 1


enzyme_display_name: 4-aminobutyrate---pyruvate transaminase

substrate_name: 4-Aminobutanoate; Pyruvate

proof_lines: forward reaction with 4-aminobutanoate and pyruvate, pH 9.0, 30°C

source_databases_merged: sabio_rk brenda uniprot

enzyme: 4-aminobutyrate---pyruvate transaminase

substrate: 4-Aminobutanoate; Pyruvate


enzyme_display_name: L-tryptophan-pyruvate aminotransferase

ki_unit: mM

proof_lines: inhibition of TAA1, competitive versus L-Tryp, pH not specificied in the publication, 55°C

enzyme: L-tryptophan-pyruvate aminotransferase


enzyme_display_name: hexokinase

organism: Aeropyrum pernix

assay_conditions_summary: pH 6.2; 363.15 K; cofactor ATP

enzyme: hexokinase


substrate_name: D-glucosamine

substrate: D-glucosamine


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


organism: Brugia malayi

substrate_name: D-Glucose; ATP

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

substrate: D-Glucose; ATP


organism: Mus musculus

assay_conditions_summary: cofactor ATP


substrate_name: alpha-D-Glucose 6-phosphate; ADP

assay_conditions_summary: cofactor ADP

substrate: alpha-D-Glucose 6-phosphate; ADP


substrate_name: alpha-D-Glucose; ATP

substrate: alpha-D-Glucose; ATP


substrate_name: ATP; alpha-D-Glucose

substrate: ATP; alpha-D-Glucose


organism: Bubalus bubalis


assay_conditions_summary: pH 8.1; 303.15 K; cofactor ATP

proof_lines:
MgATP2-, at 30°C, pH 8.1
at 30°C, pH 8.1


proof_lines:
at 30°C, pH 8.1
versus MgATP2-, at 30°C, pH 8.1
versus glucose, at 30°C, pH 8.1


organism: Mammalia

proof_lines:
type III isozyme
type I isozyme
type II isozyme


proof_lines:
type I isozyme
type II isozyme
type III isozyme


proof_lines:
type I and type II isozymes
type III isozyme


enzyme_display_name: ketohexokinase

organism: Haloarcula vallismortis

assay_conditions_summary: pH 9; 310.15 K; cofactor ATP

enzyme: ketohexokinase


enzyme_display_name: fructokinase

organism: Solanum tuberosum

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP

proof_lines:
FK 2, pH 8
FK 1, pH 8
isoenzyme FK-I, 25°C, pH 8.5

enzyme: fructokinase


proof_lines:
isoenzyme FK-I, 25°C, pH 8.5
FK 1, pH 8
FK 2, pH 8


substrate_name: GTP

proof_lines:
isoenzyme FK-I, 25°C, pH 8.5
isoenzyme FK-III, 25°C, pH 8.5
isoenzyme FK-II, 25°C, pH 8.5

substrate: GTP


substrate_name: CTP

substrate: CTP


proof_lines:
isoenzyme FK-III, 25°C, pH 8.5
isoenzyme FK-I, 25°C, pH 8.5
isoenzyme FK-II, 25°C, pH 8.5


substrate_name: D-Hexose; ATP

substrate: D-Hexose; ATP


organism: Trypanosoma cruzi


enzyme_display_name: glucokinase

substrate_name: Glucose; ATP

enzyme: glucokinase

substrate: Glucose; ATP


organism: Shewanella woodyi

substrate_name: D-glucose

substrate: D-glucose


organism: Catharanthus roseus

substrate_name: ATP

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP

proof_lines: with D-fructose as cosubstrate, pH 7.4, 30°C


substrate_name: D-fructose

substrate: D-fructose


substrate_name: UTP


substrate: ATP


organism: Brassica rapa subsp. oleifera

proof_lines:
isozyme HKII
isozyme HKI


organism: Littorina littorea

proof_lines: enzyme from hepatopancreas, 24 h anoxic conditions, pH 7.5, 22°C

proof_lines: enzyme from hepatopancreas, pH 7.5, 22°C


assay_conditions_summary: pH 7.5; 295.15 K; cofactor ATP


organism: Lithobates sylvaticus

proof_lines:
control, pH 8.2, 5°C, no glucose
control, pH 8.2, 25°C
control, pH 8.2, 25°C, no glucose


assay_conditions_summary: pH 8.2; 298.15 K; cofactor ATP

proof_lines:
control, pH 8.2, 25°C, 250 mM glucose
control, pH 8.2, 25°C
control, pH 8.2, 25°C, no glucose


organism: Ogataea angusta


assay_conditions_summary: pH 7.5; cofactor ATP


substrate_name: Unknown


organism: Lysinibacillus sphaericus


organism: Thermus thermophilus


organism: Paracoccus versutus


organism: Nicotiana tabacum

proof_lines: pH 8.4, 30°C, recombinant isozyme hexokinase 2


organism: Dictyostelium discoideum


assay_conditions_summary: pH 7; 293.15 K; cofactor ATP


organism: Asterias amurensis


organism: Thermococcus litoralis

assay_conditions_summary: pH 7.5; 353.15 K; cofactor ATP


organism: Saccharomyces cerevisiae


organism: Streptomyces violaceoruber


organism: Pisum sativum


organism: Acer pseudoplatanus


organism: Rattus norvegicus

substrate_name: 2-Deoxy-D-glucose; Phosphate

substrate: 2-Deoxy-D-glucose; Phosphate


organism: Yarrowia lipolytica


organism: Urocitellus undulatus

proof_lines: enzyme from active animals, S0.5 value, Hill coefficient 1.16, pH 7.8, 2°C

proof_lines: enzyme from active animals, S0.5 value, Hill coefficient 1.7, pH 7.8, 25°C

proof_lines: enzyme from hibernating animals, S0.5 value, Hill coefficient 1.6, pH 7.8, 25°C


organism: Zea mays

substrate_name: ATP; D-Glucose

substrate: ATP; D-Glucose


organism: Bufo marinus

substrate_name: ATP; Glucose

substrate: ATP; Glucose


substrate_name: ATP; D-Fructose

substrate: ATP; D-Fructose


organism: Camellia japonica


organism: Shewanella woodyi


organism: Lilium longiflorum


organism: Saccharum officinarum

substrate_name: D-Glucose; ATP


organism: Persea americana

substrate_name: fructose

substrate: fructose


organism: Sus scrofa


organism: Gleditsia triacanthos


substrate_name: D-Fructose; ATP

substrate: D-Fructose; ATP


organism: Entamoeba histolytica


assay_conditions_summary: pH 8; cofactor ATP


enzyme_display_name: UniProt P35557

organism: Homo sapiens

proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.4
Raw SKiD Env: Temp=37°C, pH=7.4
Raw SKiD Env: Temp=-----, pH=7.1

enzyme: UniProt P35557


assay_conditions_summary: pH 7; 310.15 K; cofactor ATP

proof_lines:
Raw SKiD Env: Temp=°C, pH=7.6
Raw SKiD Env: Temp=37°C, pH=7.4
Raw SKiD Env: Temp=30°C, pH=7.4


substrate_name: 2-deoxyglucose (at 30 degrees Celsius and pH 7.5)

proof_lines: kcat is 66.4 sec(-1) with glucose as substrate (at 30 degrees Celsius and pH 7.5) (PubMed:7742312). kcat is 56.4 sec(-1) with mannose as substrate (at 30 degrees Celsius and pH 7.5) (PubMed:7742312). kcat is 56.4 sec(-1) with 2-deoxyglucose


substrate_name: fructose (at 30 degrees Celsius and pH 7.5)


substrate_name: glucosamine (at 30 degrees Celsius and pH 9)

assay_conditions_summary: pH 9


organism: Sulfurisphaera tokodaii

assay_conditions_summary: pH 7.5; 323.15 K; cofactor ATP

proof_lines:
pH 7.5, 50°C, ATP as phosphoryl donor
pH 7.5, 50°C
Raw SKiD Env: Temp=50°C, pH=7.5

source_databases_merged: brenda skid


proof_lines: pH 7.5, 50°C, D-glucose as phosphoryl acceptor


substrate_name: D-glucosamine

substrate: D-glucosamine


substrate_name: N-acetyl-D-glucosamine

substrate: N-acetyl-D-glucosamine


substrate_name: CTP


substrate_name: D-glucose

sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature V452L to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.1; cofactor ATP

column_label: Table 1; row label: V452L; column label: kcat (sec^-1); raw value: 122.0; raw unit: sec^-1; normalized value: 122.0; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 122.0; normalized unit: s^-1

table_label: Table 1


substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature G68V to reconstruct the assayed variant sequence.

column_label: Table 1; row label: G68V; column label: ATP Km (mM); raw value: 0.31; raw unit: mM; normalized value: 0.31; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.31; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature V455M to reconstruct the assayed variant sequence.

column_label: Table 1; row label: V455M; column label: ATP Km (mM); raw value: 0.38; raw unit: mM; normalized value: 0.38; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.38; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature G68K to reconstruct the assayed variant sequence.

column_label: Table 1; row label: G68K; column label: ATP Km (mM); raw value: 0.39; raw unit: mM; normalized value: 0.39; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.39; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature M197E to reconstruct the assayed variant sequence.

column_label: Table 1; row label: M197E; column label: ATP Km (mM); raw value: 0.4; raw unit: mM; normalized value: 0.4; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.4; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature V91L to reconstruct the assayed variant sequence.

column_label: Table 1; row label: V91L; column label: ATP Km (mM); raw value: 0.48; raw unit: mM; normalized value: 0.48; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.48; normalized unit: mM


column_label: Table 1; row label: V452L; column label: ATP Km (mM); raw value: 0.53; raw unit: mM; normalized value: 0.53; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.53; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature G72R to reconstruct the assayed variant sequence.

column_label: Table 1; row label: G72R; column label: ATP Km (mM); raw value: 0.72; raw unit: mM; normalized value: 0.72; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.72; normalized unit: mM

raw_value_unit_evidence: raw value: 0.72 +−0.19; raw unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature C252Y to reconstruct the assayed variant sequence.

column_label: Table 1; row label: C252Y; column label: ATP Km (mM); raw value: 0.75; raw unit: mM; normalized value: 0.75; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.75; normalized unit: mM

raw_value_unit_evidence: raw value: 0.75; raw unit: mM


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

proof_lines: mutant enzyme Y61S, glutathione S-transferase glucokinase B fusion protein


proof_lines: mutant enzyme E265K, glutathione S-transferase glucokinase B fusion protein


proof_lines: mutant enzyme K420E, glutathione S-transferase glucokinase B fusion protein


proof_lines: mutant enzyme A379V, glutathione S-transferase glucokinase B fusion protein


organism: Mus musculus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A456V to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; cofactor ATP


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K414E with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature V389L to reconstruct the assayed variant sequence.

column_label: Table 1; row label: V389L; column label: ATP Km (mM); raw value: 0.76; raw unit: mM; normalized value: 0.76; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.76; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature A379T to reconstruct the assayed variant sequence.

column_label: Table 1; row label: A379T; column label: ATP Km (mM); raw value: 0.87; raw unit: mM; normalized value: 0.87; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.87; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature C213R to reconstruct the assayed variant sequence.

column_label: Table 1; row label: C213R; column label: ATP Km (mM); raw value: 0.89; raw unit: mM; normalized value: 0.89; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 0.89; normalized unit: mM

raw_value_unit_evidence: raw value: 0.89; raw unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature M197L to reconstruct the assayed variant sequence.

column_label: Table 1; row label: M197L; column label: ATP Km (mM); raw value: 1.31; raw unit: mM; normalized value: 1.31; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 1.31; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature M197I to reconstruct the assayed variant sequence.

column_label: Table 1; row label: M197I; column label: ATP Km (mM); raw value: 1.39; raw unit: mM; normalized value: 1.39; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 1.39; normalized unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature Y214A/V452A to reconstruct the assayed variant sequence.

column_label: Table 1; row label: Y214A/V452A; column label: ATP Km (mM); raw value: 1.42; raw unit: mM; normalized value: 1.42; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 1.42; normalized unit: mM

raw_value_unit_evidence: raw value: 1.42±0.29; raw unit: mM


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature K414E to reconstruct the assayed variant sequence.

column_label: Table 1; row label: K414E; column label: ATP Km (mM); raw value: 1.53; raw unit: mM; normalized value: 1.53; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 1.53; normalized unit: mM

raw_value_unit_evidence: raw value: 1.53; raw unit: mM


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M197I/A379T with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

proof_lines: pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant M197I/A379T


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature S336L to reconstruct the assayed variant sequence.

column_label: Table 1; row label: S336L; column label: ATP Km (mM); raw value: 12.6; raw unit: mM; normalized value: 12.6; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol B varies ATP at D-glucose 10x S0.5 with 1 mM MgCl2 excess; 150 mM KCl

normalized_value_unit_evidence: normalized value: 12.6; normalized unit: mM


column_label: Table 1; row label: S336L; column label: kcat (sec^-1); raw value: 2.46; raw unit: sec^-1; normalized value: 2.46; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 2.46; normalized unit: s^-1


column_label: Table 1; row label: M197E; column label: kcat (sec^-1); raw value: 17.7; raw unit: sec^-1; normalized value: 17.7; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 17.7; normalized unit: s^-1


column_label: Table 1; row label: K414E; column label: kcat (sec^-1); raw value: 19.9; raw unit: sec^-1; normalized value: 19.9; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 19.9; normalized unit: s^-1

raw_value_unit_evidence: raw value: 19.9; raw unit: sec^-1


column_label: Table 1; row label: Y214A/V452A; column label: kcat (sec^-1); raw value: 23.1; raw unit: sec^-1; normalized value: 23.1; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 23.1; normalized unit: s^-1

raw_value_unit_evidence: raw value: 23.1±2.38; raw unit: sec^-1


column_label: Table 1; row label: C252Y; column label: kcat (sec^-1); raw value: 29.3; raw unit: sec^-1; normalized value: 29.3; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 29.3; normalized unit: s^-1

raw_value_unit_evidence: raw value: 29.3; raw unit: sec^-1


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature G68K to reconstruct the assayed variant sequence.

column_label: Table 1; row label: G68K; column label: kcat (sec^-1); raw value: 43.2; raw unit: sec^-1; normalized value: 43.2; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 43.2; normalized unit: s^-1


column_label: Table 1; row label: C213R; column label: kcat (sec^-1); raw value: 50.0; raw unit: sec^-1; normalized value: 50.0; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 50.0; normalized unit: s^-1

raw_value_unit_evidence: raw value: 50.0; raw unit: sec^-1


column_label: Table 1; row label: M197I; column label: kcat (sec^-1); raw value: 58.1; raw unit: sec^-1; normalized value: 58.1; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 58.1; normalized unit: s^-1


column_label: Table 1; row label: V91L; column label: kcat (sec^-1); raw value: 60.6; raw unit: sec^-1; normalized value: 60.6; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 60.6; normalized unit: s^-1


column_label: Table 1; row label: A379T; column label: kcat (sec^-1); raw value: 61.2; raw unit: sec^-1; normalized value: 61.2; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 61.2; normalized unit: s^-1


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature V455M to reconstruct the assayed variant sequence.

column_label: Table 1; row label: V455M; column label: kcat (sec^-1); raw value: 61.8; raw unit: sec^-1; normalized value: 61.8; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 61.8; normalized unit: s^-1


column_label: Table 1; row label: M197L; column label: kcat (sec^-1); raw value: 62.6; raw unit: sec^-1; normalized value: 62.6; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 62.6; normalized unit: s^-1


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature G68V to reconstruct the assayed variant sequence.

column_label: Table 1; row label: G68V; column label: kcat (sec^-1); raw value: 62.7; raw unit: sec^-1; normalized value: 62.7; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 62.7; normalized unit: s^-1


sequence_variant_note: Resolved canonical sequence from official_uniprot_json: and applied mutation signature A456V to reconstruct the assayed variant sequence.

column_label: Table 1; row label: A456V; column label: kcat (sec^-1); raw value: 65.6; raw unit: sec^-1; normalized value: 65.6; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 65.6; normalized unit: s^-1


column_label: Table 1; row label: V389L; column label: kcat (sec^-1); raw value: 67.1; raw unit: sec^-1; normalized value: 67.1; assay condition: cleaved recombinant human glucokinase; routine NADP+ coupled assay; protocol A uses 5 mM ATP with 11 D-glucose dilutions; 150 mM KCl

normalized_value_unit_evidence: normalized value: 67.1; normalized unit: s^-1


substrate_name: beta-D-glucose

assay_conditions_summary: cofactor ATP

proof_lines: co-substrate: ATP, mutant W99R/W167F in the presence of 20-30% glycerol and in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication

proof_lines: co-substrate: ATP, mutant W99R/W167F in the presence of 20-30% glycerol, pH and temperature not specified in the publication

proof_lines: co-substrate: ATP, mutant W99R/W167F in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication

substrate: beta-D-glucose


proof_lines: co-substrate: ATP, mutant W99R/W257F in the presence of 20-30% glycerol, pH and temperature not specified in the publication

proof_lines: co-substrate: ATP, mutant W99R/W257F in the presence of 20-30% glycerol and in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication

proof_lines: co-substrate: ATP, mutant W99R/W257F, pH and temperature not specified in the publication


proof_lines: mutant W99R/W257F in the presence of 20-30% glycerol, pH and temperature not specified in the publication

proof_lines: mutant W99R/W257F in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication

proof_lines: mutant W99R/W257F in the presence of 20-30% glycerol and in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication


proof_lines: mutant W99R/W167F in the presence of 20-30% glycerol, pH and temperature not specified in the publication

proof_lines: mutant W99R/W167F in the presence of 20-30% glycerol and in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication

proof_lines: mutant W99R/W167F in the presence of 20 microM glucokinase activator drug (GKA), pH and temperature not specified in the publication


organism: Cryptosporidium parvum

substrate_name: D-fructose

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

proof_lines: pH 7.5, temperature not specified in the publication


substrate_name: D-mannose

substrate: D-mannose


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T228M to reconstruct the assayed variant sequence.

proof_lines: mutant T228M, 37°C, pH not specified in the puclication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature L146R to reconstruct the assayed variant sequence.

assay_conditions_summary: 310.15 K; cofactor ATP

proof_lines: mutant L146R, 37°C, pH not specified in the puclication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N166R/S151A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S151C/N166R to reconstruct the assayed variant sequence.


enzyme_display_name: Glucokinase

organism: Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)

column_label: Table 3 row 2-Deoxyglucose lists Apparent K_m 330 uM.

raw_value_unit_evidence: K_m raw_value=330 raw_unit=uM

table_label: Table 3. Substrate specificity of the GIK from A. pernix with alternate substrates

enzyme: Glucokinase


substrate_name: glucosamine

column_label: Table 3 row Glucosamine lists Apparent K_m 60 uM.

raw_value_unit_evidence: K_m raw_value=60 raw_unit=uM

row_label: Glucosamine

substrate: glucosamine


column_label: Table 3 row Fructose lists Apparent K_m 150 uM.

raw_value_unit_evidence: K_m raw_value=150 raw_unit=uM

row_label: Fructose


enzyme_display_name: O-ureido-L-serine synthase

organism: Streptomyces lavendulae

substrate_name: Hydroxyurea

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y97F to reconstruct the assayed variant sequence.

smiles: C(=O)(N)NO

assay_conditions_summary: pH 8

enzyme: O-ureido-L-serine synthase

substrate: Hydroxyurea


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


organism: Eimeria tenella

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N216K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature D217H to reconstruct the assayed variant sequence.


organism: Arabidopsis thaliana

substrate_name: glucose

proof_lines: Measured in yeast lacking glucose and hexose kinase activity.

substrate: glucose


enzyme_display_name: Fructokinase

organism: Escherichia coli (strain K12)

substrate_name: D-fructose (at 25 degrees Celsius and pH 7.6)

column_label: Table 2 row YajF with D-fructose column, Km,sugar value.

normalized_value_unit_evidence: Km 1.3 mM

raw_value_unit_evidence: Km,sugar 1.3 x 10^-3 M

row_label: YajF / D-fructose

table_label: Table 2, kinetic parameters for carbohydrate phosphorylation

enzyme: Fructokinase


substrate_name: ATP (at 25 degrees Celsius and pH 7.6)

assay_conditions_summary: pH 7.6; cofactor ATP

proof_lines: Catalytic efficiency with D-fructose as substrate is 55-fold higher than that with D-glucose.

substrate: ATP (at 25 degrees Celsius and pH 7.6)


substrate_name: glucose (at 25 degrees Celsius and pH 7.6)

column_label: Table 2 row YajF with D-glucose column, Km,sugar value.

normalized_value_unit_evidence: Km 59 mM

raw_value_unit_evidence: Km,sugar 5.9 x 10^-2 M

row_label: YajF / D-glucose


organism: Kluyveromyces lactis

proof_lines: pH and temperature not specified in the publication

substrate: D-glucose


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S64R/E67D/S69T to reconstruct the assayed variant sequence.

proof_lines: mutant S64R/E67D/S69T, K0.5 value, Hill coefficient 1.7, pH 7.6, 25°C


enzyme_display_name: Polyphosphate glucokinase

organism: Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra)

substrate_name: GTP (at pH 8.6)

assay_conditions_summary: pH 8.6; cofactor ATP

proof_lines: kcat is 199 sec(-1) with polyphosphate type 35 (Sigma) as substrate at pH 7.5. kcat is 208 sec(-1) with polyphosphate type 35 (Sigma) as substrate at pH 8.6. kcat is 108 sec(-1) with ATP as substrate at pH 7.5. kcat is 116 sec(-1) with ATP

enzyme: Polyphosphate glucokinase

substrate: GTP (at pH 8.6)


substrate_name: dATP (at pH 8.6)

substrate: dATP (at pH 8.6)


substrate_name: UTP (at pH 8.6)

substrate: UTP (at pH 8.6)


substrate_name: CTP (at pH 8.6)

substrate: CTP (at pH 8.6)


organism: Solanum tuberosum


substrate_name: fructose


substrate_name: D-glucose (at pH 7.5, in the polyphosphate-dependent glucokinase reaction)


substrate_name: ATP (at pH 7.5)

substrate: ATP (at pH 7.5)


organism: Schwanniomyces occidentalis

substrate_name: D-glucose

column_label: Official Springer PDF, abstract text extraction lines 23-24 and Results prose text extraction lines 231-233: metric label KM value; enzyme purified Schwanniomyces occidentalis hexokinase; substrate glucose; raw value 0.98 mM.

normalized_value_unit_evidence: 0.98 mM glucose is already in the exported unit and matches Km 0.98 mM.

raw_value_unit_evidence: The official Springer PDF states that purified Schwanniomyces occidentalis hexokinase had a KM value of 0.98 mM for glucose.

row_label: Purified Schwanniomyces occidentalis hexokinase, glucose substrate

table_label: Abstract and Results prose: purified Schwanniomyces occidentalis hexokinase kinetic parameters


column_label: Official Springer PDF, abstract text extraction lines 23-24 and Results prose text extraction lines 231-233: metric label KM value; enzyme purified Schwanniomyces occidentalis hexokinase; substrate fructose; raw value 9.3 mM.

normalized_value_unit_evidence: 9.3 mM fructose is already in the exported unit and matches Km 9.3 mM.

raw_value_unit_evidence: The official Springer PDF states that purified Schwanniomyces occidentalis hexokinase had a KM value of 9.3 mM for fructose.

row_label: Purified Schwanniomyces occidentalis hexokinase, fructose substrate

substrate: D-fructose


organism: Leishmania braziliensis

substrate_name: ATP

substrate: ATP


enzyme_display_name: Ketohexokinase

organism: Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)

substrate_name: ATP (at pH 7.5 and 42 degrees Celsius)

proof_lines: kcat is 47 sec(-1) for the phosphorylation of fructose.

enzyme: Ketohexokinase

substrate: ATP (at pH 7.5 and 42 degrees Celsius)


substrate_name: fructose (at pH 7.5 and 42 degrees Celsius)


substrate_name: O-acetyl-L-serine

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

substrate: O-acetyl-L-serine


organism: Solanum lycopersicum

substrate_name: D-fructose


organism: Pyrobaculum calidifontis

assay_conditions_summary: pH 8.5; cofactor ATP

column_label: Kinetic parameters section, glucose experiment, printed Km/kcat/catalytic-efficiency values; Table 1, P. calidifontis row, Km towards glucose column.

raw_value_unit_evidence: Kinetic parameters prose: glucose Km 660 +/- 7 uM; kcat 289 s^-1; catalytic efficiency 437 mM^-1 s^-1. Table 1 P. calidifontis row: glucose Km 0.66 mM.

row_label: Pcal_1032 / D-glucose

table_label: Kinetic parameters section and Table 1


column_label: Kinetic parameters section, ATP experiment, printed Km; Table 1, P. calidifontis row, Km towards ATP column.

raw_value_unit_evidence: Kinetic parameters prose: ATP Km 900 +/- 10 uM. Table 1 P. calidifontis row: ATP Km 0.9 mM.

row_label: Pcal_1032 / ATP


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature G72R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme G72R, at 30°C, in 100 mM Tris and 125 mM KCl, pH 7.4, in the presence of 14 mM beta-mercaptoethanol or 5 mM dithiothreitol

proof_lines: pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant G72R

proof_lines: mutant enzyme G72R, at 37°C, in 100 mM Tris and 125 mM KCl, pH 7.4, in the presence of 14 mM beta-mercaptoethanol or 5 mM dithiothreitol


organism: Thermotoga maritima

proof_lines:
pH 8.0, 85°C, recombinant enzyme
recombinant enyme, pH 7.3, 80°C


organism: Trypanosoma cruzi

proof_lines: His-tagged recombinant protein, pH 7.2, 22°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature A456V to reconstruct the assayed variant sequence.

proof_lines: pH 7.1, temperature not specified in the publication, co-substrate: ATP, mutant A456V


organism: Aeropyrum pernix

proof_lines: kcat is 23 sec(-1) with glucose as substrate. kcat is 30 sec(-1) with 2-deoxyglucose as substrate. kcat is 18 sec(-1) with glucosamine as substrate. kcat is 10 sec(-1) with fructose as substrate. kcat is 13 sec(-1) with mannose as substrate


organism: Ascaris suum

substrate_name: Glucose; ATP

substrate: Glucose; ATP


organism: Aspergillus niger


organism: Bacteroides fragilis

substrate_name: D-Glucose; ATP

substrate: D-Glucose; ATP


organism: Bos taurus


organism: Botrytis cinerea

substrate_name: ATP; D-Glucose

substrate: ATP; D-Glucose


organism: Candida albicans


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

proof_lines: mutant enzyme D205A, kcat less than 0.00091 s-1


enzyme_display_name: pyridoxamine---pyruvate transaminase

organism: Rhizobium loti

substrate_name: Pyruvate; Pyridoxamine

enzyme: pyridoxamine---pyruvate transaminase

substrate: Pyruvate; Pyridoxamine


organism: Escherichia coli


organism: Shigella dysenteriae


organism: Mycobacterium tuberculosis


substrate_name: 3-Hydroxy-L-kynurenine; Glyoxylate

substrate: 3-Hydroxy-L-kynurenine; Glyoxylate


organism: Mus musculus


organism: Nicotiana tabacum


organism: Oncorhynchus mykiss


organism: Pisum sativum


organism: Plasmodium falciparum


organism: Rattus norvegicus

substrate_name: ATP; Glucose

substrate: ATP; Glucose


organism: Homo sapiens


organism: Kluyveromyces lactis


organism: Leishmania mexicana


organism: Schizosaccharomyces pombe

substrate_name: ATP; D-Mannose

substrate: ATP; D-Mannose


substrate_name: ATP; D-Fructose

substrate: ATP; D-Fructose


organism: Sulfolobus tokodaii

substrate_name: D-Mannose; ATP

substrate: D-Mannose; ATP


organism: Sus scrofa


organism: Thermoproteus tenax


organism: Toxoplasma gondii


substrate_name: D-Glucose; ITP

substrate: D-Glucose; ITP


organism: Saccharomyces cerevisiae


organism: Schistosoma mansoni


organism: Triticum aestivum

substrate_name: Fructose; ATP

substrate: Fructose; ATP


organism: Trypanosoma brucei


organism: Trypanosoma cruzi


organism: Botrytis cinerea


organism: Escherichia coli


organism: Leishmania major

substrate_name: D-glucose

proof_lines:
recombinant enzyme without His6
recombinant (His)6-tagged enzyme

substrate: D-glucose


organism: Bos taurus

substrate_name: D-Fructose; ATP

substrate: D-Fructose; ATP


organism: Rattus norvegicus


organism: Fusobacterium mortiferum

sequence: MIIGAVEAGGTKFVDGVGNEKGEIFER

wild_type_sequence: MIIGAVEAGGTKFVDGVGNEKGEIFER


organism: Lactococcus lactis subsp. lactis

sequence: SVYYGSIEAGGTKFVLAIADEHFNI

wild_type_sequence: SVYYGSIEAGGTKFVLAIADEHFNI


organism: Streptomyces lavendulae

substrate_name: Hydroxyurea

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y97M to reconstruct the assayed variant sequence.

substrate: Hydroxyurea


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V74T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S121A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S121M to reconstruct the assayed variant sequence.


organism: Cryptosporidium parvum

substrate_name: Unknown

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

proof_lines: pH 7.5, temperature not specified in the publication

substrate: Unknown


organism: Entamoeba histolytica

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP


organism: Oryza sativa


organism: Solanum tuberosum

substrate_name: ATP; Fructose

substrate: ATP; Fructose


organism: Homo sapiens


organism: Solanum chacoense


organism: Aeropyrum pernix


organism: Bacillus subtilis (strain 168)


organism: Zea mays


organism: Salmo salar

sequence: ISEDAMTGTAEMLFDYIAECIS

wild_type_sequence: ISEDAMTGTAEMLFDYIAECIS


organism: Trypanosoma cruzi


organism: Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)


organism: Methylotuvimicrobium alcaliphilum


organism: Lysinibacillus sphaericus


organism: Mus musculus


organism: Rattus norvegicus


organism: Saccharomyces cerevisiae


organism: Leishmania braziliensis


organism: Mycobacterium tuberculosis


organism: Naegleria fowleri


organism: Oncorhynchus mykiss


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

proof_lines: kcat is 289 sec(-1) with glucose as substrate.


organism: Entamoeba histolytica

substrate_name: D-Glucose

column_label: PMID 10613700 Results 3.2 same prose segment for HXK2 glucose; kcat and glucose Km are reported together and kcat/Km is locked from those values.

raw_value_unit_evidence: Results section 3.2: kcat 237 s^-1 and apparent Km for glucose 47 uM for HXK2.

row_label: HXK2 glucose, optimal purified preparation prose segment

table_label: Results section 3.2 kinetic-properties prose

substrate: D-Glucose


substrate_name: D-Mannose

substrate: D-Mannose


organism: Solanum chacoense

column_label: Table 3 row D-Glucose; columns Kmapp (mM), kcat (s^-1), and kcat/Kmapp (mM^-1 s^-1).

row_label: D-Glucose

table_label: Table 3, Kinetic constants of pure ScHK2


substrate_name: GTP

column_label: Table 3 row GTP; columns Kmapp (mM), kcat (s^-1), and kcat/Kmapp (mM^-1 s^-1).

raw_value_unit_evidence: Table 3 row GTP: Kmapp 0.231 mM; kcat 0.85 s^-1; kcat/Kmapp 3.7 mM^-1 s^-1.

row_label: GTP

substrate: GTP


substrate_name: UTP

column_label: Table 3 row UTP; columns Kmapp (mM), kcat (s^-1), and kcat/Kmapp (mM^-1 s^-1).

raw_value_unit_evidence: Table 3 row UTP: Kmapp 2.2 mM; kcat 3.02 s^-1; kcat/Kmapp 1.4 mM^-1 s^-1.

row_label: UTP

substrate: UTP


enzyme_display_name: Kynurenine--oxoglutarate transaminase 3

substrate_name: phenylpyruvate

enzyme: Kynurenine--oxoglutarate transaminase 3

substrate: phenylpyruvate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I270S to reconstruct the assayed variant sequence.

column_label: PMID 10613700 official ScienceDirect Table 1; row B2; kcat and Km columns; kcat/Km locked from the same row. Materials and methods section 2.5 defines mutation code B2 for I270S.

raw_value_unit_evidence: Table 1 row B2: kcat 153 s^-1 and Km 134 uM for glucose.

row_label: HXK1 mutant B2 (I270S)

table_label: Table 1. Glucokinase activity of E. histolytica hexokinases HXK1 and HXK2 and HXK1 mutants


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R265T/Y266F with inferred residue-numbering offset +30 to reconstruct the assayed variant sequence.

column_label: PMID 10613700 official ScienceDirect Table 1; row C; kcat and Km columns; kcat/Km locked from the same row. Materials and methods section 2.5 defines mutation code C for R265T/Y266F.

raw_value_unit_evidence: Table 1 row C: kcat 110 s^-1 and Km 94 uM for glucose.

row_label: HXK1 mutant C (R265T/Y266F)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S144T to reconstruct the assayed variant sequence.

column_label: PMID 10613700 official ScienceDirect Table 1; row A; kcat and Km columns; kcat/Km locked from the same row. Materials and methods section 2.5 defines mutation code A for S144T.

raw_value_unit_evidence: Table 1 row A: kcat 165 s^-1 and Km 47 uM for glucose.

row_label: HXK1 mutant A (S144T)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S144T/R265T/Y266F to reconstruct the assayed variant sequence.

column_label: PMID 10613700 official ScienceDirect Table 1; row A+C; kcat and Km columns; kcat/Km locked from the same row. Materials and methods section 2.5 defines mutation code A+C for S144T/R265T/Y266F.

raw_value_unit_evidence: Table 1 row A+C: kcat 145 s^-1 and Km 120 uM for glucose.

row_label: HXK1 mutant A+C (S144T/R265T/Y266F)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S144T/V183T/I270S to reconstruct the assayed variant sequence.

column_label: PMID 10613700 official ScienceDirect Table 1; row A+B1+B2; kcat and Km columns; kcat/Km locked from the same row. Materials and methods section 2.5 defines mutation code A+B1+B2 for S144T/V183T/I270S.

raw_value_unit_evidence: Table 1 row A+B1+B2: kcat 102 s^-1 and Km 1060 uM for glucose.

row_label: HXK1 mutant A+B1+B2 (S144T/V183T/I270S)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S144T/V183T/I270S/R265T/Y266F to reconstruct the assayed variant sequence.

column_label: PMID 10613700 official ScienceDirect Table 1; row A+B1+B2+C; kcat and Km columns; kcat/Km locked from the same row. Materials and methods section 2.5 defines mutation code A+B1+B2+C for S144T/V183T/I270S/R265T/Y266F.

raw_value_unit_evidence: Table 1 row A+B1+B2+C: kcat 40 s^-1 and Km 1400 uM for glucose.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V183T to reconstruct the assayed variant sequence.

column_label: PMID 10613700 official ScienceDirect Table 1; row B1; kcat and Km columns; kcat/Km locked from the same row. Materials and methods section 2.5 defines mutation code B1 for V183T.

raw_value_unit_evidence: Table 1 row B1: kcat 186 s^-1 and Km 231 uM for glucose.

row_label: HXK1 mutant B1 (V183T)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V183T/I270S to reconstruct the assayed variant sequence.

column_label: PMID 10613700 official ScienceDirect Table 1; row B1+B2; kcat and Km columns; kcat/Km locked from the same row. Materials and methods section 2.5 defines mutation code B1+B2 for V183T/I270S.

raw_value_unit_evidence: Table 1 row B1+B2: kcat 133 s^-1 and Km 990 uM for glucose.

row_label: HXK1 mutant B1+B2 (V183T/I270S)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V183T/I270S/R265T/Y266F to reconstruct the assayed variant sequence.

column_label: PMID 10613700 official ScienceDirect Table 1; row B1+B2+C; kcat and Km columns; kcat/Km locked from the same row. Materials and methods section 2.5 defines mutation code B1+B2+C for V183T/I270S/R265T/Y266F.

raw_value_unit_evidence: Table 1 row B1+B2+C: kcat 83 s^-1 and Km 1950 uM for glucose.


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

column_label: PMID 10613700 Results 3.2 same prose segment for HXK1 glucose; current export uses Km 0.067 mM from Table 1 instead of the 0.059 mM prose value paired with kcat 284 s^-1.

raw_value_unit_evidence: Results section 3.2: kcat 284 s^-1 and apparent Km for glucose 59 uM for HXK1.

row_label: HXK1 glucose, optimal purified preparation prose segment


organism: Homo sapiens

substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P35557 and applied mutation signature V62A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 303.15 K; cofactor ATP

column_label: Table I: Mutational Analysis of the V62 GKA binding site (J. Biol. Chem. 2005, volume 280, number 14, pages 14105-14113; journal page 14108, PDF page 4), printed parameter column heads Yield (mg/liter), Protein concentration (mg/ml), kcat (s^-1), Glucose S0.5 (mM), ATP Km (mM), nH, GIa and EC50 for RO0274377 (uM); the article prints no catalytic-efficiency column in this table. Journal page 14108 (PDF page 4). Table I, mutant row V62A, first individual data point of each column; column kcat (s^-1) cell = 48.8; column ATP Km (mM) cell = 0.20. captured primary segment: Table I, mutant row V62A, first individual data point of each column | construct V62A GST-GCK | substrate ATP | condition kinetic analysis of the purified GST fusion enzyme, no assay pH or temperature printed for Table I | kcat 48.8 s^-1 | ATP Km 0.20 mM

normalized_value_unit_evidence: kcat: printed Table I kcat cell 48.8 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 48.8 s^(-1). Km: printed Table I ATP Km cell 0.20 mM; the printed column is already in millimolar, so no unit conversion applies and the value is 0.2 mM. kcat/Km: the exported efficiency is the quotient of those two printed cells of this one measurement, 48.8 / 0.2 = 243.99999999999997 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 14108, Table I, mutant row V62A, first individual data point of each column: kcat = 48.8 s^-1; ATP Km = 0.20 mM. Table I carries no catalytic-efficiency column.

row_label: Table I, mutant row V62A, first individual data point of each column; the cited cells are the first of the two independent expressions of this mutant

substrate: ATP


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P35557 and applied mutation signature V62E to reconstruct the assayed variant sequence.

column_label: Table I: Mutational Analysis of the V62 GKA binding site (J. Biol. Chem. 2005, volume 280, number 14, pages 14105-14113; journal page 14108, PDF page 4), printed parameter column heads Yield (mg/liter), Protein concentration (mg/ml), kcat (s^-1), Glucose S0.5 (mM), ATP Km (mM), nH, GIa and EC50 for RO0274377 (uM); the article prints no catalytic-efficiency column in this table. Journal page 14108 (PDF page 4). Table I, mutant row V62E, first individual data point of each column; column kcat (s^-1) cell = 5.22; column ATP Km (mM) cell = 0.08. captured primary segment: Table I, mutant row V62E, first individual data point of each column | construct V62E GST-GCK | substrate ATP | condition kinetic analysis of the purified GST fusion enzyme, no assay pH or temperature printed for Table I | kcat 5.22 s^-1 | ATP Km 0.08 mM

normalized_value_unit_evidence: kcat: printed Table I kcat cell 5.22 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 5.22 s^(-1). Km: printed Table I ATP Km cell 0.08 mM; the printed column is already in millimolar, so no unit conversion applies and the value is 0.08 mM. kcat/Km: the exported efficiency is the quotient of those two printed cells of this one measurement, 5.22 / 0.08 = 65.25 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 14108, Table I, mutant row V62E, first individual data point of each column: kcat = 5.22 s^-1; ATP Km = 0.08 mM. Table I carries no catalytic-efficiency column.

row_label: Table I, mutant row V62E, first individual data point of each column; the cited cells are the first of the two independent expressions of this mutant


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V62F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P35557 and applied mutation signature V62K to reconstruct the assayed variant sequence.

column_label: Table I: Mutational Analysis of the V62 GKA binding site (J. Biol. Chem. 2005, volume 280, number 14, pages 14105-14113; journal page 14108, PDF page 4), printed parameter column heads Yield (mg/liter), Protein concentration (mg/ml), kcat (s^-1), Glucose S0.5 (mM), ATP Km (mM), nH, GIa and EC50 for RO0274377 (uM); the article prints no catalytic-efficiency column in this table. Journal page 14108 (PDF page 4). Table I, mutant row V62K, first individual data point of each column; column kcat (s^-1) cell = 7.44; column ATP Km (mM) cell = 0.18. captured primary segment: Table I, mutant row V62K, first individual data point of each column | construct V62K GST-GCK | substrate ATP | condition kinetic analysis of the purified GST fusion enzyme, no assay pH or temperature printed for Table I | kcat 7.44 s^-1 | ATP Km 0.18 mM

normalized_value_unit_evidence: kcat: printed Table I kcat cell 7.44 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 7.44 s^(-1). Km: printed Table I ATP Km cell 0.18 mM; the printed column is already in millimolar, so no unit conversion applies and the value is 0.18 mM. kcat/Km: the exported efficiency is the quotient of those two printed cells of this one measurement, 7.44 / 0.18 = 41.333333333333336 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 14108, Table I, mutant row V62K, first individual data point of each column: kcat = 7.44 s^-1; ATP Km = 0.18 mM. Table I carries no catalytic-efficiency column.

row_label: Table I, mutant row V62K, first individual data point of each column; the cited cells are the first of the two independent expressions of this mutant


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V62L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P35557 and applied mutation signature V62M to reconstruct the assayed variant sequence.

column_label: Table I: Mutational Analysis of the V62 GKA binding site (J. Biol. Chem. 2005, volume 280, number 14, pages 14105-14113; journal page 14108, PDF page 4), printed parameter column heads Yield (mg/liter), Protein concentration (mg/ml), kcat (s^-1), Glucose S0.5 (mM), ATP Km (mM), nH, GIa and EC50 for RO0274377 (uM); the article prints no catalytic-efficiency column in this table. Journal page 14108 (PDF page 4). Table I, mutant row V62M, mean of four independent expressions; column kcat (s^-1) cell = 53.6; column ATP Km (mM) cell = 0.46. captured primary segment: Table I, mutant row V62M, mean of four independent expressions | construct V62M GST-GCK | substrate ATP | condition kinetic analysis of the purified GST fusion enzyme, no assay pH or temperature printed for Table I | kcat 53.6 s^-1 | ATP Km 0.46 mM

normalized_value_unit_evidence: kcat: printed Table I kcat cell 53.6 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 53.6 s^(-1). Km: printed Table I ATP Km cell 0.46 mM; the printed column is already in millimolar, so no unit conversion applies and the value is 0.46 mM. kcat/Km: the exported efficiency is the quotient of those two printed cells of this one measurement, 53.6 / 0.46 = 116.52173913043478 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 14108, Table I, mutant row V62M, mean of four independent expressions: kcat = 53.6 s^-1; ATP Km = 0.46 mM. Table I carries no catalytic-efficiency column.

row_label: Table I, mutant row V62M, mean of four independent expressions; the cited cells are the mean of the four independent expressions of this enzyme form


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P35557 and applied mutation signature V62Q to reconstruct the assayed variant sequence.

column_label: Table I: Mutational Analysis of the V62 GKA binding site (J. Biol. Chem. 2005, volume 280, number 14, pages 14105-14113; journal page 14108, PDF page 4), printed parameter column heads Yield (mg/liter), Protein concentration (mg/ml), kcat (s^-1), Glucose S0.5 (mM), ATP Km (mM), nH, GIa and EC50 for RO0274377 (uM); the article prints no catalytic-efficiency column in this table. Journal page 14108 (PDF page 4). Table I, mutant row V62Q, first individual data point of each column; column kcat (s^-1) cell = 14.9; column ATP Km (mM) cell = 0.11. captured primary segment: Table I, mutant row V62Q, first individual data point of each column | construct V62Q GST-GCK | substrate ATP | condition kinetic analysis of the purified GST fusion enzyme, no assay pH or temperature printed for Table I | kcat 14.9 s^-1 | ATP Km 0.11 mM

normalized_value_unit_evidence: kcat: printed Table I kcat cell 14.9 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 14.9 s^(-1). Km: printed Table I ATP Km cell 0.11 mM; the printed column is already in millimolar, so no unit conversion applies and the value is 0.11 mM. kcat/Km: the exported efficiency is the quotient of those two printed cells of this one measurement, 14.9 / 0.11 = 135.45454545454547 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 14108, Table I, mutant row V62Q, first individual data point of each column: kcat = 14.9 s^-1; ATP Km = 0.11 mM. Table I carries no catalytic-efficiency column.

row_label: Table I, mutant row V62Q, first individual data point of each column; the cited cells are the first of the two independent expressions of this mutant


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P35557 and applied mutation signature V62T to reconstruct the assayed variant sequence.

column_label: Table I: Mutational Analysis of the V62 GKA binding site (J. Biol. Chem. 2005, volume 280, number 14, pages 14105-14113; journal page 14108, PDF page 4), printed parameter column heads Yield (mg/liter), Protein concentration (mg/ml), kcat (s^-1), Glucose S0.5 (mM), ATP Km (mM), nH, GIa and EC50 for RO0274377 (uM); the article prints no catalytic-efficiency column in this table. Journal page 14108 (PDF page 4). Table I, mutant row V62T, first individual data point of each column; column kcat (s^-1) cell = 26.6; column ATP Km (mM) cell = 0.31. captured primary segment: Table I, mutant row V62T, first individual data point of each column | construct V62T GST-GCK | substrate ATP | condition kinetic analysis of the purified GST fusion enzyme, no assay pH or temperature printed for Table I | kcat 26.6 s^-1 | ATP Km 0.31 mM

normalized_value_unit_evidence: kcat: printed Table I kcat cell 26.6 s^-1; the printed turnover column is already per second, so no unit conversion applies and the value is 26.6 s^(-1). Km: printed Table I ATP Km cell 0.31 mM; the printed column is already in millimolar, so no unit conversion applies and the value is 0.31 mM. kcat/Km: the exported efficiency is the quotient of those two printed cells of this one measurement, 26.6 / 0.31 = 85.80645161290323 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 14108, Table I, mutant row V62T, first individual data point of each column: kcat = 26.6 s^-1; ATP Km = 0.31 mM. Table I carries no catalytic-efficiency column.

row_label: Table I, mutant row V62T, first individual data point of each column; the cited cells are the first of the two independent expressions of this mutant


proof_lines:
glucokinase
wild type
V62M


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

column_label: Table 3 row GTP; columns Kmapp (mM), kcat (s^-1), and kcat/Kmapp (mM^-1 s^-1).

raw_value_unit_evidence: Table 3 row GTP: Kmapp 0.231 mM; kcat 0.85 s^-1; kcat/Kmapp 3.7 mM^-1 s^-1.


substrate_name: TTP

column_label: Table 3 row TTP; columns Kmapp (mM), kcat (s^-1), and kcat/Kmapp (mM^-1 s^-1).

raw_value_unit_evidence: Table 3 row TTP: Kmapp 0.231 mM; kcat 1.42 s^-1; kcat/Kmapp 6.1 mM^-1 s^-1.

row_label: TTP

substrate: TTP


substrate_name: CTP

column_label: Table 3 row CTP; columns Kmapp (mM), kcat (s^-1), and kcat/Kmapp (mM^-1 s^-1).

raw_value_unit_evidence: Table 3 row CTP: Kmapp 2.0 mM; kcat 1.61 s^-1; kcat/Kmapp 0.8 mM^-1 s^-1.

row_label: CTP

substrate: CTP


column_label: Table 3 row UTP; columns Kmapp (mM), kcat (s^-1), and kcat/Kmapp (mM^-1 s^-1).

raw_value_unit_evidence: Table 3 row UTP: Kmapp 2.2 mM; kcat 3.02 s^-1; kcat/Kmapp 1.4 mM^-1 s^-1.

row_label: UTP


column_label: Table 3 row D-Glucose; columns Kmapp (mM), kcat (s^-1), and kcat/Kmapp (mM^-1 s^-1).

row_label: D-Glucose


column_label: Table 3 row ATP; columns Kmapp (mM), kcat (s^-1), and kcat/Kmapp (mM^-1 s^-1).

row_label: ATP


substrate_name: D-fructose

column_label: Table 3 row D-Fructose; columns Kmapp (mM), kcat (s^-1), and kcat/Kmapp (mM^-1 s^-1).

raw_value_unit_evidence: Table 3 row D-Fructose: Kmapp 5.2 +/- 0.4 mM; kcat 3.78 +/- 1.13 s^-1; kcat/Kmapp 0.7 mM^-1 s^-1.

row_label: D-Fructose

substrate: D-fructose


substrate_name: D-Fructose

substrate: D-Fructose


column_label: [{'metric': 'km', 'table_label': 'Table I', 'row_label': 'Isoenzyme A', 'column_label': 'Glucose', 'raw_value': '4.4 x 10^-5', 'raw_unit': 'M', 'normalized_value': 0.044, 'normalized_unit': 'mM', 'assay_condition': 'ATP:hexose phosphotransferase isoenzyme A.'}]

raw_value_unit_evidence: Km, row A, Glucose column: 4.4 x 10^-5 M.

row_label: Isoenzyme A; Glucose Km

table_label: Table I


column_label: [{'metric': 'km', 'table_label': 'Table I', 'row_label': 'Isoenzyme A', 'column_label': 'Fructose', 'raw_value': '3.1 x 10^-3', 'raw_unit': 'M', 'normalized_value': 3.1, 'normalized_unit': 'mM', 'assay_condition': 'ATP:hexose phosphotransferase isoenzyme A; fructose assay included phosphohexose isomerase.'}]

raw_value_unit_evidence: Km, row A, Fructose column: 3.1 x 10^-3 M.

row_label: Isoenzyme A; Fructose Km


column_label: [{'metric': 'km', 'table_label': 'Table I', 'row_label': 'Isoenzyme A', 'column_label': 'ATP', 'raw_value': '4.2 x 10^-4', 'raw_unit': 'M', 'normalized_value': 0.42, 'normalized_unit': 'mM', 'assay_condition': 'ATP:hexose phosphotransferase isoenzyme A.'}]

raw_value_unit_evidence: Km, row A, ATP column: 4.2 x 10^-4 M.

row_label: Isoenzyme A; ATP Km


column_label: [{'metric': 'km', 'table_label': 'Table I', 'row_label': 'Isoenzyme B', 'column_label': 'Glucose', 'raw_value': '1.3 x 10^-4', 'raw_unit': 'M', 'normalized_value': 0.13, 'normalized_unit': 'mM', 'assay_condition': 'ATP:hexose phosphotransferase isoenzyme B.'}]

raw_value_unit_evidence: Km, row B, Glucose column: 1.3 x 10^-4 M.

row_label: Isoenzyme B; Glucose Km


column_label: [{'metric': 'km', 'table_label': 'Table I', 'row_label': 'Isoenzyme B', 'column_label': 'Fructose', 'raw_value': '3.0 x 10^-3', 'raw_unit': 'M', 'normalized_value': 3.0, 'normalized_unit': 'mM', 'assay_condition': 'ATP:hexose phosphotransferase isoenzyme B; fructose assay included phosphohexose isomerase.'}]

raw_value_unit_evidence: Km, row B, Fructose column: 3.0 x 10^-3 M.

row_label: Isoenzyme B; Fructose Km


column_label: [{'metric': 'km', 'table_label': 'Table I', 'row_label': 'Isoenzyme B', 'column_label': 'ATP', 'raw_value': '7.0 x 10^-4', 'raw_unit': 'M', 'normalized_value': 0.7, 'normalized_unit': 'mM', 'assay_condition': 'ATP:hexose phosphotransferase isoenzyme B.'}]

raw_value_unit_evidence: Km, row B, ATP column: 7.0 x 10^-4 M.

row_label: Isoenzyme B; ATP Km


column_label: [{'metric': 'km', 'table_label': 'Table I', 'row_label': 'Isoenzyme C', 'column_label': 'Glucose', 'raw_value': '6.0 x 10^-6', 'raw_unit': 'M', 'normalized_value': 0.006, 'normalized_unit': 'mM', 'assay_condition': 'ATP:hexose phosphotransferase isoenzyme C.'}]

raw_value_unit_evidence: Km, row C, Glucose column: 6.0 x 10^-6 M.

row_label: Isoenzyme C; Glucose Km


column_label: [{'metric': 'km', 'table_label': 'Table I', 'row_label': 'Isoenzyme C', 'column_label': 'Fructose', 'raw_value': '1.2 x 10^-3', 'raw_unit': 'M', 'normalized_value': 1.2, 'normalized_unit': 'mM', 'assay_condition': 'ATP:hexose phosphotransferase isoenzyme C; fructose assay included phosphohexose isomerase.'}]

raw_value_unit_evidence: Km, row C, Fructose column: 1.2 x 10^-3 M.

row_label: Isoenzyme C; Fructose Km


substrate_name: glutamine

column_label: TABLE 2 | Kinetic parameters of mKAT III toward amino acids and alpha-keto acids; row Amino acid substrates / Glutamine; column Km (mM).

normalized_value_unit_evidence: km paper=0.7 mM

raw_value_unit_evidence: TABLE 2 | Kinetic parameters of mKAT III toward amino acids and alpha-keto acids, row Amino acid substrates / Glutamine: Km 0.7 ± 0.2 mM; kcat 136.0 ± 14.0 min^-1; kcat/Km 194.2 min^-1 mM^-1.

row_label: Amino acid substrates / Glutamine

substrate: glutamine


substrate_name: histidine

column_label: TABLE 2 | Kinetic parameters of mKAT III toward amino acids and alpha-keto acids; row Amino acid substrates / Histidine; column Km (mM).

raw_value_unit_evidence: TABLE 2 | Kinetic parameters of mKAT III toward amino acids and alpha-keto acids, row Amino acid substrates / Histidine: Km 0.7 ± 0.4 mM; kcat 120.0 ± 20.0 min^-1; kcat/Km 171.4 min^-1 mM^-1.

row_label: Amino acid substrates / Histidine

substrate: histidine


substrate_name: cysteine

column_label: TABLE 2 | Kinetic parameters of mKAT III toward amino acids and alpha-keto acids; row Amino acid substrates / Cysteine; column Km (mM).

raw_value_unit_evidence: TABLE 2 | Kinetic parameters of mKAT III toward amino acids and alpha-keto acids, row Amino acid substrates / Cysteine: Km 0.7 ± 0.4 mM; kcat 78.0 ± 12.0 min^-1; kcat/Km 111.4 min^-1 mM^-1.

row_label: Amino acid substrates / Cysteine

substrate: cysteine


substrate_name: methionine

column_label: TABLE 2 | Kinetic parameters of mKAT III toward amino acids and alpha-keto acids; row Amino acid substrates / Methionine; column Km (mM).

normalized_value_unit_evidence: km paper=0.9 mM

raw_value_unit_evidence: TABLE 2 | Kinetic parameters of mKAT III toward amino acids and alpha-keto acids, row Amino acid substrates / Methionine: Km 0.9 ± 0.7 mM; kcat 146.0 ± 50.0 min^-1; kcat/Km 162.2 min^-1 mM^-1.

row_label: Amino acid substrates / Methionine

substrate: methionine


substrate_name: phenylalanine

column_label: TABLE 2 | Kinetic parameters of mKAT III toward amino acids and alpha-keto acids; row Amino acid substrates / Phenylalanine; column Km (mM).

normalized_value_unit_evidence: km paper=1.1 mM

raw_value_unit_evidence: TABLE 2 | Kinetic parameters of mKAT III toward amino acids and alpha-keto acids, row Amino acid substrates / Phenylalanine: Km 1.1 ± 0.4 mM; kcat 162.0 ± 20.0 min^-1; kcat/Km 147.2 min^-1 mM^-1.

row_label: Amino acid substrates / Phenylalanine

substrate: phenylalanine


substrate_name: asparagine

column_label: TABLE 2 | Kinetic parameters of mKAT III toward amino acids and alpha-keto acids; row Amino acid substrates / Asparagine; column Km (mM).

normalized_value_unit_evidence: km paper=1.4 mM

raw_value_unit_evidence: TABLE 2 | Kinetic parameters of mKAT III toward amino acids and alpha-keto acids, row Amino acid substrates / Asparagine: Km 1.4 ± 0.4 mM; kcat 176.0 ± 18.0 min^-1; kcat/Km 125.7 min^-1 mM^-1.

row_label: Amino acid substrates / Asparagine

substrate: asparagine


substrate_name: kynurenine

column_label: TABLE 2 | Kinetic parameters of mKAT III toward amino acids and alpha-keto acids; row Amino acid substrates / Kynurenine; column Km (mM).

normalized_value_unit_evidence: km paper=1.5 mM

raw_value_unit_evidence: TABLE 2 | Kinetic parameters of mKAT III toward amino acids and alpha-keto acids, row Amino acid substrates / Kynurenine: Km 1.5 ± 0.5 mM; kcat 138.0 ± 18.0 min^-1; kcat/Km 92.0 min^-1 mM^-1.

row_label: Amino acid substrates / Kynurenine

substrate: kynurenine


substrate_name: tryptophan

column_label: TABLE 2 | Kinetic parameters of mKAT III toward amino acids and alpha-keto acids; row Amino acid substrates / Tryptophan; column Km (mM).

normalized_value_unit_evidence: km paper=7.1 mM

raw_value_unit_evidence: TABLE 2 | Kinetic parameters of mKAT III toward amino acids and alpha-keto acids, row Amino acid substrates / Tryptophan: Km 7.1 ± 4.2 mM; kcat 213.9 ± 60.0 min^-1; kcat/Km 30.1 min^-1 mM^-1.

row_label: Amino acid substrates / Tryptophan

substrate: tryptophan


substrate_name: serine

column_label: TABLE 2 | Kinetic parameters of mKAT III toward amino acids and alpha-keto acids; row Amino acid substrates / Serine; column Km (mM).

normalized_value_unit_evidence: km paper=3.0 mM

raw_value_unit_evidence: TABLE 2 | Kinetic parameters of mKAT III toward amino acids and alpha-keto acids, row Amino acid substrates / Serine: Km 3.0 ± 0.7 mM; kcat 130.0 ± 10.0 min^-1; kcat/Km 43.3 min^-1 mM^-1.

row_label: Amino acid substrates / Serine

substrate: serine


substrate_name: glyoxylate

substrate: glyoxylate


substrate_name: aminoadipate

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

column_label: Table 2; section Amino-acid substrates; row Aminoadipate; column Km (mM); raw cell 0.9±0.1; normalized Km 0.9 mM

normalized_value_unit_evidence: Km=0.9 mM

raw_value_unit_evidence: Aminoadipate: Km (mM)=0.9±0.1

row_label: Aminoadipate

table_label: Table 2. Kinetic parameters of hKAT II towards amino acids and α-oxo acids.

substrate: aminoadipate


column_label: Table 2; section Amino-acid substrates; row Kynurenine; column Km (mM); raw cell 4.7±0.8; normalized Km 4.7 mM

normalized_value_unit_evidence: Km=4.7 mM

raw_value_unit_evidence: Kynurenine: Km (mM)=4.7±0.8

row_label: Kynurenine


column_label: Table 2; section Amino-acid substrates; row Methionine; column Km (mM); raw cell 1.7±0.5; normalized Km 1.7 mM

normalized_value_unit_evidence: Km=1.7 mM

raw_value_unit_evidence: Methionine: Km (mM)=1.7±0.5

row_label: Methionine


substrate_name: glutamate

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

column_label: Table 2; section Amino-acid substrates; row Glutamate; column Km (mM); raw cell 1.6±0.4; normalized Km 1.6 mM

normalized_value_unit_evidence: Km=1.6 mM

raw_value_unit_evidence: Glutamate: Km (mM)=1.6±0.4

row_label: Glutamate

substrate: glutamate


substrate_name: tyrosine

column_label: Table 2; section Amino-acid substrates; row Tyrosine; column Km (mM); raw cell 1.8±0.2; normalized Km 1.8 mM

normalized_value_unit_evidence: Km=1.8 mM

raw_value_unit_evidence: Tyrosine: Km (mM)=1.8±0.2

row_label: Tyrosine

substrate: tyrosine


column_label: Table 2; section Oxo acid substrates; row α-Oxoglutarate; column Km (mM); raw cell 1.2±0.4; normalized Km 1.2 mM

normalized_value_unit_evidence: Km=1.2 mM

raw_value_unit_evidence: α-Oxoglutarate: Km (mM)=1.2±0.4

row_label: α-Oxoglutarate


substrate_name: phenylpyruvate

column_label: Table 2; section Oxo acid substrates; row Phenylpyruvate; column Km (mM); raw cell 1.8±0.2; normalized Km 1.8 mM

raw_value_unit_evidence: Phenylpyruvate: Km (mM)=1.8±0.2

row_label: Phenylpyruvate

substrate: phenylpyruvate


enzyme_display_name: pyridoxamine--pyruvate transaminase

organism: Rhizobium loti

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

proof_lines: pyridoxamine pyruvate pyridoxal

enzyme: pyridoxamine--pyruvate transaminase


substrate_name: L-Alanine

column_label: Official PMC Table 1 row L-Alanine: L-Alanine | Km 11 +/- 0.6 mM | kcat 41 +/- 0.7 s^-1 | kcat/Km 3700 s^-1 M^-1.

normalized_value_unit_evidence: kcat normalized_value=41 normalized_unit=s^-1; Km normalized_value=11 normalized_unit=mM; kcat/Km ratio normalized_value=3.727272727272727 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 L-Alanine cells: kcat raw_value=41 +/- 0.7 raw_unit=s^-1; Km raw_value=11 +/- 0.6 raw_unit=mM; kcat/Km raw_value=3700 raw_unit=s^-1 M^-1.

row_label: L-Alanine

substrate: L-Alanine


substrate_name: L-alpha-Aminobutyrate

substrate: L-alpha-Aminobutyrate


substrate_name: Pyridoxal

normalized_value_unit_evidence: kcat normalized_value=41 normalized_unit=s^-1; Km normalized_value=0.059 normalized_unit=mM; kcat/Km ratio normalized_value=694.9152542372882 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 PL cells: kcat raw_value=41 +/- 0.8 raw_unit=s^-1; Km raw_value=0.059 +/- 0.005 raw_unit=mM; kcat/Km raw_value=690000 raw_unit=s^-1 M^-1.

row_label: PL

substrate: Pyridoxal


substrate_name: Pyridoxamine

normalized_value_unit_evidence: kcat normalized_value=28 normalized_unit=s^-1; Km normalized_value=0.044 normalized_unit=mM; kcat/Km ratio normalized_value=636.3636363636364 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 PM cells: kcat raw_value=28 +/- 0.5 raw_unit=s^-1; Km raw_value=0.044 +/- 0.004 raw_unit=mM; kcat/Km raw_value=640000 raw_unit=s^-1 M^-1.

row_label: PM

substrate: Pyridoxamine


substrate_name: pyruvate

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

column_label: Official PMC Table 1 row Pyruvate: Pyruvate | Km 0.34 +/- 0.02 mM | kcat 29 +/- 0.6 s^-1 | kcat/Km 85000 s^-1 M^-1.

normalized_value_unit_evidence: kcat normalized_value=29 normalized_unit=s^-1; Km normalized_value=0.34 normalized_unit=mM; kcat/Km ratio normalized_value=85.29411764705881 normalized_unit=s^-1*mM^-1.

raw_value_unit_evidence: Table 1 Pyruvate cells: kcat raw_value=29 +/- 0.6 raw_unit=s^-1; Km raw_value=0.34 +/- 0.02 raw_unit=mM; kcat/Km raw_value=85000 raw_unit=s^-1 M^-1.

row_label: Pyruvate

substrate: pyruvate


substrate_name: ATP

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

substrate: ATP


substrate_name: D-Fructose

substrate: D-Fructose


substrate_name: D-Ribose

substrate: D-Ribose


substrate_name: D-Ribulose

substrate: D-Ribulose


substrate_name: D-Xylulose

substrate: D-Xylulose


substrate_name: L-Sorbose

substrate: L-Sorbose


enzyme_display_name: 4-aminobutyrate--pyruvate transaminase

organism: Arabidopsis thaliana

smiles: NCCCC(=O)O

column_label: Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Forward reaction / varied substrate GABA (4-aminobutanoate) / fixed substrate pyruvate, column kcat s^-1, raw cell 10.6, normalized 10.6 s^-1; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Forward reaction / varied substrate GABA (4-aminobutanoate) / fixed substrate pyruvate, column Km mM, raw cell 0.34+/-0.02, normalized 0.34 mM; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Forward reaction / varied substrate GABA (4-aminobutanoate) / fixed substrate pyruvate, column kcat/Km s^-1 mM^-1, raw cell 31, normalized 31 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=10.6 normalized_unit=s^-1; Km normalized_value=0.34 normalized_unit=mM; kcat/Km normalized_value=31 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=10.6 raw_unit=s^-1 raw_cell=10.6; Km raw_value=0.34+/-0.02 raw_unit=mM raw_cell=0.34+/-0.02; kcat/Km raw_value=31 raw_unit=s^-1*mM^-1 raw_cell=31

enzyme: 4-aminobutyrate--pyruvate transaminase


smiles: O=CC(=O)O

column_label: Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Reverse reaction / varied substrate glyoxylate / fixed substrate alanine, column kcat s^-1, raw cell 12.1, normalized 12.1 s^-1; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Reverse reaction / varied substrate glyoxylate / fixed substrate alanine, column Km mM, raw cell 0.14+/-0.02, normalized 0.14 mM; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Reverse reaction / varied substrate glyoxylate / fixed substrate alanine, column kcat/Km s^-1 mM^-1, raw cell 86, normalized 86 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=12.1 normalized_unit=s^-1; Km normalized_value=0.14 normalized_unit=mM; kcat/Km normalized_value=86 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=12.1 raw_unit=s^-1 raw_cell=12.1; Km raw_value=0.14+/-0.02 raw_unit=mM raw_cell=0.14+/-0.02; kcat/Km raw_value=86 raw_unit=s^-1*mM^-1 raw_cell=86


substrate_name: L-alanine

column_label: Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Reverse reaction / varied substrate alanine / fixed substrate SSA, column kcat s^-1, raw cell 15.4, normalized 15.4 s^-1; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Reverse reaction / varied substrate alanine / fixed substrate SSA, column Km mM, raw cell 2.4+/-0.3, normalized 2.4 mM; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Reverse reaction / varied substrate alanine / fixed substrate SSA, column kcat/Km s^-1 mM^-1, raw cell 6.4, normalized 6.4 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=15.4 normalized_unit=s^-1; Km normalized_value=2.4 normalized_unit=mM; kcat/Km normalized_value=6.4 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=15.4 raw_unit=s^-1 raw_cell=15.4; Km raw_value=2.4+/-0.3 raw_unit=mM raw_cell=2.4+/-0.3; kcat/Km raw_value=6.4 raw_unit=s^-1*mM^-1 raw_cell=6.4

substrate: L-alanine


column_label: Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Forward reaction / varied substrate pyruvate / fixed substrate GABA, column kcat s^-1, raw cell 10.6, normalized 10.6 s^-1; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Forward reaction / varied substrate pyruvate / fixed substrate GABA, column Km mM, raw cell 0.14+/-0.01, normalized 0.14 mM; Table 2. Kinetic parameters for the purified recombinant AtGABA-T row Forward reaction / varied substrate pyruvate / fixed substrate GABA, column kcat/Km s^-1 mM^-1, raw cell 76, normalized 76 s^-1*mM^-1

normalized_value_unit_evidence: kcat normalized_value=10.6 normalized_unit=s^-1; Km normalized_value=0.14 normalized_unit=mM; kcat/Km normalized_value=76 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=10.6 raw_unit=s^-1 raw_cell=10.6; Km raw_value=0.14+/-0.01 raw_unit=mM raw_cell=0.14+/-0.01; kcat/Km raw_value=76 raw_unit=s^-1*mM^-1 raw_cell=76