sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O31616 and applied mutation signature Y246W to reconstruct the assayed variant sequence.

column_label: Table 2 (Comparison of the apparent kinetic parameters determined at 21% oxygen saturation on glycine or sarcosine as substrates for wild-type and variants of GO), body row Y246W; under the Glycine group head: column 'kcat,app (s^-1)' = 1.21; column 'Km,app (mM)' = 17.2; column 'kcat,app/Km,app' = 0.07 in mM^-1*s^-1. The three Sarcosine columns on the same printed line carry the sarcosine cell group and are not used for this row.

normalized_value_unit_evidence: kcat: printed Table 2 glycine cell 1.21 in the column head unit s^-1; the head prints reciprocal seconds, so no unit conversion applies and the catalog carries 1.21 s^(-1). Km: printed Table 2 glycine cell 17.2 in the column head unit mM; the head prints millimolar, so no unit conversion applies and the catalog carries 17.2 mM. kcat/Km: printed Table 2 glycine cell 0.07 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 0.07 s^(-1)*mM^(-1), while the catalog carries 0.0703488372 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, glycine cell group of body row Y246W: kcat,app = 1.21 s^-1; Km,app = 17.2 mM; printed kcat,app/Km,app = 0.07 mM^-1*s^-1.

row_label: Table 2, body row Y246W, glycine cell group


enzyme_display_name: glycine oxidase

organism: Bacillus subtilis

substrate_name: sarcosine

source_db: oed

verification_status: unverified

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

kcat_over_km_origin: calculated

source_license: CC BY 4.0

km_unit: mM

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

smiles: CNCC(=O)O

data_origin: experimental

enzyme: glycine oxidase

substrate: sarcosine

status: unverified

source: oed


substrate_name: glycine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A54R to reconstruct the assayed variant sequence.

mutation_type: substitution

substrate: glycine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H244A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


enzyme_display_name: Amine oxidase [flavin-containing] A

organism: Homo sapiens

substrate_name: (R)-adrenaline

source_db: uniprot

verification_status: verified

kcat_display: Not reported

kcat_over_km_display: Not reported

column_label: Km

normalized_value_unit_evidence: normalized: km=0.208 mM; Vmax is not kcat and is not used as kcat evidence

raw_value_unit_evidence: paper Table 2 cells: MAO-A Adrenaline Km=208 uM; Vmax=379 pmol/mg protein/min

row_label: MAO-A / Adrenaline

table_label: Table 2

enzyme: Amine oxidase [flavin-containing] A

substrate: (R)-adrenaline

status: verified

source: uniprot


substrate_name: dopamine

normalized_value_unit_evidence: normalized: km=0.212 mM; Vmax is not kcat and is not used as kcat evidence

raw_value_unit_evidence: paper Table 2 cells: MAO-A Dopamine Km=212 uM; Vmax=680 pmol/mg protein/min

row_label: MAO-A / Dopamine

substrate: dopamine


substrate_name: serotonin

verification_status: corrected

column_label: Table 2. Kinetic parameters of the two forms of MAO; row 5-Hydroxytryptamine; human cerebral cortex MAO-A; Km column 137 uM normalized to 0.137 mM; Vmax column 228 pmol mg protein^-1 min^-1

raw_value_unit_evidence: Km 137 uM; Vmax 228 pmol mg protein^-1 min^-1

row_label: human cerebral cortex MAO-A / 5-Hydroxytryptamine

substrate: serotonin

status: corrected


substrate_name: (R)-noradrenaline

normalized_value_unit_evidence: normalized: km=0.284 mM; Vmax is not kcat and is not used as kcat evidence

raw_value_unit_evidence: paper Table 2 cells: MAO-A Noradrenaline Km=284 uM; Vmax=561 pmol/mg protein/min

row_label: MAO-A / Noradrenaline

substrate: (R)-noradrenaline


normalized_value_unit_evidence: normalized: km=0.14 mM; Vmax is not kcat and is not used as kcat evidence

raw_value_unit_evidence: paper Table 2 cells: MAO-A 2-phenethylamine Km=140 uM; Vmax=20 pmol/mg protein/min

row_label: MAO-A / 2-phenethylamine


substrate_name: tyramine

normalized_value_unit_evidence: normalized: km=0.127 mM; Vmax is not kcat and is not used as kcat evidence

raw_value_unit_evidence: paper Table 2 cells: MAO-A Tyramine Km=127 uM; Vmax=182 pmol/mg protein/min

row_label: MAO-A / Tyramine

substrate: tyramine


enzyme_display_name: Amine oxidase [flavin-containing] B

normalized_value_unit_evidence: normalized: km=0.226 mM; Vmax is not kcat and is not used as kcat evidence

raw_value_unit_evidence: paper Table 2 cells: MAO-B Adrenaline Km=226 uM; Vmax=465 pmol/mg protein/min

row_label: MAO-B / Adrenaline

enzyme: Amine oxidase [flavin-containing] B


normalized_value_unit_evidence: normalized: km=0.229 mM; Vmax is not kcat and is not used as kcat evidence

raw_value_unit_evidence: paper Table 2 cells: MAO-B Dopamine Km=229 uM; Vmax=702 pmol/mg protein/min

row_label: MAO-B / Dopamine


normalized_value_unit_evidence: normalized: km=1.093 mM; Vmax is not kcat and is not used as kcat evidence

raw_value_unit_evidence: paper Table 2 cells: MAO-B 5-hydroxytryptamine Km=1093 uM; Vmax=7 pmol/mg protein/min

row_label: MAO-B / 5-hydroxytryptamine


normalized_value_unit_evidence: normalized: km=0.238 mM; Vmax is not kcat and is not used as kcat evidence

raw_value_unit_evidence: paper Table 2 cells: MAO-B Noradrenaline Km=238 uM; Vmax=321 pmol/mg protein/min

row_label: MAO-B / Noradrenaline


enzyme_display_name: N-methylputrescine oxidase 1, peroxisomal

organism: Nicotiana tabacum

smiles: CNCCCN

proof_lines:
N-methylputrescine oxidase
N-methylputrescine
symmetrical diamines


substrate_name: n-butylamine

smiles: CCCCN

enzyme: N-methylputrescine oxidase 1, peroxisomal

substrate: n-butylamine


enzyme_display_name: primary-amine oxidase

organism: Lens culinaris

substrate_name: tryptamine

source_db: brenda

enzyme: primary-amine oxidase

substrate: tryptamine

source: brenda


organism: Bos taurus

substrate_name: benzylamine

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

substrate: benzylamine


substrate_name: dioxygen

smiles: O=O

substrate: dioxygen


enzyme_display_name: Amine oxidase [copper-containing] zeta, peroxisomal

organism: Arabidopsis thaliana

substrate_name: putrescine

smiles: C(CCN)CN

proof_lines:
non-N-methylated amines
N-methylated amines

substrate: putrescine


substrate_name: N-methylputrescine

smiles: CNCCCCN

enzyme: Amine oxidase [copper-containing] zeta, peroxisomal

substrate: N-methylputrescine


substrate_name: cadaverine

smiles: C(CCN)CCN

substrate: cadaverine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T42A/C245S/L301V to reconstruct the assayed variant sequence.

proof_lines:
GlyOX
Bacillus subtilis
glycine


enzyme_display_name: L-lysine 6-oxidase

organism: Marinomonas mediterranea

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

sequence_source: multiple

proof_lines:
at pH 7.5 and 25°C
Raw SKiD Env: Temp=25°C, pH=7.5

source_databases_merged: brenda skid

enzyme: L-lysine 6-oxidase


proof_lines:
human monoamine oxidase B
beta-phenylethylamine
serotonin


organism: Escherichia coli


smiles: C(CN)CN

column_label: PMID 17174363 Table 1, 1,3-diamino propane row, Km (mM) = 0.35 +/- 0.03.

normalized_value_unit_evidence: Paper Km 0.35 mM; export Km 0.158 mM.

raw_value_unit_evidence: Table 1 reports Km = 0.35 +/- 0.03 mM for 1,3-diamino propane.

row_label: 1,3-diamino propane

table_label: Table 1. Enzyme kinetics of recombinant TRX-His6-MPO1 protein


organism: Rattus norvegicus

column_label: Table 3. Kinetic parameters of the two forms of MAO; row 2-Phenethylamine; rat brain MAO-A; Km column 327 uM normalized to 0.327 mM; Vmax column 53 pmol mg protein^-1 min^-1

raw_value_unit_evidence: Km 327 uM; Vmax 53 pmol mg protein^-1 min^-1

row_label: rat brain MAO-A / 2-Phenethylamine


normalized_value_unit_evidence: normalized: km=0.116 mM; Vmax is not kcat and is not used as kcat evidence

raw_value_unit_evidence: paper Table 3 cells: MAO-A Tyramine Km=116 uM; Vmax=258 pmol/mg protein/min

table_label: Table 3


substrate_name: kynuramine (with the detergent-solubilized form)


organism: Bacillus cereus

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

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

proof_lines: mutant enzyme G51R/D60G, at pH 8.5 and 60°C


proof_lines: mutant enzyme G51R/D60G/T118A/K133R, at pH 8.5 and 60°C


proof_lines: mutant enzyme G51R/D60G/K133R/V262I, at pH 8.5 and 60°C


proof_lines: mutant enzyme G51R/D60G/T118A/K133R/I284L, at pH 8.5 and 60°C


substrate_name: glyphosate

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

substrate: glyphosate


proof_lines: mutant enzyme BG51R/G60S/S210P/M267T, at pH 8.5 and 60°C


proof_lines: mutant enzyme G51R/G60S/T118A/K133R/I198V/V262I/I284L/L307S/E357G, at pH 8.5 and 60°C


proof_lines: mutant enzyme G51R/G60S/D121G/S122P/H164Y/M267T, at pH 8.5 and 60°C


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

proof_lines: wild type enzyme, at pH 7.5, temperature not specified in the publication


proof_lines: mutant enzyme G51R/G60S/K133R/S210P/R250G/V262I, at pH 8.5 and 60°C


proof_lines: mutant enzyme BG51R/G60S/I198V/E357G, at pH 8.5 and 60°C


substrate_name: D-proline

proof_lines: apparent value for mutant enzyme H244N, at 25°C and pH 8.5

substrate: D-proline


proof_lines: apparent value for mutant enzyme M261Y, at 25°C and pH 8.5


substrate_name: D-alanine

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

proof_lines: kcat above 0.33 1/s, apparent value for mutant enzyme M261H, at 25°C and pH 8.5

proof_lines: Km above 2000 mM, apparent value for mutant enzyme M261H, at 25°C and pH 8.5

substrate: D-alanine


substrate_name: sarcosine

substrate: sarcosine


assay_conditions_summary: pH 8.5; 298.15 K; cofactor FAD

proof_lines: apparent value for wild type enzyme, at 25°C and pH 8.5

proof_lines: wild type enzyme, in 0.4 mM 4-aminoantipyrine, 7 mM phenol, 4.4 U/ml horseradish peroxidase, 0.0002 mM FAD, and 75 mM sodium diphosphate (pH 8.5) at 37°C


substrate_name: glycine

proof_lines: apparent value for mutant enzyme M261H, at 25°C and pH 8.5

substrate: glycine


proof_lines: apparent value for mutant enzyme H244F, at 25°C and pH 8.5


proof_lines: apparent value for mutant enzyme H244Q, at 25°C and pH 8.5


proof_lines:
mutant H244A, pH 8.5, 25°C
mutant enzyme H244A, at pH 8.5 and 25°C


proof_lines:
mutant A54R, pH 8.5, 25°C
mutant enzyme A54R, at pH 8.5 and 25°C


proof_lines: mutant enzyme M49L/A54R/H244K, at pH 8.5 and 25°C


proof_lines: mutant enzyme H244K/M261R, at pH 8.5 and 25°C


proof_lines: mutant enzyme A54R/H244K/M261R, at pH 8.5 and 25°C


proof_lines: mutant enzyme A54R/H244K, at pH 8.5 and 25°C


organism: Rhodococcus opacus

substrate_name: methylamine

smiles: CN

proof_lines: isoform AO1, in 200 mM potassium phosphate buffer pH 7.6, at 30°C

substrate: methylamine


substrate_name: vanillylamine

substrate: vanillylamine


substrate_name: dopamine

proof_lines: isoform AO2, in 200 mM potassium phosphate buffer pH 7.6, at 30°C

substrate: dopamine


substrate_name: ethanolamine

smiles: C(CO)N

substrate: ethanolamine


substrate_name: octopamine

substrate: octopamine


substrate_name: Butylamine

substrate: Butylamine


substrate_name: amylamine

smiles: CCCCCN

substrate: amylamine


substrate_name: ethylamine

smiles: CCN

substrate: ethylamine


substrate_name: benzylamine

substrate: benzylamine


substrate_name: histamine

substrate: histamine


substrate_name: tyramine

substrate: tyramine


substrate_name: Propylamine

smiles: CCCN

substrate: Propylamine


substrate_name: Phenylethylamine

substrate: Phenylethylamine


substrate_name: kynuramine (with the detergent-solubilized form)


substrate_name: cysteamine

smiles: C(CS)N

substrate: cysteamine


substrate_name: phenethylamine

proof_lines: recombinant enzyme expressed in CHO cells

substrate: phenethylamine


substrate_name: aminoacetone

smiles: CC(=O)CN

substrate: aminoacetone


substrate_name: cyclohexanemethylamine

substrate: cyclohexanemethylamine


substrate_name: methylamine

substrate: methylamine


substrate_name: Isoamylamine

smiles: CC(C)CCN

substrate: Isoamylamine


substrate_name: Isobutylamine

smiles: CC(C)CN

substrate: Isobutylamine


substrate_name: glyphosate

proof_lines: mutant enzyme N336R, at pH 7.5, temperature not specified in the publication

substrate: glyphosate


substrate_name: glycine

substrate: glycine


proof_lines: mutant enzyme N336K, at pH 7.5, temperature not specified in the publication


proof_lines: mutant enzyme N336H, at pH 7.5, temperature not specified in the publication


proof_lines: mutant enzyme N336A, at pH 7.5, temperature not specified in the publication


proof_lines: mutant enzyme N336G, at pH 7.5, temperature not specified in the publication


substrate_name: D-alanine

proof_lines: wild type enzyme, at pH 7.5, temperature not specified in the publication

substrate: D-alanine


substrate_name: sarcosine

smiles: CNCC(=O)O

substrate: sarcosine


substrate_name: benzylamine

assay_conditions_summary: pH 7.4; 310.15 K; buffer assay

proof_lines: mutant enzyme L469G, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C


proof_lines: mutant enzyme M211V, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C


proof_lines: wild type enzyme, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C


proof_lines: mutant enzyme Y394N, in Krebs Ringer phosphate glucose buffer, pH 7.4, at 37°C


enzyme_display_name: aspartate dehydrogenase

organism: Archaeoglobus fulgidus

substrate_name: NADH

assay_conditions_summary: 323.15 K; cofactor NADH

proof_lines: pH not specified in the publication, 50°C

enzyme: aspartate dehydrogenase

substrate: NADH


substrate_name: NAD+

assay_conditions_summary: pH 11.6; 323.15 K; cofactor NAD+

substrate: NAD+


substrate_name: L-aspartate

assay_conditions_summary: pH 11.6; 323.15 K; cofactor NADP+

proof_lines:
with NAD+ as the electron acceptor
pH 11.6, 50°C, with NAD+
with NADP+ as the electron acceptor

substrate: L-aspartate


substrate_name: NADP+

substrate: NADP+


substrate_name: oxaloacetate

proof_lines: pH not specified in the publication, 50°C, with NADH

substrate: oxaloacetate


assay_conditions_summary: pH 8.5; 310.15 K; cofactor FAD

proof_lines: mutant enzyme I15V, in 0.4 mM 4-aminoantipyrine, 7 mM phenol, 4.4 U/ml horseradish peroxidase, 0.0002 mM FAD, and 75 mM sodium diphosphate (pH 8.5) at 37°C


substrate_name: N-ethylglycine

smiles: CCNCC(=O)O

substrate: N-ethylglycine


substrate_name: glycine-ethyl-ester

smiles: CCOC(=O)CN

substrate: glycine-ethyl-ester


proof_lines: wild type enzyme, in 0.4 mM 4-aminoantipyrine, 7 mM phenol, 4.4 U/ml horseradish peroxidase, 0.0002 mM FAD, and 75 mM sodium diphosphate (pH 8.5) at 37°C


substrate_name: D-proline

substrate: D-proline


substrate_name: D-pipecolate

substrate: D-pipecolate


substrate_name: N-ethyl-glycine

substrate: N-ethyl-glycine


enzyme_display_name: leucine dehydrogenase

assay_conditions_summary: pH 8.5; 303.15 K; cofactor NADH

enzyme: leucine dehydrogenase


substrate_name: trimethylpyruvate

substrate: trimethylpyruvate


enzyme_display_name: UniProt P23378

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt P23378

source: skid


substrate_name: tyramine

normalized_value_unit_evidence: normalized: km=0.107 mM; Vmax is not kcat and is not used as kcat evidence

raw_value_unit_evidence: paper Table 2 cells: MAO-B Tyramine Km=107 uM; Vmax=343 pmol/mg protein/min

row_label: MAO-B / Tyramine

substrate: tyramine


organism: Clostridium sp.

assay_conditions_summary: pH 7; 296.15 K; cofactor NADH


assay_conditions_summary: pH 6.6; 297.15 K; cofactor NAD+

proof_lines:
pH 6.6, 24°C, dimeric form of enzyme
pH 6.8, 24°C, tetrameric form of enzyme


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

proof_lines: pH 6.8, 24°C, tetrameric form of enzyme, pH 6.8

proof_lines: pH 6.8, 24°C, tetrameric form of enzyme, above pH 6.8

proof_lines: pH 6.6, 24°C, dimeric form of enzyme, pH 6.6


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


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

proof_lines:
pH 6.8, 24°C, tetrameric form of enzyme
pH 6.7, 24°C
pH 6.6, 24°C, dimeric form of enzyme

substrate: Unknown


enzyme_display_name: diaminopimelate dehydrogenase

organism: Brevibacterium sp.

assay_conditions_summary: cofactor NADP+

enzyme: diaminopimelate dehydrogenase


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


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


assay_conditions_summary: cofactor NAD+


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


smiles: N


organism: Cupriavidus necator

assay_conditions_summary: pH 8.2; 310.15 K; cofactor NADH

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


assay_conditions_summary: pH 10.2; 310.15 K; cofactor NAD+


assay_conditions_summary: pH 10.2; 310.15 K; cofactor NADP+

proof_lines:
pH 10.2, 37°C, with NAD+
pH 10.2, 37°C, with NADP+


proof_lines: pH not specified in the publication, 37°C, with NADH


organism: Rhodopseudomonas palustris

assay_conditions_summary: pH 9.8; 301.15 K; cofactor NAD+


assay_conditions_summary: pH 9.8; 301.15 K; cofactor NADP+


assay_conditions_summary: pH 9; 301.15 K; cofactor NADH


assay_conditions_summary: pH 9; 301.15 K; cofactor NADPH


enzyme_display_name: D-aspartate oxidase

substrate_name: DL-cysteic acid

enzyme: D-aspartate oxidase

substrate: DL-cysteic acid


substrate_name: D-aspartic acid-beta-hydroxamate

substrate: D-aspartic acid-beta-hydroxamate


substrate_name: cis-2,3-piperidine dicarboxylic acid

substrate: cis-2,3-piperidine dicarboxylic acid


substrate_name: D-homocysteic acid

substrate: D-homocysteic acid


substrate_name: D-alpha-aminoadipic acid

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

substrate: D-alpha-aminoadipic acid


substrate_name: glycyl-D-aspartic acid

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

substrate: glycyl-D-aspartic acid


enzyme_display_name: aminomethyltransferase

organism: Canis familiaris

substrate_name: 5,6,7,8-Tetrahydrofolate; NAD+; Glycine

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

enzyme: aminomethyltransferase

substrate: 5,6,7,8-Tetrahydrofolate; NAD+; Glycine


enzyme_display_name: glycine dehydrogenase (decarboxylating)

organism: Gallus gallus

substrate_name: GLDC; Methylamine

enzyme: glycine dehydrogenase (decarboxylating)

substrate: GLDC; Methylamine


substrate_name: Lipoylprotein; Glycine

substrate: Lipoylprotein; Glycine


organism: Homo sapiens

substrate_name: 5,6,7,8-Tetrahydrofolate; Glycine; NAD+

substrate: 5,6,7,8-Tetrahydrofolate; Glycine; NAD+


enzyme_display_name: dihydrolipoyl dehydrogenase

organism: Pisum sativum

enzyme: dihydrolipoyl dehydrogenase


substrate_name: NAD+; Glycine; 5,6,7,8-Tetrahydrofolate

substrate: NAD+; Glycine; 5,6,7,8-Tetrahydrofolate


enzyme_display_name: diamine oxidase

organism: Lathyrus cicera

enzyme: diamine oxidase


substrate_name: histamine

substrate: histamine


substrate_name: agmatine

smiles: C(CCN=C(N)N)CN

substrate: agmatine


substrate_name: spermine

smiles: C(CCNCCCN)CNCCCN

substrate: spermine


substrate_name: tyramine

substrate: tyramine


substrate_name: Phenylethylamine

substrate: Phenylethylamine


substrate_name: spermidine

smiles: C(CCNCCCN)CN

substrate: spermidine


substrate_name: putrescine

smiles: C(CCN)CN

substrate: putrescine


substrate_name: cadaverine

smiles: C(CCN)CCN

substrate: cadaverine


organism: Glycine max


substrate_name: Unknown

substrate: Unknown


organism: Lathyrus sativus

smiles: C(CN)C(CCN)O


substrate_name: cystamine

smiles: C(CSSCCN)N

substrate: cystamine


smiles: C(C=CCN)N


smiles: C(CN)C(CN)O


organism: Nicotiana tabacum

substrate_name: N-methylputrescine

smiles: CNCCCCN

proof_lines: Vmax: 28.8 nkat, pH and temperature not specified in the publication

substrate: N-methylputrescine


smiles: C(CN)CN

proof_lines: Vmax: 11.3 nkat, pH and temperature not specified in the publication


proof_lines: Vmax: 11.1 nkat, pH and temperature not specified in the publication


proof_lines: Vmax: 5.2 nkat, pH and temperature not specified in the publication


organism: Hyoscyamus niger

proof_lines: pH 7.9, 30°C, lowest KM-value compared with putrescine or cadaverine as substrates, Vmax: 90.4 pkat


proof_lines: pH 7.9, 30°C, higher KM-value compared with N-methylputrescine or cadaverine as substrates, Vmax: 82.7 pkat, specifiity constant 11% of the constant for N-methylputrescine


proof_lines: pH 7.9, 30°C, higher KM-value compared with N-putrescine or cadaverine as substrates, Vmax: 19.6 pkat, specifiity constant 1% of the constant for N-methylputrescine


organism: Lathyrus oleraceus


organism: Onobrychis viciifolia


smiles: C(COCCN)N


proof_lines: 30°C, pH 7.2, with respect to oxidative half-reaction


smiles: C(COCCOCCN)N


organism: Trifolium subterraneum


organism: Lathyrus odoratus


assay_conditions_summary: pH 7.4; 298.15 K; buffer 0.1 M phosphate

proof_lines: free enzyme, in 0.1 M phosphate buffer, pH 7.4, at 25°C

proof_lines: immobilized enzyme, apparent value, in 0.1 M phosphate buffer, pH 7.4, at 25°C


proof_lines: pH 7.9, 30°C, lowest KM-value compared with N-putrescine or cadaverine as substrates, Vmax: 96.2 pkat


proof_lines: pH 7.9, 30°C, highest KM-value compared with putrescine or cadaverine as substrates, Vmax: 93.5 pkat


organism: Phaseolus vulgaris


substrate_name: H2O; Putrescine; O2

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

substrate: H2O; Putrescine; O2


substrate_name: benzylamine

substrate: benzylamine


enzyme_display_name: L-arginine oxidase

organism: Pseudomonas sp.

substrate_name: L-arginine

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

enzyme: L-arginine oxidase

substrate: L-arginine


substrate_name: L-lysine

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

substrate: L-lysine


organism: Triticum aestivum


organism: Trichomonas vaginalis

substrate_name: Lipoamide

proof_lines: the apparent Km-value of rTvL for binding the free lipoamide

substrate: Lipoamide


substrate_name: rTvH1 protein

proof_lines: the apparent Km-value of rTvL for binding rTvH1

substrate: rTvH1 protein


organism: Arachis hypogaea


organism: Crystallibacter crystallopoietes

substrate_name: histamine

substrate: histamine


organism: Euphorbia characias


substrate_name: benzaldehyde

substrate: benzaldehyde


proof_lines:
xenon-treated enzyme
pH 7.0, 30°C


organism: Lens culinaris


proof_lines:
pH 7.0, 30°C
apparent value


organism: Oryza sativa


organism: Seriola quinqueradiata


organism: Yarrowia lipolytica


organism: Komagataella pastoris

proof_lines:
30°C, pH 7.0, per dimer
30°C, pH 7.0


smiles: O=O


proof_lines: 30°C, pH 7.0, with respect to oxidative half-reaction

proof_lines: 30°C, pH 7.0, with respect to reductive half-reaction


organism: Streptomyces sp. X-119-6

proof_lines: pH 8.0, 40°C, L-glutamate oxidase mutant R305E


organism: Vicia faba


organism: Glycine max

substrate_name: spermine

substrate: spermine


organism: Lathyrus oleraceus

proof_lines: reaction performed with benzylamine. KM value is too low to be measurable. Therefore, it is calculated from KCAT_KM with putrescine


proof_lines:
xenon-treated enzyme
pH 8.5, 25°C
30°C, pH 7.2, per dimer


substrate_name: Putrescine; H2O; O2

substrate: Putrescine; H2O; O2


substrate_name: glycine

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

substrate: glycine


organism: Synechococcus cedorum

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


enzyme_display_name: Diamine oxidase [copper-containing]

organism: Homo sapiens

substrate_name: histamine (at pH 7.5 and 37 degrees Celsius)

proof_lines: kcat is 139 min(-1) with histamine as substrate (at pH 7.5 and 37 degrees Celsius) (PubMed:12072962). kcat is 103 min(-1) with 1-methylhistamine as substrate (at pH 7.5 and 37 degrees Celsius) (PubMed:12072962). kcat is 475 min(-1) with put

enzyme: Diamine oxidase [copper-containing]


substrate_name: 1-methylhistamine (at pH 7.5 and 37 degrees Celsius)


substrate_name: cadaverine (at pH 7.5 and 37 degrees Celsius)


substrate_name: spermidine (at pH 7.5 and 37 degrees Celsius)


organism: Synechococcus elongatus


enzyme_display_name: homospermidine oxidase

organism: Heliotropium indicum

substrate_name: sym-homospermidine

smiles: C(CCNCCCCN)CN

enzyme: homospermidine oxidase

substrate: sym-homospermidine


enzyme_display_name: 7-chloro-L-tryptophan oxidase

organism: Lentzea aerocolonigenes

proof_lines: kcat is 12.12 min(-1), 1.53 min(-1), 14.32 min(-1), and 39.82 min(-1) for L-tryptophan, 1-methyl-L-tryptophan, 5-fluoro-L-tryptophan and 7-chloro-L-tryptophan, respectively (at pH 7.8).

source_databases_merged: brenda uniprot

enzyme: 7-chloro-L-tryptophan oxidase


substrate_name: L-Trp

substrate: L-Trp


substrate_name: putrescine (at pH 7.5 and 37 degrees Celsius)


organism: Synechocystis sp.

assay_conditions_summary: pH 6

proof_lines: P-subunit in the absesence of H-apoprotein, at pH 6

proof_lines: P-subunit in the presence of non-tagged lipoylated H-apoprotein, at pH 8

proof_lines: P-subunit in the presence of His-tagged non-lipoylated H-apoprotein, at pH 6


organism: Arthrobacter globiformis

proof_lines:
30°C, pH 7.2, per dimer
30°C, pH 7.2


substrate_name: Unknown

proof_lines: 30°C, pH 7.2, with respect to reductive half-reaction

proof_lines: 30°C, pH 7.2, with respect to oxidative half-reaction


enzyme_display_name: L-amino-acid oxidase 4

organism: Hebeloma cylindrosporum

enzyme: L-amino-acid oxidase 4


enzyme_display_name: L-amino-acid oxidase

organism: Mus musculus

enzyme: L-amino-acid oxidase


substrate_name: lipoylated H-apoprotein

proof_lines:
P-subunit, at pH 6
P-subunit, at pH 8

substrate: lipoylated H-apoprotein


organism: Aspergillus niger

substrate_name: aminopentane

smiles: CCCCCN

column_label: Table 3. Substrate specificity and kinetic constants for the two amine oxidases of A. niger; AO column group; row Pentylamine; Km (mM)=0.35; kcat (s^-1)=142; kcat/Km (mM^-1 s^-1)=406. Footnote a: calculated on a molecular mass of 83 kDa.

normalized_value_unit_evidence: Km normalized_value=0.35 normalized_unit=mM; kcat normalized_value=142 normalized_unit=s^-1

raw_value_unit_evidence: AO Table 3 row Pentylamine: Km raw_value=0.35 raw_unit=mM; kcat raw_value=142 raw_unit=s^-1; kcat/Km raw_value=406 raw_unit=mM^-1 s^-1

row_label: AO / Pentylamine

substrate: aminopentane


organism: Pisum sativum

substrate_name: O2; H2O; 3-Oxapentane 1,5-diamine

smiles: NCCOCCN

column_label: PMID 12686157 Table 1, OPD row, PSAO reaction column, Km or Ki = 0.2 mM; stoichiometry column = 1:1:1.

normalized_value_unit_evidence: Km 0.2 mM.

raw_value_unit_evidence: Table 1 lists OPD as PSAO substrate S (13%) with Km or Ki = 0.2 mM and stoichiometry 1:1:1.

row_label: OPD / PSAO reaction

table_label: Table 1. Results of kinetic measurements with PSAO and MPAO and the studied group of amine compounds

substrate: O2; H2O; 3-Oxapentane 1,5-diamine


organism: Sus scrofa

substrate_name: H2O; O2; N-Methylputrescine

substrate: H2O; O2; N-Methylputrescine


enzyme_display_name: Glycine dehydrogenase (decarboxylating), mitochondrial

organism: Gallus gallus

substrate_name: glycine in presence of GCSH

substrate: glycine in presence of GCSH


organism: Oryctolagus cuniculus

substrate_name: 5,6,7,8-Tetrahydrofolate; NAD+; Glycine

substrate: 5,6,7,8-Tetrahydrofolate; NAD+; Glycine


organism: Rattus norvegicus

substrate_name: Lipoylprotein; Glycine

substrate: Lipoylprotein; Glycine


substrate_name: L-glutamine (untreated)

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

column_label: Columns Substrate, vmax [U mg^-1], Km [mM], kcat [s^-1], kcat/Km; untreated top block row L-Glutamine.

raw_value_unit_evidence: Untreated Table 2 row L-Glutamine: vmax 2.22 +/- 0.65 U mg^-1; Km 0.46 +/- 0.07 mM; kcat 2.56 s^-1; kcat/Km 5.58.

row_label: L-Glutamine

table_label: Table 2, kinetic properties of untreated and acid-activated 6His-hcLAAO4

substrate: L-glutamine (untreated)


substrate_name: L-leucine (untreated)

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

substrate: L-leucine (untreated)


substrate_name: L-phenylalanine (untreated)

column_label: Columns Substrate, vmax [U mg^-1], Km [mM], kcat [s^-1], kcat/Km; untreated top block row L-Phenylalanine.

raw_value_unit_evidence: Untreated Table 2 row L-Phenylalanine: vmax 0.72 +/- 0.21 U mg^-1; Km 0.26 +/- 0.11 mM; kcat 0.83 s^-1; kcat/Km 3.14.

row_label: L-Phenylalanine

substrate: L-phenylalanine (untreated)


substrate_name: L-leucine methyl ester (untreated)

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

substrate: L-leucine methyl ester (untreated)


column_label: Table 1. Substrate specificity of recombinant RebO enzyme; row 1-Methyl-L-tryptophan; column Km (mM) raw 1.43 +/- 0.52 mM; column kcat (min^-1) raw 1.53 +/- 0.30 min^-1; column kcat/Km raw 1.07 min^-1 mM^-1.

raw_value_unit_evidence: Table 1, 1-Methyl-L-tryptophan row: Km column 1.43 +/- 0.52 mM; kcat column 1.53 +/- 0.30 min^-1; kcat/Km column 1.07 min^-1 mM^-1.


column_label: Table 1. Substrate specificity of recombinant RebO enzyme; row L-Tryptophan; column Km (mM) raw 1.53 +/- 0.61 mM; column kcat (min^-1) raw 12.12 +/- 0.61 min^-1; column kcat/Km raw 7.94 min^-1 mM^-1.

raw_value_unit_evidence: Table 1, L-Tryptophan row: Km column 1.53 +/- 0.61 mM; kcat column 12.12 +/- 0.61 min^-1; kcat/Km column 7.94 min^-1 mM^-1.

row_label: L-Tryptophan


substrate_name: L-phenylalanine

assay_conditions_summary: pH 5

column_label: Full text reports apparent maximum velocity 3.236 U/mg and Michaelis-Menten constant Km 1.48 mM for the human enzyme.

raw_value_unit_evidence: Km raw_value=1.48 mM raw_unit=mM

row_label: human IL4I1 / L-phenylalanine oxidase activity

table_label: Blood full-text Results prose / Figure 2

substrate: L-phenylalanine


substrate_name: benzylamine

column_label: Table 3. Substrate specificity and kinetic constants for the two amine oxidases of A. niger; AO column group; row Benzylamine; Km (mM)=0.24; kcat (s^-1)=37; kcat/Km (mM^-1 s^-1)=153. Footnote a: calculated on a molecular mass of 83 kDa.

normalized_value_unit_evidence: Km normalized_value=0.24 normalized_unit=mM; kcat normalized_value=37 normalized_unit=s^-1; kcat/Km normalized_value=153 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: AO Table 3 row Benzylamine: Km raw_value=0.24 raw_unit=mM; kcat raw_value=37 raw_unit=s^-1; kcat/Km raw_value=153 raw_unit=mM^-1 s^-1

row_label: AO / Benzylamine

substrate: benzylamine


substrate_name: norepinephrine

column_label: Table 3. Substrate specificity and kinetic constants for the two amine oxidases of A. niger; AO column group; row Norepinephrine; Km (mM)=1.05; kcat (s^-1)=65; kcat/Km (mM^-1 s^-1)=62. Footnote a: calculated on a molecular mass of 83 kDa.

normalized_value_unit_evidence: Km normalized_value=1.05 normalized_unit=mM; kcat normalized_value=65 normalized_unit=s^-1; kcat/Km normalized_value=62 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: AO Table 3 row Norepinephrine: Km raw_value=1.05 raw_unit=mM; kcat raw_value=65 raw_unit=s^-1; kcat/Km raw_value=62 raw_unit=mM^-1 s^-1

row_label: AO / Norepinephrine

substrate: norepinephrine


column_label: Table 3. Substrate specificity and kinetic constants for the two amine oxidases of A. niger; AO column group; row 1,4-Methylhistamine; Km (mM)=0.14; kcat (s^-1)=68; kcat/Km (mM^-1 s^-1)=488. Footnote a: calculated on a molecular mass of 83 kDa.

normalized_value_unit_evidence: Km normalized_value=0.14 normalized_unit=mM; kcat normalized_value=68 normalized_unit=s^-1; kcat/Km normalized_value=488 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: AO Table 3 row 1,4-Methylhistamine: Km raw_value=0.14 raw_unit=mM; kcat raw_value=68 raw_unit=s^-1; kcat/Km raw_value=488 raw_unit=mM^-1 s^-1

row_label: AO / 1,4-Methylhistamine


substrate_name: tyramine

column_label: Table 3. Substrate specificity and kinetic constants for the two amine oxidases of A. niger; AO column group; row Tyramine; Km (mM)=0.12; kcat (s^-1)=80; kcat/Km (mM^-1 s^-1)=667. Footnote a: calculated on a molecular mass of 83 kDa.

normalized_value_unit_evidence: Km normalized_value=0.12 normalized_unit=mM; kcat normalized_value=80 normalized_unit=s^-1; kcat/Km normalized_value=667 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: AO Table 3 row Tyramine: Km raw_value=0.12 raw_unit=mM; kcat raw_value=80 raw_unit=s^-1; kcat/Km raw_value=667 raw_unit=mM^-1 s^-1

row_label: AO / Tyramine

substrate: tyramine


substrate_name: histamine

column_label: Table 3. Substrate specificity and kinetic constants for the two amine oxidases of A. niger; AO column group; row Histamine; Km (mM)=0.6; kcat (s^-1)=95; kcat/Km (mM^-1 s^-1)=159. Footnote a: calculated on a molecular mass of 83 kDa.

normalized_value_unit_evidence: Km normalized_value=0.6 normalized_unit=mM; kcat normalized_value=95 normalized_unit=s^-1; kcat/Km normalized_value=159 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: AO Table 3 row Histamine: Km raw_value=0.6 raw_unit=mM; kcat raw_value=95 raw_unit=s^-1; kcat/Km raw_value=159 raw_unit=mM^-1 s^-1

row_label: AO / Histamine

substrate: histamine


substrate_name: tryptamine

column_label: Table 3. Substrate specificity and kinetic constants for the two amine oxidases of A. niger; AO column group; row Tryptamine; Km (mM)=0.1; kcat (s^-1)=100; kcat/Km (mM^-1 s^-1)=1004. Footnote a: calculated on a molecular mass of 83 kDa.

normalized_value_unit_evidence: Km normalized_value=0.1 normalized_unit=mM; kcat normalized_value=100 normalized_unit=s^-1; kcat/Km normalized_value=1004 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: AO Table 3 row Tryptamine: Km raw_value=0.1 raw_unit=mM; kcat raw_value=100 raw_unit=s^-1; kcat/Km raw_value=1004 raw_unit=mM^-1 s^-1

row_label: AO / Tryptamine

substrate: tryptamine


substrate_name: octopamine

column_label: Table 3. Substrate specificity and kinetic constants for the two amine oxidases of A. niger; AO column group; row Octopamine; Km (mM)=0.36; kcat (s^-1)=122; kcat/Km (mM^-1 s^-1)=338. Footnote a: calculated on a molecular mass of 83 kDa.

normalized_value_unit_evidence: Km normalized_value=0.36 normalized_unit=mM; kcat normalized_value=122 normalized_unit=s^-1; kcat/Km normalized_value=338 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: AO Table 3 row Octopamine: Km raw_value=0.36 raw_unit=mM; kcat raw_value=122 raw_unit=s^-1; kcat/Km raw_value=338 raw_unit=mM^-1 s^-1

row_label: AO / Octopamine

substrate: octopamine


substrate_name: Aminopropane

smiles: CCCN

column_label: Table 3. Substrate specificity and kinetic constants for the two amine oxidases of A. niger; AO column group; row Propylamine; Km (mM)=1.6; kcat (s^-1)=132; kcat/Km (mM^-1 s^-1)=82. Footnote a: calculated on a molecular mass of 83 kDa.

normalized_value_unit_evidence: Km normalized_value=1.6 normalized_unit=mM; kcat normalized_value=132 normalized_unit=s^-1; kcat/Km normalized_value=82 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: AO Table 3 row Propylamine: Km raw_value=1.6 raw_unit=mM; kcat raw_value=132 raw_unit=s^-1; kcat/Km raw_value=82 raw_unit=mM^-1 s^-1

row_label: AO / Propylamine

substrate: Aminopropane


substrate_name: aminobutane

smiles: CCCCN

column_label: Table 3. Substrate specificity and kinetic constants for the two amine oxidases of A. niger; AO column group; row Butylamine; Km (mM)=0.6; kcat (s^-1)=132; kcat/Km (mM^-1 s^-1)=220. Footnote a: calculated on a molecular mass of 83 kDa.

normalized_value_unit_evidence: Km normalized_value=0.6 normalized_unit=mM; kcat normalized_value=132 normalized_unit=s^-1; kcat/Km normalized_value=220 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: AO Table 3 row Butylamine: Km raw_value=0.6 raw_unit=mM; kcat raw_value=132 raw_unit=s^-1; kcat/Km raw_value=220 raw_unit=mM^-1 s^-1

row_label: AO / Butylamine

substrate: aminobutane


substrate_name: dopamine

column_label: Table 3. Substrate specificity and kinetic constants for the two amine oxidases of A. niger; AO column group; row Dopamine; Km (mM)=0.6; kcat (s^-1)=135; kcat/Km (mM^-1 s^-1)=225. Footnote a: calculated on a molecular mass of 83 kDa.

normalized_value_unit_evidence: Km normalized_value=0.6 normalized_unit=mM; kcat normalized_value=135 normalized_unit=s^-1; kcat/Km normalized_value=225 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: AO Table 3 row Dopamine: Km raw_value=0.6 raw_unit=mM; kcat raw_value=135 raw_unit=s^-1; kcat/Km raw_value=225 raw_unit=mM^-1 s^-1

row_label: AO / Dopamine

substrate: dopamine


substrate_name: glycine

enzyme: Glycine dehydrogenase (decarboxylating), mitochondrial

substrate: glycine


substrate_name: lipoic acid

substrate: lipoic acid


substrate_name: methylamine

smiles: CN

substrate: methylamine


enzyme_display_name: UniProt P55038

organism: Synechocystis sp. PCC 6803

substrate_name: L-glutamine

assay_conditions_summary: pH 8

enzyme: UniProt P55038

substrate: L-glutamine


substrate_name: L-methionine (untreated)

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

assay_conditions_summary: pH 7; buffer TEA

column_label: Table 2; row l-methionine; untreated columns Km (mM) and vmax (U/mg).

normalized_value_unit_evidence: Untreated l-methionine Km is already reported as 0.16 mM, matching the export.

raw_value_unit_evidence: Table 2 row l-methionine reports untreated Km 0.16 +/- 0.10 mM and vmax 5.98 +/- 0.38 U/mg; activated Km is separate at 0.41 +/- 0.17 mM.

row_label: l-methionine, untreated 9His-hcLAAO4

table_label: Table 2: Kinetic properties of untreated and acid-activated 9His-hcLAAO4

substrate: L-methionine (untreated)


substrate_name: L-phenylalanine methyl ester (untreated)


organism: Streptomyces sp. X-119-6

substrate_name: L-Arginine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R305E with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.

substrate: L-Arginine


substrate_name: phenylalanine (at 37 degrees Celsius)

substrate: phenylalanine (at 37 degrees Celsius)


enzyme_display_name: methylamine dehydrogenase (amicyanin)

organism: Paracoccus denitrificans

substrate_name: Amylamine

enzyme: methylamine dehydrogenase (amicyanin)

substrate: Amylamine


smiles: NCCCCCCN


smiles: NCCCCCCCCCN


smiles: NCCCCCCCCN


substrate_name: Propylamine

substrate: Propylamine


substrate_name: Cadaverine

smiles: NCCCCCN

substrate: Cadaverine


substrate_name: serotonin

column_label: Table 3. Substrate specificity and kinetic constants for the two amine oxidases of A. niger; AO column group; row Serotonin; Km (mM)=0.29; kcat (s^-1)=136; kcat/Km (mM^-1 s^-1)=469. Footnote a: calculated on a molecular mass of 83 kDa.

normalized_value_unit_evidence: Km normalized_value=0.29 normalized_unit=mM; kcat normalized_value=136 normalized_unit=s^-1; kcat/Km normalized_value=469 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: AO Table 3 row Serotonin: Km raw_value=0.29 raw_unit=mM; kcat raw_value=136 raw_unit=s^-1; kcat/Km raw_value=469 raw_unit=mM^-1 s^-1

row_label: AO / Serotonin

substrate: serotonin


column_label: Table 3. Substrate specificity and kinetic constants for the two amine oxidases of A. niger; AO column group; row 2-Phenethylamine; Km (mM)=0.12; kcat (s^-1)=137; kcat/Km (mM^-1 s^-1)=1142. Footnote a: calculated on a molecular mass of 83 kDa.

normalized_value_unit_evidence: Km normalized_value=0.12 normalized_unit=mM; kcat normalized_value=137 normalized_unit=s^-1; kcat/Km normalized_value=1142 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: AO Table 3 row 2-Phenethylamine: Km raw_value=0.12 raw_unit=mM; kcat raw_value=137 raw_unit=s^-1; kcat/Km raw_value=1142 raw_unit=mM^-1 s^-1

row_label: AO / 2-Phenethylamine


substrate_name: aminohexane

substrate: aminohexane


substrate_name: ethylamine

smiles: CCN

substrate: ethylamine


substrate_name: Butylamine

substrate: Butylamine


substrate_name: Acceptor; H2O; Methylamine

substrate: Acceptor; H2O; Methylamine


substrate_name: H2O; Butylamine; Acceptor

substrate: H2O; Butylamine; Acceptor


enzyme_display_name: D-amino acid dehydrogenase (quinone)

organism: Escherichia coli B

substrate_name: D-glutamine

enzyme: D-amino acid dehydrogenase (quinone)

substrate: D-glutamine


substrate_name: D-serine

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

substrate: D-serine


substrate_name: D-proline

substrate: D-proline


substrate_name: D-phenylalanine

substrate: D-phenylalanine


substrate_name: D-alanine

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

proof_lines:
with ferricyanide
with 2,6-dichlorophenolindophenol
with coenzyme Q

substrate: D-alanine


substrate_name: D-2-amino butyrate

proof_lines:
coenzyme Q mediated
with D-alanine
with 2,6-dichlorophenolindophenol

substrate: D-2-amino butyrate


substrate_name: D-methionine

substrate: D-methionine


organism: Pseudomonas aeruginosa

proof_lines:
purified preparation
solubilized enzyme
native enzyme


substrate_name: D-cycloserine

substrate: D-cycloserine


smiles: NCCCCCCCCCCN


smiles: NCCCCCCCN


enzyme_display_name: glutamate synthase (ferredoxin)

organism: Hydrogenobacter thermophilus

substrate_name: reduced bacterial ferredoxin 1

enzyme: glutamate synthase (ferredoxin)

substrate: reduced bacterial ferredoxin 1


proof_lines: in 20 mM NaPO4 (pH 7.2), 10 mM L-glutamine, 5 mM methylviologen, 5 mM dithionite, at 70°C


substrate_name: L-glutamine

proof_lines: in 20 mM NaPO4 (pH 7.2), 1 mM 2-oxoglutarate, 5 mM methylviologen, 5 mM dithionite, at 70°C

substrate: L-glutamine


organism: Medicago sativa

substrate_name: reduced ferredoxin

substrate: reduced ferredoxin


organism: Pseudomonas reinekei


enzyme_display_name: taurine dehydrogenase

organism: Bacteria

substrate_name: phenazine methosulfate

enzyme: taurine dehydrogenase

substrate: phenazine methosulfate


substrate_name: taurine

substrate: taurine


organism: Haloferax mediterranei


enzyme_display_name: Aralkylamine dehydrogenase light chain

organism: Alcaligenes faecalis

substrate_name: tyramine

proof_lines: The enzyme is substrate inhibited at high substrate concentrations (Ki=1.08 mM for tyramine).

enzyme: Aralkylamine dehydrogenase light chain

substrate: tyramine


enzyme_display_name: Aralkylamine dehydrogenase heavy chain

enzyme: Aralkylamine dehydrogenase heavy chain


organism: Synechocystis sp.

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R1162A with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.

proof_lines: mutant R1162A, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature N1147A with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.

proof_lines: mutant N1147A, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature H1144Q with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.

proof_lines: mutant H1144Q, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature W676A with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.

proof_lines: mutant W676A, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature W676F with inferred residue-numbering offset +8 to reconstruct the assayed variant sequence.

proof_lines: mutant W676F, pH not specified in the publication, temperature not specified in the publication


organism: Solanum lycopersicum


substrate_name: 2-Phenylethylamine; Acceptor; H2O

substrate: 2-Phenylethylamine; Acceptor; H2O


substrate_name: Acceptor; H2O; Methylamine

substrate: Acceptor; H2O; Methylamine


substrate_name: Ethylamine; Acceptor; H2O

substrate: Ethylamine; Acceptor; H2O


substrate_name: Amicyanin; H2O; Methylamine

substrate: Amicyanin; H2O; Methylamine


enzyme_display_name: aralkylamine dehydrogenase

substrate_name: Acceptor; Tyramine; H2O

enzyme: aralkylamine dehydrogenase

substrate: Acceptor; Tyramine; H2O


substrate_name: Tyramine; Acceptor; H2O

substrate: Tyramine; Acceptor; H2O


substrate_name: oxidized ferredoxin

substrate: oxidized ferredoxin


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: D-amino acid dehydrogenase

organism: Helicobacter pylori

substrate_name: D-proline

enzyme: D-amino acid dehydrogenase

substrate: D-proline


substrate_name: D-alanine

proof_lines:
DadA
D-proline
coenzyme Q1

substrate: D-alanine


substrate_name: coenzyme Q1

substrate: coenzyme Q1


substrate_name: DCIP

substrate: DCIP


organism: Desmonostoc muscorum


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


enzyme_display_name: aralkylamine dehydrogenase (azurin)

organism: Achromobacter xylosoxidans

substrate_name: beta-phenylethylamine

column_label: PMID 15388968 abstract and PDF page 1926; enzyme aromatic amine dehydrogenase; substrate beta-phenylethylamine; metric Michaelis constant/Km; raw value 1.8 microM; normalized value 0.0018 mM.

normalized_value_unit_evidence: 1.8 microM normalized to 0.0018 mM.

raw_value_unit_evidence: PubMed abstract and PDF kinetic-parameter section report beta-phenylethylamine Michaelis constant = 1.8 microM.

row_label: aromatic amine dehydrogenase / beta-phenylethylamine Km

table_label: PubMed abstract plus J-STAGE PDF prose (PMID 15388968; PDF page 1926)

enzyme: aralkylamine dehydrogenase (azurin)

substrate: beta-phenylethylamine


column_label: PMID 15388968 abstract and PDF page 1926; enzyme aromatic amine dehydrogenase; substrate tyramine; metric Michaelis constant/Km; raw value 6.9 microM; normalized value 0.0069 mM.

normalized_value_unit_evidence: 6.9 microM normalized to 0.0069 mM.

raw_value_unit_evidence: PubMed abstract and PDF kinetic-parameter section report tyramine Michaelis constant = 6.9 microM.

row_label: aromatic amine dehydrogenase / tyramine Km


column_label: Figure 5A and adjacent Results prose. Double-reciprocal analysis of variable PMS; row/segment Phenazine methosulfate (PMS); column/metric Michaelis constant (Km)

raw_value_unit_evidence: The Results state that the Km for phenazine methosulfate was 48.1 uM.

row_label: Phenazine methosulfate (PMS)


substrate_name: histamine

column_label: PMID 15388968 abstract and PDF page 1926; enzyme aromatic amine dehydrogenase; substrate histamine; metric Michaelis constant/Km; raw value 171 microM; normalized value 0.171 mM.

normalized_value_unit_evidence: 171 microM normalized to 0.171 mM.

raw_value_unit_evidence: PubMed abstract and PDF kinetic-parameter section report histamine Michaelis constant = 171 microM.

row_label: aromatic amine dehydrogenase / histamine Km

substrate: histamine


substrate_name: L-glutamine

substrate: L-glutamine


organism: Homo sapiens

substrate_name: glycine

substrate: glycine


enzyme_display_name: leucine dehydrogenase

organism: Lysinibacillus sphaericus

substrate_name: NAD+

enzyme: leucine dehydrogenase

substrate: NAD+


substrate_name: L-Val

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

substrate: L-Val


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


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


enzyme_display_name: glutamate dehydrogenase (NADP+)

organism: Escherichia coli

substrate_name: NADP+

assay_conditions_summary: pH 8; cofactor NADP+

proof_lines: mutant K286Q/R289Q/R292Q/S264L, pH 8.0, temperature not specified in the publication

enzyme: glutamate dehydrogenase (NADP+)

substrate: NADP+


proof_lines: mutant K286Q/R289Q/R292Q/S264L/S240A, pH 8.0, temperature not specified in the publication


proof_lines: mutant K286Q/R289Q/R292Q, pH 8.0, temperature not specified in the publication

proof_lines: mutant K286Q/R289Q/R292Q , pH 8.0, temperature not specified in the publication


proof_lines: mutant K286Q, pH 8.0, temperature not specified in the publication


proof_lines: mutant K289Q, pH 8.0, temperature not specified in the publication


proof_lines: mutant K292Q, pH 8.0, temperature not specified in the publication


enzyme_display_name: glutamate dehydrogenase [NAD(P)+]

organism: Pyrococcus

substrate_name: glutamate

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

proof_lines:
concentration range: 0.05-1.0 mM
concentration range: 1.0-10.0 mM

enzyme: glutamate dehydrogenase [NAD(P)+]

substrate: glutamate


proof_lines:
concentration range: 0.2-5 mM
concentration range: 10-200 mM


substrate_name: NADH

substrate: NADH


substrate_name: NADPH

substrate: NADPH


organism: Bacillus cereus

proof_lines:
wild-type, pH 7.5, 37°C
wild-type, pH 9.5, 35°C


enzyme_display_name: D-aspartate oxidase

organism: Mus musculus

substrate_name: D-histidine

enzyme: D-aspartate oxidase

substrate: D-histidine


substrate_name: D-asparagine

substrate: D-asparagine


substrate_name: D-glutamate

substrate: D-glutamate


substrate_name: N-Methyl-D-aspartate

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

substrate: N-Methyl-D-aspartate


enzyme_display_name: D-arginine dehydrogenase

organism: Pseudomonas aeruginosa

substrate_name: D-Lysine

enzyme: D-arginine dehydrogenase

substrate: D-Lysine


substrate_name: D-phenylalanine

substrate: D-phenylalanine


substrate_name: D-Tyrosine

substrate: D-Tyrosine


substrate_name: D-Methionine

substrate: D-Methionine


enzyme_display_name: UniProt P32322

enzyme: UniProt P32322


enzyme_display_name: dihydrofolate reductase

organism: Crithidia fasciculata

substrate_name: dihydropteroate

enzyme: dihydrofolate reductase

substrate: dihydropteroate


substrate_name: L-threo-neopterin

substrate: L-threo-neopterin


enzyme_display_name: UniProt G4VJD6

organism: Schistosoma mansoni

enzyme: UniProt G4VJD6


enzyme_display_name: UniProt J9F199

organism: Wuchereria bancrofti

enzyme: UniProt J9F199


enzyme_display_name: UniProt O30463

organism: Mycobacterium avium

enzyme: UniProt O30463


enzyme_display_name: UniProt P0ABQ4

proof_lines:
Raw SKiD Env: Temp=-----, pH=7.5
Raw SKiD Env: Temp=15°C, pH=7

enzyme: UniProt P0ABQ4


enzyme_display_name: UniProt P16184

organism: Pneumocystis carinii

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

enzyme: UniProt P16184


proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.4
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=-----, pH=7


enzyme_display_name: UniProt Q54801

organism: Streptococcus pneumoniae

substrate_name: dihydrofolate

enzyme: UniProt Q54801

substrate: dihydrofolate


enzyme_display_name: UniProt Q81R22

organism: Bacillus anthracis

enzyme: UniProt Q81R22


enzyme_display_name: UniProt P00374

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.4
Raw SKiD Env: Temp=23°C, pH=7.6

enzyme: UniProt P00374


enzyme_display_name: UniProt P13922

organism: Plasmodium falciparum

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=-----, pH=7
Raw SKiD Env: Temp=25°C, pH=5

enzyme: UniProt P13922


proof_lines:
Raw SKiD Env: Temp=25°C, pH=5
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=-----, pH=7


enzyme_display_name: UniProt P24186

enzyme: UniProt P24186


enzyme_display_name: Bifunctional protein FolD

organism: Photobacterium phosphoreum

substrate_name: NADP(+)

enzyme: Bifunctional protein FolD

substrate: NADP(+)


substrate_name: NAD(+)

substrate: NAD(+)


enzyme_display_name: leucine dehydrogenase

organism: Pseudoalteromonas sp. ANT 178

substrate_name: L-arginine

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

enzyme: leucine dehydrogenase

substrate: L-arginine


substrate_name: DL-methionine

substrate: DL-methionine


substrate_name: L-proline

substrate: L-proline


substrate_name: L-tyrosine

substrate: L-tyrosine


substrate_name: L-leucine

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

substrate: L-leucine


enzyme_display_name: pyrroline-5-carboxylate reductase

organism: Rattus norvegicus

enzyme: pyrroline-5-carboxylate reductase


organism: Homo sapiens


organism: Colwellia psychrerythraea

assay_conditions_summary: pH 10.5; 303.15 K; cofactor NADP+

proof_lines:
pH 10.5, 30°C, coenzyme: NAD+
pH 10.5, 30°C, coenzyme: NADP+


substrate_name: L-pipecolate

substrate: L-pipecolate


assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADPH

proof_lines:
pH 6.5, 30°C, coenzyme: NADH
pH 6.5, 30°C, coenzyme: NADPH


organism: Human gammaherpesvirus 8


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

proof_lines: for native and recombinant enzymes, monophasic

substrate: NADPH


substrate_name: Unknown

substrate: Unknown


organism: Tequatrovirus T4


organism: Chloroidium saccharophilum

substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


organism: Ureibacillus thermosphaericus

substrate_name: 2-oxo-4-methylvaleric acid

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

substrate: 2-oxo-4-methylvaleric acid


organism: Hyphomicrobium zavarzinii

proof_lines: bifunctional methylenetetrahydrofolate dehydrogenase-cyclohydrolase enzyme


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

substrate: NADP+


organism: Lacticaseibacillus casei

proof_lines:
isozyme I
+ NADPH


organism: Salmonella enterica subsp. enterica serovar Typhimurium


organism: unknown prokaryotic organism

substrate_name: Dihydrofolate; NADPH; H+

substrate: Dihydrofolate; NADPH; H+


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M1A/C85A/C152S to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M1P/C85A/C152S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature C85A/C152S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M1S/C85A/C152S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M1A/M16S/M20L/M42Y/M92F/C85A/C152S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M1A/M16F/M20L/M42Y/M92F/C85A/C152S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M1A/M16N/M20L/M42Y/M92F/C85A/C152S to reconstruct the assayed variant sequence.


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

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADPH

proof_lines: kcat is 70.4 sec(-1) for the NADH-dependent reduction of (S)-1-pyrroline-5-carboxylate. kcat is 29.4 sec(-1) for the NADPH-dependent reduction of (S)-1-pyrroline-5-carboxylate (PubMed:23024808). kcat is 31 sec(-1) for the NADPH-dependent re

source_databases_merged: skid uniprot


assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADH


enzyme_display_name: UniProt Q96C36

proof_lines: kcat is 149 sec(-1) for the NADH-dependent reduction of (S)-1-pyrroline-5-carboxylate. kcat is 85 sec(-1) for the NADPH-dependent reduction of (S)-1-pyrroline-5-carboxylate (PubMed:23024808). kcat is 218.8 sec(-1) for the oxidation of NADH

enzyme: UniProt Q96C36


enzyme_display_name: Pyrroline-5-carboxylate reductase 3

substrate_name: (S)-1-pyrroline-5-carboxylate (in the presence of NADH)

proof_lines: kcat is 197 sec(-1) for the NADH-dependent reduction of (S)-1-pyrroline-5-carboxylate. kcat is 35 sec(-1) for the NADPH-dependent reduction of (S)-1-pyrroline-5-carboxylate (PubMed:23024808). 146 kcat is sec(-1) for the NADH-dependent reduc

enzyme: Pyrroline-5-carboxylate reductase 3


organism: Azospirillum brasilense

assay_conditions_summary: pH 6.5; cofactor NADP+

proof_lines: purified recombinant His-tagged enzyme, with NAD+, pH 6.5, 30°C

proof_lines: purified recombinant His-tagged enzyme, with NADP+, pH 6.5, 30°C


assay_conditions_summary: pH 6.5; cofactor NADPH

proof_lines: purified recombinant His-tagged enzyme, with NADH, pH 6.5, 30°C

proof_lines: purified recombinant His-tagged enzyme, with NADPH, pH 6.5, 30°C


organism: Drosophila melanogaster

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Q134K with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


assay_conditions_summary: pH 8.5; 298.15 K; cofactor NADPH

column_label: Table 2 row WT, column Km DHF (uM): 1.19 +/- 0.35

row_label: WT


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature L30Q with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


column_label: Table 2 row WT, column Km NADPH (uM): 6.9 +/- 1.3

raw_value_unit_evidence: Km NADPH 6.9 +/- 1.3 uM


enzyme_display_name: UniProt Q9HXE3

organism: Pseudomonas aeruginosa

substrate_name: D-methionine

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

proof_lines: kcat is 204 sec(-1) for dehydrogenase activity with D-arginine as substrate (at pH 8.7 and 25 degrees Celsius). kcat is 154 sec(-1) for dehydrogenase activity with D-methionine as substrate (at pH 8.7 and 25 degrees Celsius). kcat is 141 se

enzyme: UniProt Q9HXE3

substrate: D-methionine


substrate_name: D-Lysine

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

substrate: D-Lysine


substrate_name: D-histidine

substrate: D-histidine


substrate_name: D-phenylalanine

substrate: D-phenylalanine


substrate_name: D-tyrosine

substrate: D-tyrosine


enzyme_display_name: dihydrofolate reductase

organism: Leishmania major

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

enzyme: dihydrofolate reductase


enzyme_display_name: Hydrogen cyanide synthase subunit HcnA

organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

substrate_name: glycine

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

enzyme: Hydrogen cyanide synthase subunit HcnA

substrate: glycine


enzyme_display_name: Hydrogen cyanide synthase subunit HcnC

enzyme: Hydrogen cyanide synthase subunit HcnC


enzyme_display_name: Hydrogen cyanide synthase subunit HcnB

enzyme: Hydrogen cyanide synthase subunit HcnB


organism: Mus musculus

proof_lines:
altered enzyme
pH 7.4, 37°C


assay_conditions_summary: pH 7.4; cofactor NADPH


enzyme_display_name: Pyrroline-5-carboxylate reductase 1, mitochondrial

organism: Homo sapiens

substrate_name: NAD(+)

substrate: NAD(+)


substrate_name: NADP(+)

enzyme: Pyrroline-5-carboxylate reductase 1, mitochondrial

substrate: NADP(+)


substrate_name: D-leucine

proof_lines:
Raw SKiD Env: Temp=25°C, pH=10
Raw SKiD Env: Temp=25°C, pH=8.7
Raw SKiD Env: Temp=25°C, pH=6

substrate: D-leucine


substrate_name: D-arginine

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=25°C, pH=8.7
Raw SKiD Env: Temp=25°C, pH=5.5

substrate: D-arginine


substrate_name: NADPH


enzyme_display_name: Pyrroline-5-carboxylate reductase 2

substrate_name: pyrroline-5-carboxylate (in the presence of NADH)

enzyme: Pyrroline-5-carboxylate reductase 2


organism: Lathyrus oleraceus

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

proof_lines:
etiolated shoots
chloroplast


substrate_name: NADH

proof_lines:
chloroplast
etiolated shoots


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K32M/Q67H to reconstruct the assayed variant sequence.

proof_lines: mutant carrying the K32M mutation in gene copies 1 and 3 with the Q67H mutation in all gene copies, pH 7.0, 30°C

proof_lines: mutant isoform that carries the K32M mutation in gene copies 1 and 3 and the Q67H mutation in gene copies 2 and 4, pH 7.0, 30°C


assay_conditions_summary: pH 7; cofactor NADPH


enzyme_display_name: Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase 2, mitochondrial

organism: Rattus norvegicus

proof_lines: Has similar catalytic efficiencies, at physiological concentrations, with either NAD(+) or NADP(+) as substrates for the dehydrogenation of (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate.


enzyme: Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase 2, mitochondrial


substrate_name: 5,10-methylenetetrahydrofolate (in presence of NAD(+))


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V115C with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -8, so it is treated as a source-provided variant sequence.


organism: Moritella japonica

proof_lines: pH 7.0, 25°C, under atmospheric pressure


substrate_name: dihydrofolate

substrate: dihydrofolate


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature L20M to reconstruct the assayed variant sequence.


substrate: NADPH


enzyme_display_name: Dihydrofolate reductase

organism: Schistosoma mansoni

proof_lines: kcat is 35.9 sec(-1) for dihydrofolate. kcat is 130 sec(-1) for NADPH.

enzyme: Dihydrofolate reductase


organism: Thermotoga maritima


proof_lines:
recombinant enzyme
Raw SKiD Env: Temp=20°C, pH=7


proof_lines:
recombinant enzyme
Raw SKiD Env: Temp=-----, pH=-----


enzyme_display_name: FAD-dependent catabolic D-arginine dehydrogenase DauA

substrate_name: D-ornithine (at pH 8.7 and 37 degrees Celsius)

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


substrate_name: NADP+

assay_conditions_summary: pH 7.3; cofactor NADP+

proof_lines: 25 mM MOPS pH 7.3, 2.5 mM formaldehyde, 30 mM 2-mercaptoethanol, 27°C, with 250 microM 5,10-methylene-tetrahydrofolate


proof_lines: 25 mM MOPS pH 7.3, 2.5 mM formaldehyde, 1 mM NADP+, 30 mM 2-mercaptoethanol, 27°C


mutation_signature: Δ1

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Δ1 to reconstruct the assayed variant sequence.

mutation_type: deletion

proof_lines:
+ DELTA1-piperidine-2-carboxylate
+ DELTA1-pyrroline-2-carboxylate


organism: Crithidia fasciculata

proof_lines: with 7,8-dihydrofolate or 6-hydroxymetylpterin


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M1A/M16N/M20L/M42Y/C85A/M92F/C152S to reconstruct the assayed variant sequence.


organism: Leishmania braziliensis

assay_conditions_summary: pH 6


substrate_name: folate

proof_lines: bifunctional enzyme DHFR-thymidylate synthase

substrate: folate


organism: Gallus gallus

substrate_name: Dihydrofolate; NADPH; H+


substrate_name: H+; Dihydrofolate; NADPH

substrate: H+; Dihydrofolate; NADPH


organism: Lactobacillus casei


substrate_name: NADPH; Folate; H+

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

substrate: NADPH; Folate; H+


organism: Leishmania tarentolae

substrate_name: NADPH; H+; Folate

substrate: NADPH; H+; Folate


substrate_name: Dihydrofolate; H+; NADPH

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADPH

substrate: Dihydrofolate; H+; NADPH


organism: Plasmodium falciparum


organism: Pneumocystis carinii

substrate: Dihydrofolate; NADPH; H+


organism: Pneumocystis jiroveci


substrate_name: H+; NADPH; Dihydrofolate

substrate: H+; NADPH; Dihydrofolate


organism: Trypanosoma brucei brucei


organism: Trypanosoma cruzi


organism: Bos taurus

substrate_name: Folate; H+; NADPH

substrate: Folate; H+; NADPH


organism: Crithidia oncopelti

substrate_name: NADPH; H+; Dihydrofolate

column_label: Page 453 Summary gives 1 x 10^-5 M for NADPH; page 455 prose gives cofactor Km 1 x 10^-5 M

raw_value_unit_evidence: Paper reports cofactor Km values for the two enzymes essentially the same at 1 x 10^-5 M for NADPH

row_label: C. oncopelti / NADPH cofactor Km

table_label: BBA 178:453-458 summary and page 455 prose

substrate: NADPH; H+; Dihydrofolate


organism: Enterococcus faecium


organism: Escherichia coli


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

assay_conditions_summary: pH 7.5; cofactor NADPH


enzyme_display_name: pyrroline-2-carboxylate reductase

organism: Azospirillum brasilense

substrate_name: NADPH; 1-Pyrroline-2-carboxylate; H+

proof_lines: purified recombinant His-tagged enzyme, with NADPH, pH 6.5, 30°C

enzyme: pyrroline-2-carboxylate reductase

substrate: NADPH; 1-Pyrroline-2-carboxylate; H+


substrate_name: Delta(1)-pyrroline-2-carboxylate (using NADPH, at pH 6.5)

sequence_variant_note: Mutation signature H2C could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: kcat is 31400 min(-1) for Pyr2C reduction using NADPH. kcat is 36900 min(-1) for Pyr2C reduction using NADH. kcat is 9950 min(-1) for Pip2C reduction using NADPH. kcat is 9690 min(-1) for Pip2C reduction using NADH. kcat is 621 min(-1) for


organism: Mus musculus

substrate_name: Unknown

substrate: Unknown


organism: Homo sapiens

substrate_name: H+; (S)-1-Pyrroline-5-carboxylate; NADH

proof_lines: kcat is 149 sec(-1) for the NADH-dependent reduction of (S)-1-pyrroline-5-carboxylate. kcat is 85 sec(-1) for the NADPH-dependent reduction of (S)-1-pyrroline-5-carboxylate (PubMed:23024808). kcat is 218.8 sec(-1) for the oxidation of NADH

substrate: H+; (S)-1-Pyrroline-5-carboxylate; NADH


organism: Bacteria

proof_lines: bacterial chromosomal encoded isozyme type III

proof_lines: bacterial, R factor encoded isozyme type II


organism: Crithidia fasciculata


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature V115A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


organism: Lactobacillus leichmannii


organism: Leishmania braziliensis


organism: Leishmania major


organism: Clostridium formicaceticum

substrate_name: 5,10-Methylenetetrahydrofolate; NAD+

assay_conditions_summary: cofactor NAD+

substrate: 5,10-Methylenetetrahydrofolate; NAD+


substrate_name: NADP+; 5,10-Methylenetetrahydrofolate

column_label: Valid JBC PDF text, page 5 Pyridine Nucleotide paragraph: in the presence of saturating 5,10-methylene-THF, the Km of 5,10-methylene-THF dehydrogenase for NADP is 300 uM. Local text refs: supantha_download_20260707_2312_jbc_text.txt lines 393-395 and per-page extraction page 5 lines 22-24.

normalized_value_unit_evidence: 300 uM normalizes to 0.3 mM, matching the export Km 0.3 mM for the NADP+ / 5,10-methylenetetrahydrofolate reaction context.

raw_value_unit_evidence: The Pyridine Nucleotide paragraph reports that, in the presence of saturating 5,10-methylene-THF, the Km of 5,10-methylene-THF dehydrogenase for NADP is 300 uM.

table_label: Results prose, Pyridine Nucleotide paragraph

substrate: NADP+; 5,10-Methylenetetrahydrofolate


organism: Photobacterium phosphoreum


organism: Pisum sativum

substrate_name: 5,6,7,8-Tetrahydrofolate; NADP+

substrate: 5,6,7,8-Tetrahydrofolate; NADP+


enzyme_display_name: Ketimine reductase mu-crystallin

substrate_name: 3,4-dehydro-thiomorpholine-3-carboxylate (at pH 5.0 and 37 degrees Celsius)

assay_conditions_summary: pH 5; cofactor NADH

column_label: Table V (Apparent kinetic constants), row S-Aminoethylcysteine ketimine, column Km (mM), value 0.24; Table V note says NADH for AECK and pH 5.0; Materials and Methods says spectrophotometry at 340 nm and 37 C

raw_value_unit_evidence: Table V row S-Aminoethylcysteine ketimine, column Km (mM) = 0.24

row_label: S-Aminoethylcysteine ketimine

table_label: Table V

enzyme: Ketimine reductase mu-crystallin


assay_conditions_summary: pH 5

substrate: 3,4-dehydro-thiomorpholine-3-carboxylate (at pH 5.0 and 37 degrees Celsius)


organism: Arabidopsis thaliana

substrate_name: (S)-1-Pyrroline-5-carboxylate; NADH; H+

assay_conditions_summary: cofactor NADPH

substrate: (S)-1-Pyrroline-5-carboxylate; NADH; H+


substrate_name: Thioproline; NADP+

assay_conditions_summary: cofactor NADP+

substrate: Thioproline; NADP+


column_label: PMID 16667072 PDF text page 3; Kinetic Properties of PCR section; NADPH prose reports Km 0.12 mM and Vmax 0.19 umol min^-1 mg protein^-1.

normalized_value_unit_evidence: Km normalized_value=0.12 normalized_unit=mM | Vmax normalized_value=0.000003166667 normalized_unit=mol*s^(-1)*g^(-1)

raw_value_unit_evidence: Kinetic Properties of PCR prose: at pH 7.5 and 2 mM D,L-P4C, apparent Kms for NADPH and NADH were 0.12 mM and 0.19 mM, respectively; Vmax was greater with NADPH (0.19 umol min^-1 mg protein^-1) than with NADH (0.15 umol min^-1 mg protein^-1).

row_label: Chloroplast PCR NADPH kinetic prose

table_label: Kinetic Properties of PCR prose


organism: Pseudomonas aeruginosa


substrate_name: NADPH; Dihydrofolate; H+

assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

proof_lines:
recombinant enzyme
pH 7.0, 25°C

substrate: NADPH; Dihydrofolate; H+


organism: Plasmodium falciparum


organism: Toxoplasma gondii

substrate_name: H+; Dihydrofolate; NADPH

substrate: H+; Dihydrofolate; NADPH


proof_lines: pH and temperature not specified in the publication


proof_lines: pH 7.3, 27°C, Leishmania wild-type growth is inhibited with an EC50 of 1.1 microM, DHCH1 or formate-tetrahydrofolate ligase overexpressing (FTL) Leishmania transfectants show 4-5fold or 3fold resistance, respectively


enzyme_display_name: Bifunctional protein MdtA

organism: Methylorubrum extorquens (strain ATCC 14718 / DSM 1338 / JCM 2805 / NCIMB 9133 / AM1)

enzyme: Bifunctional protein MdtA


organism: Rattus norvegicus

substrate_name: tetrahydropteroylpentaglutamate/H4PteGlu5 (in presence of NAD(+))

proof_lines: Has similar catalytic efficiencies, at physiological concentrations, with either NAD(+) or NADP(+) as substrates for the dehydrogenation of (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate.


organism: Salmonella enterica subsp. enterica serovar Typhimurium


organism: Escherichia coli

substrate_name: dihydrofolate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I155A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 288.15 K; buffer pH 7; cofactor NADPH

column_label: Table 2; row I155A; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay

raw_value_unit_evidence: Table 2 cells: kcat=5.2 s^-1; Km=1.44 uM; kcat/Km=3.62 uM^-1 s^-1

substrate: dihydrofolate


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I155D to reconstruct the assayed variant sequence.

column_label: Table 2; row I155D; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay

raw_value_unit_evidence: Table 2 cells: kcat=7.55 s^-1; Km=2.2 uM; kcat/Km=3.43 uM^-1 s^-1


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I155E to reconstruct the assayed variant sequence.

column_label: Table 2; row I155E; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay

raw_value_unit_evidence: Table 2 cells: kcat=5.8 s^-1; Km=1.76 uM; kcat/Km=3.29 uM^-1 s^-1


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I155K to reconstruct the assayed variant sequence.

column_label: Table 2; row I155K; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I155L to reconstruct the assayed variant sequence.

column_label: Table 2; row I155L; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I155Q to reconstruct the assayed variant sequence.

column_label: Table 2; row I155Q; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I155R to reconstruct the assayed variant sequence.

column_label: Table 2; row I155R; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I155S to reconstruct the assayed variant sequence.

column_label: Table 2; row I155S; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I155T to reconstruct the assayed variant sequence.

column_label: Table 2; row I155T; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I155V to reconstruct the assayed variant sequence.

column_label: Table 2; row I155V; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay

raw_value_unit_evidence: Table 2 cells: kcat=4.8 s^-1; Km=1.5 uM; kcat/Km=3.19 uM^-1 s^-1


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I155W to reconstruct the assayed variant sequence.

column_label: Table 2; row I155W; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I155Y to reconstruct the assayed variant sequence.

column_label: Table 2; row I155Y; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay

raw_value_unit_evidence: Table 2 cells: kcat=6.03 s^-1; Km=1.51 uM; kcat/Km=4 uM^-1 s^-1


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N59C to reconstruct the assayed variant sequence.

column_label: Table 2; row N59C; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N59E to reconstruct the assayed variant sequence.

column_label: Table 2; row N59E; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N59G to reconstruct the assayed variant sequence.

column_label: Table 2; row N59G; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N59H to reconstruct the assayed variant sequence.

column_label: Table 2; row N59H; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay

raw_value_unit_evidence: Table 2 cells: kcat=1.45 s^-1; Km=1.1 uM; kcat/Km=1.31 uM^-1 s^-1


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N59I to reconstruct the assayed variant sequence.

column_label: Table 2; row N59I; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N59K to reconstruct the assayed variant sequence.

column_label: Table 2; row N59K; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay

normalized_value_unit_evidence: normalized: kcat=4.3 s^-1; Km=0.0136 mM; kcat/Km=320 s^-1 mM^-1

raw_value_unit_evidence: Table 2 cells: kcat=4.3 s^-1; Km=13.6 uM; kcat/Km=0.32 uM^-1 s^-1


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N59L to reconstruct the assayed variant sequence.

column_label: Table 2; row N59L; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay

raw_value_unit_evidence: Table 2 cells: kcat=3.45 s^-1; Km=1.82 uM; kcat/Km=1.9 uM^-1 s^-1


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N59M to reconstruct the assayed variant sequence.

column_label: Table 2; row N59M; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprotkb:P0ABQ4 and applied mutation signature W30Y to reconstruct the assayed variant sequence.

column_label: Table 2; row W30Y; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V40N to reconstruct the assayed variant sequence.

column_label: Table 2; row V40N; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V40R to reconstruct the assayed variant sequence.

column_label: Table 2; row V40R; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V40S to reconstruct the assayed variant sequence.

column_label: Table 2; row V40S; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay

raw_value_unit_evidence: Table 2 cells: kcat=5.5 s^-1; Km=2.21 uM; kcat/Km=2.49 uM^-1 s^-1


sequence_variant_note: Resolved canonical sequence from uniprotkb:P0ABQ4 and applied mutation signature W30A to reconstruct the assayed variant sequence.

column_label: Table 2; row W30A; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprotkb:P0ABQ4 and applied mutation signature W30E to reconstruct the assayed variant sequence.

column_label: Table 2; row W30E; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprotkb:P0ABQ4 and applied mutation signature W30H to reconstruct the assayed variant sequence.

column_label: Table 2; row W30H; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprotkb:P0ABQ4 and applied mutation signature W30M to reconstruct the assayed variant sequence.

column_label: Table 2; row W30M; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprotkb:P0ABQ4 and applied mutation signature W30N to reconstruct the assayed variant sequence.

column_label: Table 2; row W30N; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprotkb:P0ABQ4 and applied mutation signature W30R to reconstruct the assayed variant sequence.

column_label: Table 2; row W30R; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprotkb:P0ABQ4 and applied mutation signature W30S to reconstruct the assayed variant sequence.

column_label: Table 2; row W30S; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay

raw_value_unit_evidence: Table 2 cells: kcat=15 s^-1; Km=2.09 uM; kcat/Km=7.17 uM^-1 s^-1


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N59P to reconstruct the assayed variant sequence.

column_label: Table 2; row N59P; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N59Q to reconstruct the assayed variant sequence.

column_label: Table 2; row N59Q; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N59S to reconstruct the assayed variant sequence.

column_label: Table 2; row N59S; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N59T to reconstruct the assayed variant sequence.

column_label: Table 2; row N59T; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay

raw_value_unit_evidence: Table 2 cells: kcat=10.3 s^-1; Km=4.91 uM; kcat/Km=2.1 uM^-1 s^-1


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N59V to reconstruct the assayed variant sequence.

column_label: Table 2; row N59V; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N59W to reconstruct the assayed variant sequence.

column_label: Table 2; row N59W; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S148A to reconstruct the assayed variant sequence.

column_label: Table 2; row S148A; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay

raw_value_unit_evidence: Table 2 cells: kcat=4.8 s^-1; Km=0.5 uM; kcat/Km=9.61 uM^-1 s^-1


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S148E to reconstruct the assayed variant sequence.

column_label: Table 2; row S148E; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S148K to reconstruct the assayed variant sequence.

column_label: Table 2; row S148K; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S148N to reconstruct the assayed variant sequence.

column_label: Table 2; row S148N; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S148P to reconstruct the assayed variant sequence.

column_label: Table 2; row S148P; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S148R to reconstruct the assayed variant sequence.

column_label: Table 2; row S148R; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay

raw_value_unit_evidence: Table 2 cells: kcat=4.55 s^-1; Km=1.6 uM; kcat/Km=2.84 uM^-1 s^-1


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S148T to reconstruct the assayed variant sequence.

column_label: Table 2; row S148T; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S148V to reconstruct the assayed variant sequence.

column_label: Table 2; row S148V; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V40A to reconstruct the assayed variant sequence.

column_label: Table 2; row V40A; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V40F to reconstruct the assayed variant sequence.

column_label: Table 2; row V40F; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V40H to reconstruct the assayed variant sequence.

column_label: Table 2; row V40H; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V40I to reconstruct the assayed variant sequence.

column_label: Table 2; row V40I; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay

raw_value_unit_evidence: Table 2 cells: kcat=3.8 s^-1; Km=1.8 uM; kcat/Km=2.11 uM^-1 s^-1


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V40L to reconstruct the assayed variant sequence.

column_label: Table 2; row V40L; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V40M to reconstruct the assayed variant sequence.

column_label: Table 2; row V40M; columns kcat, Km, kcat/Km; substrate dihydrofolate/DHF; assay condition as recorded for enzyme assay

raw_value_unit_evidence: Table 2 cells: kcat=3.7 s^-1; Km=2.23 uM; kcat/Km=1.66 uM^-1 s^-1


enzyme_display_name: D-arginine dehydrogenase

substrate_name: D-arginine

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

column_label: Table 1 'Table 1: Kinetic parameters of DadA with different D-amino acids'; row d-Arginine; kcat, Km, and kcat/Km cells.

normalized_value_unit_evidence: Table 1 row d-Arginine, normalized: kcat 1.27 s^-1; Km 5.37 mM; kcat/Km 0.236 s^-1 mM^-1.

row_label: d-Arginine

enzyme: D-arginine dehydrogenase

substrate: D-arginine


substrate_name: D-histidine

column_label: Table 1 'Table 1: Kinetic parameters of DadA with different D-amino acids'; row d-Histidine; kcat, Km, and kcat/Km cells.

normalized_value_unit_evidence: Table 1 row d-Histidine, normalized: kcat 0.84 s^-1; Km 0.81 mM; kcat/Km 1.04 s^-1 mM^-1.

row_label: d-Histidine

substrate: D-histidine


substrate_name: D-Alanine

column_label: Table 1 'Table 1: Kinetic parameters of DadA with different D-amino acids'; row d-Alanine; kcat, Km, and kcat/Km cells.

normalized_value_unit_evidence: Table 1 row d-Alanine, normalized: kcat 0.74 s^-1; Km 0.46 mM; kcat/Km 1.61 s^-1 mM^-1.

row_label: d-Alanine

substrate: D-Alanine


substrate_name: D-phenylalanine

column_label: Table 1 'Table 1: Kinetic parameters of DadA with different D-amino acids'; row d-Phenylalanine; kcat, Km, and kcat/Km cells.

normalized_value_unit_evidence: Table 1 row d-Phenylalanine, normalized: kcat 1.1 s^-1; Km 1.07 mM; kcat/Km 1.03 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row d-Phenylalanine: kcat 1.10 ± 0.06 s^-1; Km 1.07 ± 0.22 mM; kcat/Km 1.03 x 10^3 M^-1 s^-1.

row_label: d-Phenylalanine

substrate: D-phenylalanine


substrate_name: D-proline

column_label: Table 1 'Table 1: Kinetic parameters of DadA with different D-amino acids'; row d-Proline; kcat, Km, and kcat/Km cells.

normalized_value_unit_evidence: Table 1 row d-Proline, normalized: kcat 0.97 s^-1; Km 1.82 mM; kcat/Km 0.533 s^-1 mM^-1.

row_label: d-Proline

substrate: D-proline


substrate_name: D-serine

column_label: Table 1 'Table 1: Kinetic parameters of DadA with different D-amino acids'; row d-Serine; kcat, Km, and kcat/Km cells.

normalized_value_unit_evidence: Table 1 row d-Serine, normalized: kcat 0.8 s^-1; Km 1.65 mM; kcat/Km 0.485 s^-1 mM^-1.

row_label: d-Serine

substrate: D-serine


substrate_name: D-valine

column_label: Table 1 'Table 1: Kinetic parameters of DadA with different D-amino acids'; row d-Valine; kcat, Km, and kcat/Km cells.

normalized_value_unit_evidence: Table 1 row d-Valine, normalized: kcat 0.78 s^-1; Km 3.01 mM; kcat/Km 0.259 s^-1 mM^-1.

row_label: d-Valine

substrate: D-valine


substrate_name: D-Threonine

column_label: Table 1 'Table 1: Kinetic parameters of DadA with different D-amino acids'; row d-Threonine; kcat, Km, and kcat/Km cells.

normalized_value_unit_evidence: Table 1 row d-Threonine, normalized: kcat 0.68 s^-1; Km 2.47 mM; kcat/Km 0.275 s^-1 mM^-1.

row_label: d-Threonine

substrate: D-Threonine


substrate_name: D-Tyrosine

column_label: Table 1 'Table 1: Kinetic parameters of DadA with different D-amino acids'; row d-Tyrosine; kcat, Km, and kcat/Km cells.

normalized_value_unit_evidence: Table 1 row d-Tyrosine, normalized: kcat 1.1 s^-1; Km 1.78 mM; kcat/Km 0.618 s^-1 mM^-1.

row_label: d-Tyrosine

substrate: D-Tyrosine


organism: Homo sapiens

sequence_variant_note: Resolved canonical sequence from uniprotkb_reviewed:P00374 and applied mutation signature Q35K/N64F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

column_label: Official PMC Table 2 Q35K/N64F row under Km DHFA, kcat, and kcat/Km DHFA columns; Table 2 footnote * preserved.

normalized_value_unit_evidence: Km 0.00049 mM; kcat 43 s^-1; explicit kcat/Km 88000 s^-1 mM^-1; * denotes a statistically significant comparison with native human DHFR.

raw_value_unit_evidence: Km DHFA 0.49 +/- 0.05 microM (n=4), footnote *; kcat 43 +/- 2.5 s^-1 (n=4); printed DHFA kcat/Km 88 s^-1 microM^-1.

row_label: Q35K/N64F; Km DHFA, kcat, and kcat/Km DHFA


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q35S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q35S/N64S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


substrate_name: NADPH

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

substrate: NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N64S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +12, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q35K/N64F with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q35S with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.


enzyme_display_name: pyrroline-5-carboxylate reductase

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q96C36 and applied mutation signature R119C to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADPH

column_label: PMID 33771508 Table 1; row R119C with varied substrate DL-P5C and fixed substrate NADPH; columns KMapp, kcatapp, and kcatapp/KMapp.

row_label: R119C; varied substrate DL-P5C; fixed substrate NADPH

table_label: Table 1. Steady-state kinetic parameters for PYCR2


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q96C36 and applied mutation signature R251C to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADH

column_label: PMID 33771508 Table 1; row R251C with varied substrate DL-P5C and fixed substrate NADH; columns KMapp, kcatapp, and kcatapp/KMapp.

row_label: R251C; varied substrate DL-P5C; fixed substrate NADH


column_label: PMID 33771508 Table 1; row Wild-type with varied substrate DL-P5C and fixed substrate NADH; columns KMapp, kcatapp, and kcatapp/KMapp.

raw_value_unit_evidence: Table 1 row Wild-type / DL-P5C / NADH: KMapp 1509 +/- 69 uM; kcatapp 61.3 +/- 1.4 s^-1; kcatapp/KMapp (41 +/- 2) x 10^3 M^-1 s^-1.

row_label: Wild-type; varied substrate DL-P5C; fixed substrate NADH


substrate_name: NADH

column_label: PMID 33771508 Table 1; row R119C with varied substrate NADH and fixed substrate DL-P5C; columns KMapp, kcatapp, and kcatapp/KMapp.

row_label: R119C; varied substrate NADH; fixed substrate DL-P5C

substrate: NADH


column_label: PMID 33771508 Table 1; row R251C with varied substrate NADH and fixed substrate DL-P5C; columns KMapp, kcatapp, and kcatapp/KMapp.

row_label: R251C; varied substrate NADH; fixed substrate DL-P5C


column_label: PMID 33771508 Table 1; row Wild-type with varied substrate NADH and fixed substrate DL-P5C; columns KMapp, kcatapp, and kcatapp/KMapp.

raw_value_unit_evidence: Table 1 row Wild-type / NADH / DL-P5C: KMapp 298 +/- 73 uM; kcatapp 47.9 +/- 5.3 s^-1; kcatapp/KMapp (161 +/- 44) x 10^3 M^-1 s^-1.

row_label: Wild-type; varied substrate NADH; fixed substrate DL-P5C


column_label: PMID 33771508 Table 1; row R119C with varied substrate NADPH and fixed substrate DL-P5C; columns KMapp, kcatapp, and kcatapp/KMapp.

row_label: R119C; varied substrate NADPH; fixed substrate DL-P5C


column_label: PMID 33771508 Table 1; row R251C with varied substrate NADPH and fixed substrate DL-P5C; columns KMapp, kcatapp, and kcatapp/KMapp.

row_label: R251C; varied substrate NADPH; fixed substrate DL-P5C


column_label: PMID 33771508 Table 1; row Wild-type with varied substrate NADPH and fixed substrate DL-P5C; columns KMapp, kcatapp, and kcatapp/KMapp.

raw_value_unit_evidence: Table 1 row Wild-type / NADPH / DL-P5C: KMapp 216 +/- 17 uM; kcatapp 24.0 +/- 0.7 s^-1; kcatapp/KMapp (111 +/- 9) x 10^3 M^-1 s^-1.

row_label: Wild-type; varied substrate NADPH; fixed substrate DL-P5C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y69F with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 303.15 K; cofactor NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y69H with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 303.15 K; buffer MTA; cofactor NADPH

column_label: Table 1: Comparison of Steady State Kinetic Values for R67 DHFR Variants at pH 7.0; row Y69H R67 DHFR; columns kcat (s^-1), Km(DHF) (uM), Km(NADPH) (uM); substrate-specific evidence uses Km(NADPH) for NADPH.

raw_value_unit_evidence: Table 1 Y69H R67 DHFR row: kcat 0.014 s^-1; Km(DHF) 46 uM; Km(NADPH) 176 uM.

row_label: Y69H R67 DHFR


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I68L with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.

column_label: Table 1: Comparison of Steady State Kinetic Values for R67 DHFR Variants at pH 7.0; row I68L R67 DHFR; columns kcat (s^-1), Km(DHF) (uM), Km(NADPH) (uM); substrate-specific evidence uses Km(DHF) for dihydrofolate.

raw_value_unit_evidence: Table 1 I68L R67 DHFR row: kcat 0.32 s^-1; Km(DHF) 24 uM; Km(NADPH) 26 uM.

row_label: I68L R67 DHFR


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I68M with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.

column_label: Table 1: Comparison of Steady State Kinetic Values for R67 DHFR Variants at pH 7.0; row I68M R67 DHFR; columns kcat (s^-1), Km(DHF) (uM), Km(NADPH) (uM); substrate-specific evidence uses Km(DHF) for dihydrofolate.

raw_value_unit_evidence: Table 1 I68M R67 DHFR row: kcat 0.17 s^-1; Km(DHF) 25 uM; Km(NADPH) 21 uM.

row_label: I68M R67 DHFR


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q67C to reconstruct the assayed variant sequence.

column_label: Table 1: Comparison of Steady State Kinetic Values for R67 DHFR Variants at pH 7.0; row Q67C R67 DHFR; columns kcat (s^-1), Km(DHF) (uM), Km(NADPH) (uM); substrate-specific evidence uses Km(DHF) for dihydrofolate.

raw_value_unit_evidence: Table 1 Q67C R67 DHFR row: kcat 0.10 s^-1; Km(DHF) 55 uM; Km(NADPH) 26 uM.

row_label: Q67C R67 DHFR


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S65A with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.

column_label: Table 1: Comparison of Steady State Kinetic Values for R67 DHFR Variants at pH 7.0; row S65A R67 DHFR; columns kcat (s^-1), Km(DHF) (uM), Km(NADPH) (uM); substrate-specific evidence uses Km(DHF) for dihydrofolate.

raw_value_unit_evidence: Table 1 S65A R67 DHFR row: kcat 1.1 s^-1; Km(DHF) 4.0 uM; Km(NADPH) 2.9 uM.

row_label: S65A R67 DHFR


column_label: Table 1: Comparison of Steady State Kinetic Values for R67 DHFR Variants at pH 7.0; row Y69H R67 DHFR; columns kcat (s^-1), Km(DHF) (uM), Km(NADPH) (uM); substrate-specific evidence uses Km(DHF) for dihydrofolate.