substrate_name: D-Proline

column_label: Table II; row D-Pro; M213R DAAO kcat, Km, and kcat/Km columns.

normalized_value_unit_evidence: normalized values: kcat=26.917 s^-1; Km=1280 mM; kcat/Km=0.0217 s^-1 mM^-1.

raw_value_unit_evidence: Table II row D-Pro under M213R DAAO; columns: kcat=1615 min^-1; Km=1280 mM; kcat/Km=1.3 mM^-1 min^-1.

row_label: D-Pro M213R

substrate: D-Proline


enzyme_display_name: D-amino-acid oxidase

organism: Rhodosporidium toruloides

source_db: oed

verification_status: corrected

ki_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

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.

column_label: Table II; row D-Pro; wild-type DAAO kcat, Km, and kcat/Km columns.

normalized_value_unit_evidence: normalized values: kcat=77.333 s^-1; Km=21.5 mM; kcat/Km=3.6 s^-1 mM^-1.

raw_value_unit_evidence: Table II row D-Pro under wild-type DAAO; columns: kcat=4640 min^-1; Km=21.5 mM; kcat/Km=216 mM^-1 min^-1.

row_label: D-Pro wild-type

table_label: Table II

data_origin: experimental

enzyme: D-amino-acid oxidase

status: corrected

source: oed


substrate_name: N-Methyl-D-aspartic acid

verification_status: unverified

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M213R to reconstruct the assayed variant sequence.

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

mutation_type: substitution

substrate: N-Methyl-D-aspartic acid

status: unverified


substrate_name: D-Alanine

proof_lines: M213R D-alanine DAAO

substrate: D-Alanine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature M213R/Y238R to reconstruct the assayed variant sequence.

proof_lines: M213R/Y238R D-alanine DAAO


substrate_name: D-Asparagine

substrate: D-Asparagine


substrate_name: D-Aspartate

proof_lines: M213R D-aspartate DAAO

substrate: D-Aspartate


proof_lines: M213R/Y238R D-aspartate DAAO


proof_lines: D-aspartate M213R/Y238R DAAO


substrate_name: D-Glutamate

proof_lines: D-glutamate M213R/Y238R DAAO

substrate: D-Glutamate


proof_lines: D-glutamate DAAO


substrate_name: D-Glutamine

proof_lines: D-glutamine DAAO

substrate: D-Glutamine


organism: Sus scrofa

substrate_name: D-Serine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature G313A to reconstruct the assayed variant sequence.

proof_lines:
D-amino acid oxidase
G313A
D-serine

substrate: D-Serine


substrate_name: D-Valine

assay_conditions_summary: pH 8.3; 298.15 K; buffer 100 mM pyrophosphate; cofactor FAD

column_label: TABLE III. Steady-state kinetic parameters, substrate row D-Valine, wild type column of each printed group; column K_m (mM) = 0.67; column k_cat (s^-1) = 2.5; column k_cat/K_m (mM^-1 s^-1) = 3.7.

normalized_value_unit_evidence: Km: printed cell 0.67 mM; the printed column head is K_m (mM), so no unit conversion applies and the paper value is 0.67 mM. kcat: printed cell 2.5 s^-1; the printed column head is k_cat (s^-1), so no unit conversion applies and the paper value is 2.5 s^(-1). kcat/Km: printed cell 3.7 mM^-1 s^-1; the printed column head is k_cat/K_m (mM^-1 s^-1), which is the canonical efficiency unit, so no unit conversion applies and the printed cell is 3.7 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 2.5 / 0.67 = 3.7313432835820897 s^-1 mM^-1.

raw_value_unit_evidence: TABLE III. Steady-state kinetic parameters, substrate row D-Valine, wild type column of each printed group: Km = 0.67 mM; kcat = 2.5 s^-1; printed kcat/Km = 3.7 mM^-1 s^-1.

table_label: TABLE III: Steady-state kinetic parameters of wild-type DAO and the T317A mutant (J. Biochem. 131, 59-69, 2002); printed column groups K_m (mM), k_cat (s^-1) and k_cat/K_m (mM^-1 s^-1), each printing a Wild type and a T317 column

substrate: D-Valine


verification_status: verified

column_label: TABLE III. Steady-state kinetic parameters, substrate row D-Alanine, wild type column of each printed group; column K_m (mM) = 1.1; column k_cat (s^-1) = 8.5; column k_cat/K_m (mM^-1 s^-1) = 7.7.

normalized_value_unit_evidence: Km: printed cell 1.1 mM; the printed column head is K_m (mM), so no unit conversion applies and the paper value is 1.1 mM. kcat: printed cell 8.5 s^-1; the printed column head is k_cat (s^-1), so no unit conversion applies and the paper value is 8.5 s^(-1). kcat/Km: printed cell 7.7 mM^-1 s^-1; the printed column head is k_cat/K_m (mM^-1 s^-1), which is the canonical efficiency unit, so no unit conversion applies and the printed cell is 7.7 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 8.5 / 1.1 = 7.727272727272727 s^-1 mM^-1.

raw_value_unit_evidence: TABLE III. Steady-state kinetic parameters, substrate row D-Alanine, wild type column of each printed group: Km = 1.1 mM; kcat = 8.5 s^-1; printed kcat/Km = 7.7 mM^-1 s^-1.

status: verified


proof_lines:
D-amino acid oxidase
G313A
various D-amino acids


substrate_name: D-Arginine

substrate: D-Arginine


substrate_name: D-Isoleucine

substrate: D-Isoleucine


column_label: TABLE I. Kinetic parameters, substrate row D-Isoleucine, wild type column of each printed group; column K_m (mM) = 1.3; column k_cat (s^-1) = 4.8; column k_cat/K_m (mM^-1 s^-1) = 3.7.

normalized_value_unit_evidence: Km: printed cell 1.3 mM; the printed column head is K_m (mM), so no unit conversion applies and the paper value is 1.3 mM. kcat: printed cell 4.8 s^-1; the printed column head is k_cat (s^-1), so no unit conversion applies and the paper value is 4.8 s^(-1). kcat/Km: printed cell 3.7 mM^-1 s^-1; the printed column head is k_cat/K_m (mM^-1 s^-1), which is the canonical efficiency unit, so no unit conversion applies and the printed cell is 3.7 s^(-1)*mM^(-1). Quotient disclosure for this cell group: 4.8 / 1.3 = 3.692307692307692 s^-1 mM^-1.

raw_value_unit_evidence: TABLE I. Kinetic parameters, substrate row D-Isoleucine, wild type column of each printed group: Km = 1.3 mM; kcat = 4.8 s^-1; printed kcat/Km = 3.7 mM^-1 s^-1.

table_label: TABLE I: Kinetic parameters of G313A in comparison with the wild type DAO (J. Biochem. 131, 59-69, 2002); printed column groups K_m (mM), k_cat (s^-1) and k_cat/K_m (mM^-1 s^-1), each printing a Wild type and a G313A column


substrate_name: D-Methionine

substrate: D-Methionine


proof_lines:
D-amino acid oxidase
various D-amino acids
G313A


enzyme_display_name: L-amino-acid oxidase

organism: Calloselasma rhodostoma

substrate_name: L-ornithine

source_db: brenda

kcat_display: Not reported

kcat_over_km_display: Not reported

sequence_source: multiple

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

proof_lines: Purification and properties of the L-amino acid oxidase

source_databases_merged: brenda uniprot

enzyme: L-amino-acid oxidase

substrate: L-ornithine

source: brenda


enzyme_display_name: Amine oxidase [flavin-containing] A

organism: Rattus norvegicus

substrate_name: (R)-noradrenaline

source_db: uniprot

column_label: Km

normalized_value_unit_evidence: normalized: km=0.582 mM; Vmax is not kcat and is not used as kcat evidence

raw_value_unit_evidence: paper Table 3 cells: MAO-A Noradrenaline Km=582 uM; Vmax=1213 pmol/mg protein/min

row_label: MAO-A / Noradrenaline

table_label: Table 3

enzyme: Amine oxidase [flavin-containing] A

substrate: (R)-noradrenaline

source: uniprot


substrate_name: tyramine

substrate: tyramine


substrate_name: tryptamine

substrate: tryptamine


substrate_name: L-norleucine

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

substrate: L-norleucine


substrate_name: L-isoleucine

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

substrate: L-isoleucine


substrate_name: L-norvaline

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

substrate: L-norvaline


substrate_name: L-arginine

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

substrate: L-arginine


substrate_name: L-asparagine

substrate: L-asparagine


substrate_name: L-histidine

substrate: L-histidine


substrate_name: L-aminobutyric acid

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

substrate: L-aminobutyric acid


substrate_name: L-glutamine

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

substrate: L-glutamine


substrate_name: L-lysine

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

substrate: L-lysine


substrate_name: L-alanine

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

substrate: L-alanine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I230A/R283G to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature I230C/R283G could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature I230F/R283G could not be applied safely because the resolved sequence does not match the expected reference residue(s).


enzyme_display_name: L-amino-acid oxidase L2

organism: Daboia russelii

substrate_name: L-Trp

sequence: ADDKNPLEECFCEDDDYCEG

wild_type_sequence: ADDKNPLEECFCEDDDYCEG

column_label: Table 2 row L-Trp; Km (M) column L2

raw_value_unit_evidence: Table 2 row L-Trp, Km (M) column L2 reports 235.1 x 10^-6 M.

row_label: L-Trp; L-amino-acid oxidase L2

table_label: Table 2. Substrate specificity of L1 and L2

enzyme: L-amino-acid oxidase L2

substrate: L-Trp


substrate_name: L-Tyr

column_label: Table 2 row L-Tyr; Km (M) column L2

raw_value_unit_evidence: Table 2 row L-Tyr, Km (M) column L2 reports 538.2 x 10^-6 M.

row_label: L-Tyr; L-amino-acid oxidase L2

substrate: L-Tyr


enzyme_display_name: L-amino-acid oxidase L1

substrate_name: L-Met

sequence: ADDINPKEECFFEDDYYEFE

wild_type_sequence: ADDINPKEECFFEDDYYEFE

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

column_label: Table 2 row L-Met; Km (M) column L1

raw_value_unit_evidence: Table 2 row L-Met, Km (M) column L1 reports 297.3 x 10^-6 M.

row_label: L-Met; L-amino-acid oxidase L1

enzyme: L-amino-acid oxidase L1

substrate: L-Met


substrate_name: L-Ile

column_label: Table 2 row L-Ile; Km (M) column L1

raw_value_unit_evidence: Table 2 row L-Ile, Km (M) column L1 reports 1.44 x 10^-3 M.

row_label: L-Ile; L-amino-acid oxidase L1

substrate: L-Ile


substrate_name: L-Leu

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

column_label: Table 2 row L-Leu; Km (M) column L1

raw_value_unit_evidence: Table 2 row L-Leu, Km (M) column L1 reports 750.8 x 10^-6 M.

row_label: L-Leu; L-amino-acid oxidase L1

substrate: L-Leu


substrate_name: L-Phe

column_label: Table 2 row L-Phe; Km (M) column L1

raw_value_unit_evidence: Table 2 row L-Phe, Km (M) column L1 reports 66.5 x 10^-6 M.

row_label: L-Phe; L-amino-acid oxidase L1

substrate: L-Phe


column_label: Table 2 row L-Trp; Km (M) column L1

raw_value_unit_evidence: Table 2 row L-Trp, Km (M) column L1 reports 210.9 x 10^-6 M.

row_label: L-Trp; L-amino-acid oxidase L1


column_label: Table 2 row L-Tyr; Km (M) column L1

raw_value_unit_evidence: Table 2 row L-Tyr, Km (M) column L1 reports 52.0 x 10^-6 M.

row_label: L-Tyr; L-amino-acid oxidase L1


column_label: Table 2 row L-Ile; Km (M) column L2

raw_value_unit_evidence: Table 2 row L-Ile, Km (M) column L2 reports 1.89 x 10^-3 M.

row_label: L-Ile; L-amino-acid oxidase L2


column_label: Table 2 row L-Leu; Km (M) column L2

raw_value_unit_evidence: Table 2 row L-Leu, Km (M) column L2 reports 599.7 x 10^-6 M.

row_label: L-Leu; L-amino-acid oxidase L2


column_label: Table 2 row L-Met; Km (M) column L2

raw_value_unit_evidence: Table 2 row L-Met, Km (M) column L2 reports 222.8 x 10^-6 M.

row_label: L-Met; L-amino-acid oxidase L2


column_label: Table 2 row L-Phe; Km (M) column L2

raw_value_unit_evidence: Table 2 row L-Phe, Km (M) column L2 reports 49.3 x 10^-6 M.

row_label: L-Phe; L-amino-acid oxidase L2


substrate_name: L-Ala (at pH 7.5 and 25 degrees Celsius)

proof_lines:
L-amino-acid oxidase
DrLAO
hydrophobic l-amino acids


enzyme_display_name: UniProt P21396

substrate_name: Phenylethylamine

source_db: skid

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

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

source_databases_merged: skid uniprot

enzyme: UniProt P21396

substrate: Phenylethylamine

source: skid


substrate_name: serotonin

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

substrate: serotonin


enzyme_display_name: Amine oxidase [flavin-containing] B

substrate_name: (R)-adrenaline

normalized_value_unit_evidence: normalized: km=0.84 mM; Vmax is not kcat and is not used as kcat evidence

raw_value_unit_evidence: paper Table 3 cells: MAO-B Adrenaline Km=840 uM; Vmax=531 pmol/mg protein/min

row_label: MAO-B / Adrenaline

enzyme: Amine oxidase [flavin-containing] B

substrate: (R)-adrenaline


substrate_name: dopamine

normalized_value_unit_evidence: normalized: km=0.29 mM; Vmax is not kcat and is not used as kcat evidence

raw_value_unit_evidence: paper Table 3 cells: MAO-B Dopamine Km=290 uM; Vmax=396 pmol/mg protein/min

row_label: MAO-B / Dopamine

substrate: dopamine


normalized_value_unit_evidence: normalized: km=0.533 mM; Vmax is not kcat and is not used as kcat evidence

raw_value_unit_evidence: paper Table 3 cells: MAO-B 5-hydroxytryptamine Km=533 uM; Vmax=125 pmol/mg protein/min

row_label: MAO-B / 5-hydroxytryptamine


substrate_name: (R)-noradrenaline

normalized_value_unit_evidence: normalized: km=1.954 mM; Vmax is not kcat and is not used as kcat evidence

raw_value_unit_evidence: paper Table 3 cells: MAO-B Noradrenaline Km=1954 uM; Vmax=383 pmol/mg protein/min

row_label: MAO-B / Noradrenaline

substrate: (R)-noradrenaline


normalized_value_unit_evidence: normalized: km=0.005 mM; Vmax is not kcat and is not used as kcat evidence

raw_value_unit_evidence: paper Table 3 cells: MAO-B 2-phenethylamine Km=5 uM; Vmax=489 pmol/mg protein/min

row_label: MAO-B / 2-phenethylamine


substrate_name: tyramine

normalized_value_unit_evidence: normalized: km=0.328 mM; Vmax is not kcat and is not used as kcat evidence

raw_value_unit_evidence: paper Table 3 cells: MAO-B Tyramine Km=328 uM; Vmax=687 pmol/mg protein/min

row_label: MAO-B / Tyramine

substrate: tyramine


normalized_value_unit_evidence: normalized: km=0.61 mM; Vmax is not kcat and is not used as kcat evidence

raw_value_unit_evidence: paper Table 3 cells: MAO-A Adrenaline Km=610 uM; Vmax=558 pmol/mg protein/min

row_label: MAO-A / Adrenaline


normalized_value_unit_evidence: normalized: km=0.15 mM; Vmax is not kcat and is not used as kcat evidence

raw_value_unit_evidence: paper Table 3 cells: MAO-A Dopamine Km=150 uM; Vmax=889 pmol/mg protein/min

row_label: MAO-A / Dopamine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00371 and applied mutation signature I230A/R283G to reconstruct the assayed variant sequence.

column_label: Table 1; row 2a; variant column I230A/R283G; metric rows Km, kcat, and kcat/Km; raw Km 5.23 +/- 0.65 mM; raw kcat 3.30 +/- 0.49 s^-1; explicit kcat/Km 0.629 s^-1 mM^-1.

table_label: PMID 30333894, Table 1: Kinetic parameter of wild-type and variants pkDAO


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00371 and applied mutation signature I230C/R283G to reconstruct the assayed variant sequence.

column_label: Table 1; row 2a; variant column I230C/R283G; metric rows Km, kcat, and kcat/Km; raw Km 2.40 +/- 0.30 mM; raw kcat 3.42 +/- 0.30 s^-1; explicit kcat/Km 1.45 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00371 and applied mutation signature I230F/R283G to reconstruct the assayed variant sequence.

column_label: Table 1; row 2a; variant column I230F/R283G; metric rows Km, kcat, and kcat/Km; raw Km 2.63 +/- 0.43 mM; raw kcat 0.366 +/- 0.036 s^-1; explicit kcat/Km 0.141 s^-1 mM^-1.


column_label: Table 1; row (R)-1a; variant column I230A/R283G; metric rows Km, kcat, and kcat/Km; raw Km 7.28 +/- 0.90 mM; raw kcat 0.349 +/- 0.013 s^-1; explicit kcat/Km 0.0482 s^-1 mM^-1.


column_label: Table 1; row (R)-1a; variant column I230C/R283G; metric rows Km, kcat, and kcat/Km; raw Km 6.90 +/- 1.11 mM; raw kcat 0.111 +/- 0.014 s^-1; explicit kcat/Km 0.0161 s^-1 mM^-1.


column_label: Table 1; row (R)-1a; variant column I230F/R283G; metric rows Km, kcat, and kcat/Km; raw Km 6.25 +/- 0.89 mM; raw kcat 0.0474 +/- 0.0059 s^-1; explicit kcat/Km 0.00777 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00371 and applied mutation signature R283G to reconstruct the assayed variant sequence.

column_label: Table 1; row (R)-1a; variant column R283G; metric rows Km, kcat, and kcat/Km; raw Km 6.98 +/- 0.67 mM; raw kcat 1.46 +/- 0.08 s^-1; explicit kcat/Km 0.211 s^-1 mM^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P00371 and applied mutation signature Y228L/R283G to reconstruct the assayed variant sequence.

column_label: Table 1; substrate block (R)-1a; variant column Y228L/R283G; metric rows Km, kcat, and kcat/Km.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y228L/R283G to reconstruct the assayed variant sequence.


substrate_name: D-phenylalanine

substrate: D-phenylalanine


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y228L with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


substrate_name: L-Arginine

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

substrate: L-Arginine


substrate_name: L-Tyr (at pH 7.5 and 25 degrees Celsius)

column_label: Table 1 row L-Tyr column Km (uM) has cell 81.

raw_value_unit_evidence: Km raw_value=81 raw_unit=uM

row_label: L-Tyr

table_label: Table 1. Kinetic specificity and Km values of DrLAO toward amino acid substrates and their reported plasma levels in three mammals


substrate_name: L-Phe (at pH 7.5 and 25 degrees Celsius)

column_label: Table 1 row L-Phe column Km (uM) has cell 142.

raw_value_unit_evidence: Km raw_value=142 raw_unit=uM

row_label: L-Phe


substrate_name: L-Met (at pH 7.5 and 25 degrees Celsius)

column_label: Table 1 row L-Met column Km (uM) has cell 373.

raw_value_unit_evidence: Km raw_value=373 raw_unit=uM

row_label: L-Met


substrate_name: L-Trp (at pH 7.5 and 25 degrees Celsius)

column_label: Table 1 row L-Trp column Km (uM) has cell 318.

raw_value_unit_evidence: Km raw_value=318 raw_unit=uM

row_label: L-Trp


substrate_name: L-Leu (at pH 7.5 and 25 degrees Celsius)

column_label: Table 1 row L-Leu column Km (uM) has cell 490.

raw_value_unit_evidence: Km raw_value=490 raw_unit=uM

row_label: L-Leu


substrate_name: L-Ile (at pH 7.5 and 25 degrees Celsius)


substrate_name: L-Arg (at pH 7.5 and 25 degrees Celsius)


substrate_name: L-Val (at pH 7.5 and 25 degrees Celsius)

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


substrate_name: L-Lys (at pH 7.5 and 25 degrees Celsius)


enzyme_display_name: UniProt P21397

organism: Homo sapiens

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=30°C, pH=7.2
Raw SKiD Env: Temp=11°C, pH=-----

enzyme: UniProt P21397


substrate_name: Phenylethylamine

proof_lines:
Raw SKiD Env: Temp=30°C, pH=7.2
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=11°C, pH=-----


km_display: Not reported


column_label: Km

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

table_label: Table 2


enzyme_display_name: UniProt P27338

substrate_name: serotonin

column_label: Table 2. Kinetic parameters of the two forms of MAO; row 5-Hydroxytryptamine; human cerebral cortex MAO-B; Km column 1093 uM normalized to 1.093 mM; Vmax column 7 pmol mg protein^-1 min^-1

raw_value_unit_evidence: Km 1093 uM; Vmax 7 pmol mg protein^-1 min^-1

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

enzyme: UniProt P27338


substrate_name: (R)-adrenaline

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


substrate_name: dopamine

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


substrate_name: (R)-noradrenaline

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


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


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


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


enzyme_display_name: L-amino-acid oxidase BmooLAAO-I

organism: Bothrops moojeni

substrate_name: L-Phe

assay_conditions_summary: pH 7; buffer pH 7

column_label: Table 2. Kinetic parameters for BmooLAAO-I; row Phe; column Km (mM); raw cell 0.2 ± 0.0; normalized Km 0.2 mM

normalized_value_unit_evidence: Km=0.2 mM (explicit table value)

row_label: BmooLAAO-I / Phe (L-Phe)

enzyme: L-amino-acid oxidase BmooLAAO-I


substrate_name: L-Leu

column_label: Table 2. Kinetic parameters for BmooLAAO-I; row Leu; column Km (mM); raw cell 0.2 ± 0.0; normalized Km 0.2 mM

row_label: BmooLAAO-I / Leu (L-Leu)


substrate_name: L-Met

column_label: Table 2. Kinetic parameters for BmooLAAO-I; row Met; column Km (mM); raw cell 0.3 ± 0.0; normalized Km 0.3 mM

normalized_value_unit_evidence: Km=0.3 mM (explicit table value)

row_label: BmooLAAO-I / Met (L-Met)


substrate_name: L-Tyr

column_label: Table 2. Kinetic parameters for BmooLAAO-I; row Tyr; column Km (mM); raw cell 1.1 ± 0.1; normalized Km 1.1 mM

normalized_value_unit_evidence: Km=1.1 mM (explicit table value)

row_label: BmooLAAO-I / Tyr (L-Tyr)


substrate_name: L-Ile

column_label: Table 2. Kinetic parameters for BmooLAAO-I; row Ile; column Km (mM); raw cell 1.4 ± 0.2; normalized Km 1.4 mM

normalized_value_unit_evidence: Km=1.4 mM (explicit table value)

row_label: BmooLAAO-I / Ile (L-Ile)


substrate_name: L-His

column_label: Table 2. Kinetic parameters for BmooLAAO-I; row His; column Km (mM); raw cell 7.4 ± 0.7; normalized Km 7.4 mM

normalized_value_unit_evidence: Km=7.4 mM (explicit table value)

row_label: BmooLAAO-I / His (L-His)

substrate: L-His


substrate_name: L-Gln

column_label: Table 2. Kinetic parameters for BmooLAAO-I; row Gln; column Km (mM); raw cell 6.1 ± 0.5; normalized Km 6.1 mM

normalized_value_unit_evidence: Km=6.1 mM (explicit table value)

raw_value_unit_evidence: BmooLAAO-I / Gln (L-Gln): Km=6.1 ± 0.5 mM; kcat=1723 ± 95 s^-1; kcat/Km=285 ± 8 mM^-1 s^-1

row_label: BmooLAAO-I / Gln (L-Gln)

substrate: L-Gln


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


enzyme_display_name: L-amino-acid oxidase BjussuLAAO-II

organism: Bothrops jararacussu

column_label: Table 1. Kinetic parameters for BjussuLAAO-II; row Phe; column Km (mM); raw cell 0.1 ± 0.0; normalized Km 0.1 mM

normalized_value_unit_evidence: Km=0.1 mM (explicit table value)

row_label: BjussuLAAO-II / Phe (L-Phe)

enzyme: L-amino-acid oxidase BjussuLAAO-II


column_label: Table 1. Kinetic parameters for BjussuLAAO-II; row Leu; column Km (mM); raw cell 0.3 ± 0.0; normalized Km 0.3 mM

row_label: BjussuLAAO-II / Leu (L-Leu)


column_label: Table 1. Kinetic parameters for BjussuLAAO-II; row Met; column Km (mM); raw cell 0.6 ± 0.1; normalized Km 0.6 mM

normalized_value_unit_evidence: Km=0.6 mM (explicit table value)

row_label: BjussuLAAO-II / Met (L-Met)


column_label: Table 1. Kinetic parameters for BjussuLAAO-II; row Tyr; column Km (mM); raw cell 1.1 ± 0.1; normalized Km 1.1 mM

row_label: BjussuLAAO-II / Tyr (L-Tyr)


column_label: Table 1. Kinetic parameters for BjussuLAAO-II; row Ile; column Km (mM); raw cell 2.0 ± 0.1; normalized Km 2 mM

normalized_value_unit_evidence: Km=2 mM (explicit table value)

raw_value_unit_evidence: BjussuLAAO-II / Ile (L-Ile): Km=2.0 ± 0.1 mM; kcat=2472 ± 39 s^-1; kcat/Km=1222 ± 30 mM^-1 s^-1

row_label: BjussuLAAO-II / Ile (L-Ile)


column_label: Table 1. Kinetic parameters for BjussuLAAO-II; row His; column Km (mM); raw cell 14.1 ± 1.9; normalized Km 14.1 mM

normalized_value_unit_evidence: Km=14.1 mM (explicit table value)

raw_value_unit_evidence: BjussuLAAO-II / His (L-His): Km=14.1 ± 1.9 mM; kcat=4935 ± 492 s^-1; kcat/Km=352 ± 14 mM^-1 s^-1

row_label: BjussuLAAO-II / His (L-His)


column_label: Table 1. Kinetic parameters for BjussuLAAO-II; row Gln; column Km (mM); raw cell 3.2 ± 0.3; normalized Km 3.2 mM

normalized_value_unit_evidence: Km=3.2 mM (explicit table value)

raw_value_unit_evidence: BjussuLAAO-II / Gln (L-Gln): Km=3.2 ± 0.3 mM; kcat=614 ± 10 s^-1; kcat/Km=192 ± 15 mM^-1 s^-1

row_label: BjussuLAAO-II / Gln (L-Gln)


organism: Pseudomonas sp.

substrate_name: L-lysine

sequence_variant_note: Resolved canonical sequence from uniprotkb:W6JQJ6 and applied mutation signature D238A to reconstruct the assayed variant sequence.

column_label: PMID 29511608 Table 2; row D238A / L-lysine; oxidase columns kcat, Km, kcat/Km; PMC article HTML lines 1799-1809.

normalized_value_unit_evidence: Oxidase kcat 0.50 s^-1; Oxidase Km 0.61 mM; Oxidase kcat/Km 0.82 s^-1 mM^-1

raw_value_unit_evidence: Oxidase kcat 0.50 ± 0.03 s^-1; Oxidase Km 0.61 ± 0.05 mM; Oxidase kcat/Km 0.82 ± 0.09 s^-1 mM^-1

row_label: D238A / L-lysine / Oxidase

table_label: PMID 29511608 Table 2. Kinetic parameters of wild-type and mutant enzymes of l-AAO/MOG

substrate: L-lysine


sequence_variant_note: Resolved canonical sequence from uniprotkb:W6JQJ6 and applied mutation signature D238E to reconstruct the assayed variant sequence.

column_label: PMID 29511608 Table 2; row D238E / L-lysine; oxidase columns kcat, Km, kcat/Km; PMC article HTML lines 1833-1843.

normalized_value_unit_evidence: Oxidase kcat 2.3 s^-1; Oxidase Km 0.018 mM; Oxidase kcat/Km 130 s^-1 mM^-1

raw_value_unit_evidence: Oxidase kcat 2.3 ± 0.3 s^-1; Oxidase Km 0.018 ± 0.006 mM; Oxidase kcat/Km 130 ± 10 s^-1 mM^-1

row_label: D238E / L-lysine / Oxidase


sequence_variant_note: Resolved canonical sequence from uniprotkb:W6JQJ6 and applied mutation signature D238F to reconstruct the assayed variant sequence.

column_label: PMID 29511608 Table 2; row D238F / L-lysine; oxidase columns kcat, Km, kcat/Km; PMC article HTML lines 1856-1866.

normalized_value_unit_evidence: Oxidase kcat 0.17 s^-1; Oxidase Km 0.049 mM; Oxidase kcat/Km 3.5 s^-1 mM^-1

raw_value_unit_evidence: Oxidase kcat 0.17 ± 0.01 s^-1; Oxidase Km 0.049 ± 0.009 mM; Oxidase kcat/Km 3.5 ± 0.2 s^-1 mM^-1

row_label: D238F / L-lysine / Oxidase


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

column_label: PMID 29511608 Table 2; row WT / L-lysine; oxidase columns kcat, Km, kcat/Km; PMC article HTML lines 1766-1775.

normalized_value_unit_evidence: Oxidase kcat 0.80 s^-1; Oxidase Km 0.027 mM; Oxidase kcat/Km 30 s^-1 mM^-1

raw_value_unit_evidence: Oxidase kcat 0.80 ± 0.09 s^-1; Oxidase Km 0.027 ± 0.003 mM; Oxidase kcat/Km 30 ± 1 s^-1 mM^-1

row_label: WT / L-lysine / Oxidase


substrate_name: L-Ornithine

column_label: PMID 29511608 Table 2; row D238A / L-Ornithine; oxidase columns kcat, Km, kcat/Km; PMC article HTML lines 1811-1820.

normalized_value_unit_evidence: Oxidase kcat 0.37 s^-1; Oxidase Km 0.45 mM; Oxidase kcat/Km 0.82 s^-1 mM^-1

raw_value_unit_evidence: Oxidase kcat 0.37 ± 0.05 s^-1; Oxidase Km 0.45 ± 0.02 mM; Oxidase kcat/Km 0.82 ± 0.10 s^-1 mM^-1

row_label: D238A / L-Ornithine / Oxidase

substrate: L-Ornithine


column_label: PMID 29511608 Table 2; row D238E / L-Ornithine; oxidase columns kcat, Km, kcat/Km; PMC article HTML lines 1845-1854.

normalized_value_unit_evidence: Oxidase kcat 0.58 s^-1; Oxidase Km 0.041 mM; Oxidase kcat/Km 14 s^-1 mM^-1

raw_value_unit_evidence: Oxidase kcat 0.58 ± 0.03 s^-1; Oxidase Km 0.041 ± 0.004 mM; Oxidase kcat/Km 14 ± 0.3 s^-1 mM^-1

row_label: D238E / L-Ornithine / Oxidase


column_label: PMID 29511608 Table 2; row WT / L-Ornithine; oxidase columns kcat, Km, kcat/Km; PMC article HTML lines 1777-1786.

normalized_value_unit_evidence: Oxidase kcat 1.5 s^-1; Oxidase Km 0.022 mM; Oxidase kcat/Km 68 s^-1 mM^-1

raw_value_unit_evidence: Oxidase kcat 1.5 ± 0.2 s^-1; Oxidase Km 0.022 ± 0.004 mM; Oxidase kcat/Km 68 ± 1.8 s^-1 mM^-1

row_label: WT / L-Ornithine / Oxidase


substrate_name: L-Arginine

column_label: PMID 29511608 Table 2; row D238A / L-Arginine; oxidase columns kcat, Km, kcat/Km; PMC article HTML lines 1822-1831.

normalized_value_unit_evidence: Oxidase kcat 0.10 s^-1; Oxidase Km 0.41 mM; Oxidase kcat/Km 0.24 s^-1 mM^-1

raw_value_unit_evidence: Oxidase kcat 0.10 ± 0.02 s^-1; Oxidase Km 0.41 ± 0.01 mM; Oxidase kcat/Km 0.24 ± 0.06 s^-1 mM^-1

row_label: D238A / L-Arginine / Oxidase


column_label: PMID 29511608 Table 2; row D238F / L-Arginine; oxidase columns kcat, Km, kcat/Km; PMC article HTML lines 1868-1877.

normalized_value_unit_evidence: Oxidase kcat 0.10 s^-1; Oxidase Km 0.080 mM; Oxidase kcat/Km 1.3 s^-1 mM^-1

raw_value_unit_evidence: Oxidase kcat 0.10 ± 0.01 s^-1; Oxidase Km 0.080 ± 0.018 mM; Oxidase kcat/Km 1.3 ± 0.1 s^-1 mM^-1

row_label: D238F / L-Arginine / Oxidase


column_label: PMID 29511608 Table 2; row WT / L-Arginine; oxidase columns kcat, Km, kcat/Km; PMC article HTML lines 1788-1797.

normalized_value_unit_evidence: Oxidase kcat 0.41 s^-1; Oxidase Km 0.048 mM; Oxidase kcat/Km 8.5 s^-1 mM^-1

raw_value_unit_evidence: Oxidase kcat 0.41 ± 0.02 s^-1; Oxidase Km 0.048 ± 0.001 mM; Oxidase kcat/Km 8.5 ± 0.65 s^-1 mM^-1

row_label: WT / L-Arginine / Oxidase


substrate_name: D-Alanine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D224G with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.

proof_lines:
porcine kidney D-amino acid oxidase
mutant family
D-alanine

substrate: D-Alanine


substrate_name: D-Arginine

proof_lines:
porcine kidney D-amino acid oxidase
mutant family
D-arginine

substrate: D-Arginine


substrate_name: D-Lysine

substrate: D-Lysine


assay_conditions_summary: pH 8.3; 298.15 K; buffer a Galvani-type oxygen electrode in 50 mM sodium pyrophosphate; cofactor FAD

column_label: Table 2 (apparent kcat in min-1 and Km in mM for the wild type and the five lid mutants of pig DAO), substrate row 'D-Lys'; column head 'Wild type', sub-column 'Kcat app' = 48; column head 'Wild type', sub-column 'Km app' = 10. The five mutant columns of the same substrate row carry their own construct cells (220D224G 200 and 14, 221D224G 300 and 20, 222D224G 300 and 20, 223D224G 180 and 20, 224D 140 and 18) and belong to the mutant catalog rows, not to this wild-type one. Table 2 carries no catalytic-efficiency column at all.

normalized_value_unit_evidence: kcat: printed Table 2 cell 48 min-1; 48 / 60 = 0.8 s^-1, and the exported value is 0.8 s^(-1). Km: printed Table 2 cell 10 mM; the cell is already in mM, so no unit conversion applies, and the exported value is 10.0 mM. kcat/Km: Table 2 prints no efficiency cell, so the exported ratio is typed as the quotient of the two printed cells of this same Table 2 tuple, 0.8 / 10.0 = 0.08 s^-1 mM^-1, which is the exported value 0.08 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, substrate row 'D-Lys', 'Wild type' column: printed Kcat app cell 48 with printed unit min-1, and printed Km app cell 10 with printed unit mM. Table 2 prints no catalytic-efficiency cell.

row_label: Table 2, substrate row D-Lys, Wild type column (the first Kcat app / Km app pair of that row)

table_label: Table 2: Comparison of the apparent kcat (in min-1) and Km (in mM) values of the wild type and mutant pig DAOs (J. Biochem. 139, 873-879 (2006))


substrate_name: D-Methionine

substrate: D-Methionine


substrate_name: D-Phenylalanine

substrate: D-Phenylalanine


substrate_name: D-Proline

substrate: D-Proline


substrate_name: D-Serine

substrate: D-Serine


substrate_name: D-Valine

substrate: D-Valine


organism: Ophiophagus hannah

column_label: Table 2 row L-His, column Km (mM) = 3.0.

normalized_value_unit_evidence: Km 3.0 mM.

raw_value_unit_evidence: Km 3.0 mM.

row_label: L-His


column_label: Table 2 row L-Ileu, column Km (mM) = 1.3.

normalized_value_unit_evidence: Km 1.3 mM.

raw_value_unit_evidence: Km 1.3 mM.

row_label: L-Ileu / L-Ile

substrate: L-Ile


substrate_name: L-Leu

column_label: Table 2 row L-Leu, column Km (mM) = 0.20.

row_label: L-Leu

substrate: L-Leu


substrate_name: L-Lys

column_label: Table 2 row L-Lys, column Km (mM) = 0.14.

row_label: L-Lys

substrate: L-Lys


substrate_name: L-Met

column_label: Table 2 row L-Met, column Km (mM) = 0.63.

row_label: L-Met

substrate: L-Met


organism: Rasamsonia emersonii

substrate_name: D-arginine

column_label: PMID 31420577 Table 2 'Kinetic parameters of purified ReDAAO', row d-Arg, columns kcat (s^-1), Km (mM), kcat/Km (s^-1 M^-1).

row_label: d-Arg

table_label: Table 2. Kinetic parameters of purified ReDAAO.

substrate: D-arginine


substrate_name: D-valine

column_label: PMID 31420577 Table 2 'Kinetic parameters of purified ReDAAO', row d-Val, columns kcat (s^-1), Km (mM), kcat/Km (s^-1 M^-1).

row_label: d-Val

substrate: D-valine


column_label: PMID 31420577 Table 2 'Kinetic parameters of purified ReDAAO', row d-Met, columns kcat (s^-1), Km (mM), kcat/Km (s^-1 M^-1).

row_label: d-Met


column_label: PMID 31420577 Table 2 'Kinetic parameters of purified ReDAAO', row d-Ala, columns kcat (s^-1), Km (mM), kcat/Km (s^-1 M^-1).

normalized_value_unit_evidence: paper normalized: kcat=189 s^-1; km=2.7 mM; kcat_over_km=69.9 s^-1*mM^-1 (converted from 69,900 s^-1 M^-1 / 1000). export: kcat=189.0 s^-1; km=2.7 mM; kcat_over_km=70.0 s^-1*mM^-1.

row_label: d-Ala


substrate_name: D-Glutamate

column_label: PMID 31420577 Table 2 'Kinetic parameters of purified ReDAAO', row d-Glu, columns kcat (s^-1), Km (mM), kcat/Km (s^-1 M^-1).

row_label: d-Glu

substrate: D-Glutamate


organism: Rubrobacter xylanophilus

substrate_name: D-Ile

assay_conditions_summary: pH 8; 333.15 K; buffer 50 mM potassium phosphate

column_label: Table 2. Kinetic parameters of RxDAO, row D-Ile; kcat column cell 23.0 +/- 0.4 s^-1; kcat/Km column cell 442 s^-1 mM^-1; Km column cell 0.052 +/- 0.005 mM.

row_label: RxDAO / D-Ile

table_label: Table 2. Kinetic parameters of RxDAO

substrate: D-Ile


substrate_name: D-Leu

column_label: Table 2. Kinetic parameters of RxDAO, row D-Leu; kcat column cell 24.0 +/- 0.3 s^-1; kcat/Km column cell 490 s^-1 mM^-1; Km column cell 0.049 +/- 0.004 mM.

row_label: RxDAO / D-Leu

substrate: D-Leu


substrate_name: D-Thr

column_label: Table 2. Kinetic parameters of RxDAO, row D-Thr; kcat column cell 7.6 +/- 0.3 s^-1; kcat/Km column cell 0.931 s^-1 mM^-1; Km column cell 8.16 +/- 0.93 mM.

row_label: RxDAO / D-Thr

substrate: D-Thr


substrate_name: D-Tyr

column_label: Table 2. Kinetic parameters of RxDAO, row D-Tyr; kcat column cell 53.0 +/- 8.0 s^-1; kcat/Km column cell 269 s^-1 mM^-1; Km column cell 0.197 +/- 0.043 mM.

row_label: RxDAO / D-Tyr

substrate: D-Tyr


substrate_name: D-Val

column_label: Table 2. Kinetic parameters of RxDAO, row D-Val; kcat column cell 31.4 +/- 0.7 s^-1; kcat/Km column cell 334 s^-1 mM^-1; Km column cell 0.094 +/- 0.011 mM.

row_label: RxDAO / D-Val

substrate: D-Val


substrate_name: D-Alanine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P219L to reconstruct the assayed variant sequence.

substrate: D-Alanine


substrate_name: D-proline

substrate: D-proline


substrate_name: D-serine

substrate: D-serine


substrate_name: D-cysteine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P14920 and applied mutation signature R120E to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.5; 298.15 K; cofactor FAD

column_label: Table 2: Comparison of the apparent kinetic properties of hDAAO variants (Front. Mol. Biosci. 2019, 6:125; PDF page 6), printed group heads D-Ala | D-Ser | D-Cys, each group carrying the printed column heads kcat (s^-1) | Km (mM) | kcat /Km (mM^-1 s^-1); the printed footnote of the table reads Conditions: air saturation, 25 C, pH 8.5. Cited cell: Table 2, enzyme row R120E, D-Cys column group; column kcat (s^-1) = 9.9; column Km (mM) = 0.6; column kcat /Km (mM^-1 s^-1) = 16.5. captured primary segment: D-cysteine | R120E hDAAO, the site-directed R120E variant of recombinant His-tagged human D-amino acid oxidase expressed in Escherichia coli and purified as the holoenzyme | Table 2 D-Cys group kcat 9.9 s^-1 | Table 2 D-Cys group Km 0.6 mM | Table 2 D-Cys group kcat/Km printed cell 16.5 under the column head kcat /Km (mM^-1 s^-1)

normalized_value_unit_evidence: kcat: printed Table 2 cell 9.9 s^-1 in the D-Cys group; the printed column head is kcat (s^-1) and the canonical unit is s^(-1), so no unit conversion applies and the canonical value is 9.9 s^(-1). Km: printed Table 2 cell 0.6 mM in the D-Cys group; the printed column head is Km (mM) and the canonical unit is mM, so no unit conversion applies and the canonical value is 0.6 mM. kcat/Km: printed Table 2 cell 16.5 in the D-Cys group under the column head kcat /Km (mM^-1 s^-1); mM^-1 s^-1 is the canonical unit s^(-1)*mM^(-1) written the other way round, so no unit conversion applies and the canonical value is 16.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: PDF page 6, Table 2, enzyme row R120E, D-Cys column group: kcat = 9.9 s^-1; Km = 0.6 mM; kcat/Km = 16.5 under the printed column head kcat /Km (mM^-1 s^-1).

substrate: D-cysteine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P14920 and applied mutation signature R120L to reconstruct the assayed variant sequence.

column_label: Table 2: Comparison of the apparent kinetic properties of hDAAO variants (Front. Mol. Biosci. 2019, 6:125; PDF page 6), printed group heads D-Ala | D-Ser | D-Cys, each group carrying the printed column heads kcat (s^-1) | Km (mM) | kcat /Km (mM^-1 s^-1); the printed footnote of the table reads Conditions: air saturation, 25 C, pH 8.5. Cited cell: Table 2, enzyme row R120L, D-Cys column group; column kcat (s^-1) = 15.6; column Km (mM) = 0.7; column kcat /Km (mM^-1 s^-1) = 22.6. captured primary segment: D-cysteine | R120L hDAAO, the site-directed R120L variant of recombinant His-tagged human D-amino acid oxidase expressed in Escherichia coli and purified as the holoenzyme | Table 2 D-Cys group kcat 15.6 s^-1 | Table 2 D-Cys group Km 0.7 mM | Table 2 D-Cys group kcat/Km printed cell 22.6 under the column head kcat /Km (mM^-1 s^-1)

normalized_value_unit_evidence: kcat: printed Table 2 cell 15.6 s^-1 in the D-Cys group; the printed column head is kcat (s^-1) and the canonical unit is s^(-1), so no unit conversion applies and the canonical value is 15.6 s^(-1). Km: printed Table 2 cell 0.7 mM in the D-Cys group; the printed column head is Km (mM) and the canonical unit is mM, so no unit conversion applies and the canonical value is 0.7 mM. kcat/Km: printed Table 2 cell 22.6 in the D-Cys group under the column head kcat /Km (mM^-1 s^-1); mM^-1 s^-1 is the canonical unit s^(-1)*mM^(-1) written the other way round, so no unit conversion applies and the canonical value is 22.6 s^(-1)*mM^(-1).

raw_value_unit_evidence: PDF page 6, Table 2, enzyme row R120L, D-Cys column group: kcat = 15.6 s^-1; Km = 0.7 mM; kcat/Km = 22.6 under the printed column head kcat /Km (mM^-1 s^-1).


column_label: Table 2: Comparison of the apparent kinetic properties of hDAAO variants (Front. Mol. Biosci. 2019, 6:125; PDF page 6), printed group heads D-Ala | D-Ser | D-Cys, each group carrying the printed column heads kcat (s^-1) | Km (mM) | kcat /Km (mM^-1 s^-1); the printed footnote of the table reads Conditions: air saturation, 25 C, pH 8.5. Cited cell: Table 2, enzyme row R120E, D-Ser column group; column kcat (s^-1) = 8.5; column Km (mM) = 17.6; column kcat /Km (mM^-1 s^-1) = 0.5. captured primary segment: D-serine | R120E hDAAO, the site-directed R120E variant of recombinant His-tagged human D-amino acid oxidase expressed in Escherichia coli and purified as the holoenzyme | Table 2 D-Ser group kcat 8.5 s^-1 | Table 2 D-Ser group Km 17.6 mM | Table 2 D-Ser group kcat/Km printed cell 0.5 under the column head kcat /Km (mM^-1 s^-1)

normalized_value_unit_evidence: kcat: printed Table 2 cell 8.5 s^-1 in the D-Ser group; the printed column head is kcat (s^-1) and the canonical unit is s^(-1), so no unit conversion applies and the canonical value is 8.5 s^(-1). Km: printed Table 2 cell 17.6 mM in the D-Ser group; the printed column head is Km (mM) and the canonical unit is mM, so no unit conversion applies and the canonical value is 17.6 mM. kcat/Km: printed Table 2 cell 0.5 in the D-Ser group under the column head kcat /Km (mM^-1 s^-1); mM^-1 s^-1 is the canonical unit s^(-1)*mM^(-1) written the other way round, so no unit conversion applies and the canonical value is 0.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: PDF page 6, Table 2, enzyme row R120E, D-Ser column group: kcat = 8.5 s^-1; Km = 17.6 mM; kcat/Km = 0.5 under the printed column head kcat /Km (mM^-1 s^-1).


column_label: Table 2: Comparison of the apparent kinetic properties of hDAAO variants (Front. Mol. Biosci. 2019, 6:125; PDF page 6), printed group heads D-Ala | D-Ser | D-Cys, each group carrying the printed column heads kcat (s^-1) | Km (mM) | kcat /Km (mM^-1 s^-1); the printed footnote of the table reads Conditions: air saturation, 25 C, pH 8.5. Cited cell: Table 2, enzyme row R120L, D-Ser column group; column kcat (s^-1) = 11.3; column Km (mM) = 26.7; column kcat /Km (mM^-1 s^-1) = 0.4. captured primary segment: D-serine | R120L hDAAO, the site-directed R120L variant of recombinant His-tagged human D-amino acid oxidase expressed in Escherichia coli and purified as the holoenzyme | Table 2 D-Ser group kcat 11.3 s^-1 | Table 2 D-Ser group Km 26.7 mM | Table 2 D-Ser group kcat/Km printed cell 0.4 under the column head kcat /Km (mM^-1 s^-1)

normalized_value_unit_evidence: kcat: printed Table 2 cell 11.3 s^-1 in the D-Ser group; the printed column head is kcat (s^-1) and the canonical unit is s^(-1), so no unit conversion applies and the canonical value is 11.3 s^(-1). Km: printed Table 2 cell 26.7 mM in the D-Ser group; the printed column head is Km (mM) and the canonical unit is mM, so no unit conversion applies and the canonical value is 26.7 mM. kcat/Km: printed Table 2 cell 0.4 in the D-Ser group under the column head kcat /Km (mM^-1 s^-1); mM^-1 s^-1 is the canonical unit s^(-1)*mM^(-1) written the other way round, so no unit conversion applies and the canonical value is 0.4 s^(-1)*mM^(-1).

raw_value_unit_evidence: PDF page 6, Table 2, enzyme row R120L, D-Ser column group: kcat = 11.3 s^-1; Km = 26.7 mM; kcat/Km = 0.4 under the printed column head kcat /Km (mM^-1 s^-1).


column_label: Table 2: Comparison of the apparent kinetic properties of hDAAO variants (Front. Mol. Biosci. 2019, 6:125; PDF page 6), printed group heads D-Ala | D-Ser | D-Cys, each group carrying the printed column heads kcat (s^-1) | Km (mM) | kcat /Km (mM^-1 s^-1); the printed footnote of the table reads Conditions: air saturation, 25 C, pH 8.5. Cited cell: Table 2, enzyme row R120E, D-Ala column group; column kcat (s^-1) = 12.6; column Km (mM) = 1.4; column kcat /Km (mM^-1 s^-1) = 8.9. captured primary segment: D-alanine | R120E hDAAO, the site-directed R120E variant of recombinant His-tagged human D-amino acid oxidase expressed in Escherichia coli and purified as the holoenzyme | Table 2 D-Ala group kcat 12.6 s^-1 | Table 2 D-Ala group Km 1.4 mM | Table 2 D-Ala group kcat/Km printed cell 8.9 under the column head kcat /Km (mM^-1 s^-1)

normalized_value_unit_evidence: kcat: printed Table 2 cell 12.6 s^-1 in the D-Ala group; the printed column head is kcat (s^-1) and the canonical unit is s^(-1), so no unit conversion applies and the canonical value is 12.6 s^(-1). Km: printed Table 2 cell 1.4 mM in the D-Ala group; the printed column head is Km (mM) and the canonical unit is mM, so no unit conversion applies and the canonical value is 1.4 mM. kcat/Km: printed Table 2 cell 8.9 in the D-Ala group under the column head kcat /Km (mM^-1 s^-1); mM^-1 s^-1 is the canonical unit s^(-1)*mM^(-1) written the other way round, so no unit conversion applies and the canonical value is 8.9 s^(-1)*mM^(-1).

raw_value_unit_evidence: PDF page 6, Table 2, enzyme row R120E, D-Ala column group: kcat = 12.6 s^-1; Km = 1.4 mM; kcat/Km = 8.9 under the printed column head kcat /Km (mM^-1 s^-1).


column_label: Table 2: Comparison of the apparent kinetic properties of hDAAO variants (Front. Mol. Biosci. 2019, 6:125; PDF page 6), printed group heads D-Ala | D-Ser | D-Cys, each group carrying the printed column heads kcat (s^-1) | Km (mM) | kcat /Km (mM^-1 s^-1); the printed footnote of the table reads Conditions: air saturation, 25 C, pH 8.5. Cited cell: Table 2, enzyme row R120L, D-Ala column group; column kcat (s^-1) = 17.3; column Km (mM) = 2.0; column kcat /Km (mM^-1 s^-1) = 8.5. captured primary segment: D-alanine | R120L hDAAO, the site-directed R120L variant of recombinant His-tagged human D-amino acid oxidase expressed in Escherichia coli and purified as the holoenzyme | Table 2 D-Ala group kcat 17.3 s^-1 | Table 2 D-Ala group Km 2.0 mM | Table 2 D-Ala group kcat/Km printed cell 8.5 under the column head kcat /Km (mM^-1 s^-1)

normalized_value_unit_evidence: kcat: printed Table 2 cell 17.3 s^-1 in the D-Ala group; the printed column head is kcat (s^-1) and the canonical unit is s^(-1), so no unit conversion applies and the canonical value is 17.3 s^(-1). Km: printed Table 2 cell 2.0 mM in the D-Ala group; the printed column head is Km (mM) and the canonical unit is mM, so no unit conversion applies and the canonical value is 2.0 mM. kcat/Km: printed Table 2 cell 8.5 in the D-Ala group under the column head kcat /Km (mM^-1 s^-1); mM^-1 s^-1 is the canonical unit s^(-1)*mM^(-1) written the other way round, so no unit conversion applies and the canonical value is 8.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: PDF page 6, Table 2, enzyme row R120L, D-Ala column group: kcat = 17.3 s^-1; Km = 2.0 mM; kcat/Km = 8.5 under the printed column head kcat /Km (mM^-1 s^-1).


organism: [Candida] boidinii


substrate_name: D-leucine

substrate: D-leucine


substrate_name: D-methionine

substrate: D-methionine


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


enzyme_display_name: L-amino acid oxidase

organism: Cerastes cerastes

enzyme: L-amino acid oxidase


substrate_name: L-Leu

substrate: L-Leu


substrate_name: L-Phe

substrate: L-Phe


organism: Trigonopsis variabilis

substrate_name: cephalosporin C

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F54A with inferred residue-numbering offset -21 to reconstruct the assayed variant sequence.

substrate: cephalosporin C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F54S with inferred residue-numbering offset -21 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F54Y with inferred residue-numbering offset -21 to reconstruct the assayed variant sequence.


organism: Hebeloma cylindrosporum

substrate_name: L-glutamine

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

raw_value_unit_evidence: Acid-activated Table 2 row L-Glutamine: vmax 33.6 +/- 7.4 U mg^-1; Km 0.56 +/- 0.17 mM; kcat 38.8 s^-1; kcat/Km 69.4.

row_label: L-Glutamine

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

substrate: L-glutamine


substrate_name: L-leucine

column_label: Columns Substrate, vmax [U mg^-1], Km [mM], kcat [s^-1], kcat/Km; acid-activated block row L-Leucine.

raw_value_unit_evidence: Acid-activated Table 2 row L-Leucine: vmax 39.2 +/- 12.1 U mg^-1; Km 0.26 +/- 0.13 mM; kcat 45.3 s^-1; kcat/Km 176.2.

row_label: L-Leucine

substrate: L-leucine


substrate_name: L-leucine methyl ester

column_label: Columns Substrate, vmax [U mg^-1], Km [mM], kcat [s^-1], kcat/Km; acid-activated block row L-Leucine methyl ester.

raw_value_unit_evidence: Acid-activated Table 2 row L-Leucine methyl ester: vmax 24.1 +/- 6.7 U mg^-1; Km 0.67 +/- 0.40 mM; kcat 27.8 s^-1; kcat/Km 41.5.

row_label: L-Leucine methyl ester

substrate: L-leucine methyl ester


substrate_name: L-Phenylalanine

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

raw_value_unit_evidence: Acid-activated Table 2 row L-Phenylalanine: vmax 18.9 +/- 0.7 U mg^-1; Km 0.48 +/- 0.16 mM; kcat 21.9 s^-1; kcat/Km 45.2.

row_label: L-Phenylalanine

substrate: L-Phenylalanine


enzyme_display_name: monoamine oxidase

column_label: Table 3 row Phenylethylamine under Rat MAO A lists kcat 85.0 +/- 0.7 min^-1, Km 0.35 +/- 0.01 mM, and kcat/Km 242.9 +/- 7.2 min^-1 mM^-1.

normalized_value_unit_evidence: kcat normalized=1.4166666666666667 s^-1; Km normalized=0.35 mM; kcat/Km normalized=4.057142857142857 s^-1 mM^-1 from exported rounded kcat/Km quotient

row_label: Phenylethylamine

table_label: Table 3. Comparison of substrate and inhibitor specificities for purified rat and human MAO A

enzyme: monoamine oxidase


substrate_name: benzylamine

column_label: Table 3 row Benzylamine under Rat MAO A lists kcat 19.5 +/- 0.2 min^-1, Km 0.21 +/- 0.02 mM, and kcat/Km 92.9 +/- 8.9 min^-1 mM^-1.

normalized_value_unit_evidence: kcat normalized=0.325 s^-1; Km normalized=0.21 mM; kcat/Km normalized=1.5476190476190477 s^-1 mM^-1 from rounded kcat/Km quotient

row_label: Benzylamine

substrate: benzylamine


substrate_name: kynuramine

column_label: Table 3 row Kynuramine under Rat MAO A lists kcat 149.1 +/- 1.7 min^-1, Km 0.09 +/- 0.01 mM, and kcat/Km 1656.7 +/- 185.0 min^-1 mM^-1.

normalized_value_unit_evidence: kcat normalized=2.485 s^-1; Km normalized=0.09 mM; kcat/Km normalized=27.61111111111111 s^-1 mM^-1 from rounded kcat/Km quotient

row_label: Kynuramine

substrate: kynuramine


substrate_name: serotonin

column_label: Table 3 row Serotonin under Rat MAO A lists kcat 358.7 +/- 6.7 min^-1, Km 0.30 +/- 0.02 mM, and kcat/Km 1195.7 +/- 82.8 min^-1 mM^-1.

normalized_value_unit_evidence: kcat normalized=5.9783333333333335 s^-1; Km normalized=0.30 mM; kcat/Km normalized=19.933333333333337 s^-1 mM^-1 from exported rounded kcat/Km quotient

row_label: Serotonin

substrate: serotonin


organism: Vipera berus berus

substrate_name: L-Leucine

proof_lines:
Vipera berus berus
L-amino acid oxidase
isolated and characterized structurally

substrate: L-Leucine


substrate_name: L-Methionine

substrate: L-Methionine


organism: Caenorhabditis elegans

substrate_name: D-Arginine

substrate: D-Arginine


substrate_name: D-Alanine

substrate: D-Alanine


substrate_name: D-Methionine

assay_conditions_summary: pH 8.3; 310.15 K; buffer pH 8; cofactor FAD

column_label: Table 2. Kinetic parameters of purified recombinant Y69Ap, C47Ap, and F18Ep; row Y69Ap / D-Met; column(s) kcat (s^-1); Km (mM); kcat/Km (s^-1*M^-1) plus normalized mM conversion

normalized_value_unit_evidence: kcat normalized_value=4.98 normalized_unit=s^-1; Km normalized_value=1.22 normalized_unit=mM; kcat/Km normalized_value=4.081967213114755 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=4.98 raw_unit=s^-1; Km raw_value=1.22 raw_unit=mM; table kcat/Km raw_value=4082 raw_unit=s^-1*M^-1; kcat/Km computed_from_table_kcat_km=4.98/1.22 raw_unit=s^-1*mM^-1

row_label: Y69Ap / D-Met

substrate: D-Methionine


substrate_name: D-cycloserine

column_label: Table 1 row D-Cycloserine; columns kcat (s^-1), Km (mM), kcat/Km (mM^-1 x s^-1)

row_label: D-Cycloserine

table_label: Table 1

substrate: D-cycloserine


substrate_name: D-cysteine

substrate: D-cysteine


substrate_name: D-kynurenine

column_label: Table 1 row D-Kynurenine; columns kcat (s^-1), Km (mM), kcat/Km (mM^-1 x s^-1)

row_label: D-Kynurenine

substrate: D-kynurenine


organism: Bothriechis schlegelii

proof_lines:
BslAAO
Bothriechis schlegelii
L-amino acid oxidase


enzyme_display_name: L-amino acid oxidase Bs29

substrate_name: L-Leu

enzyme: L-amino acid oxidase Bs29

substrate: L-Leu


organism: Aplysia californica

substrate_name: L-Lys

substrate: L-Lys


substrate_name: L-Arg

substrate: L-Arg


substrate_name: D-Dopa

substrate: D-Dopa


substrate_name: D-Phenylalanine

proof_lines:
human DAO
D-phenylalanine
aromatic D-amino acids

substrate: D-Phenylalanine


substrate_name: D-Tyrosine

proof_lines:
human DAO
D-tyrosine
natural D-amino acids

substrate: D-Tyrosine


organism: Sus scrofa

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y224F with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.


smiles: O=O


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y228F with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


organism: Neurospora crassa

substrate_name: L-phenylalanine

substrate: L-phenylalanine


organism: Crotalus durissus terrificus

substrate_name: L-Tyr

proof_lines: LAAOcdt L-Tyr L-Phe

substrate: L-Tyr


substrate_name: L-Ala

proof_lines: LAAOcdt L-Ala

substrate: L-Ala


organism: Rhodosporidium toruloides

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R285K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R285A to reconstruct the assayed variant sequence.


substrate_name: D-ethionine

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

proof_lines:
15 D-amino acids
23 tested

substrate: D-ethionine


substrate_name: D-citrulline

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

proof_lines:
D-citrulline
maximal activity
D-isoleucine

substrate: D-citrulline


substrate_name: D-arginine

substrate: D-arginine


enzyme_display_name: UniProt Q9NVS9

organism: Homo sapiens

substrate_name: pyridoxine 5'-phosphate

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

proof_lines:
PNPO
human pyridoxine 5'-phosphate oxidase
genomic organization

enzyme: UniProt Q9NVS9

substrate: pyridoxine 5'-phosphate


enzyme_display_name: Pyridoxine-5'-phosphate oxidase

substrate_name: pyridoxamine 5'-phosphate

enzyme: Pyridoxine-5'-phosphate oxidase

substrate: pyridoxamine 5'-phosphate


organism: Bombyx mori

substrate_name: pyridoxamine 5'-phosphate (at pH 9.0 and 37 degrees Celsius)


substrate_name: pyridoxine 5'-phosphate (at pH 9.0 and 37 degrees Celsius)


substrate_name: L-Leu (Cc-LAAOI isoform)

substrate: L-Leu (Cc-LAAOI isoform)


organism: Bos taurus

substrate_name: benzylamine

column_label: Table 1 row H, column Km(amine) (uM)

row_label: H; unsubstituted benzylamine

table_label: Table 1: Steady-State Kinetic Constants for the MAO B-Catalyzed Oxidation of para- and meta-Substituted Benzylamine Analogues

substrate: benzylamine


substrate_name: dioxygen

column_label: Table 1 row H, column Km(O2) (uM)

substrate: dioxygen


organism: Chlamydomonas reinhardtii

substrate_name: S-ribosyl-L-homocysteine

proof_lines:
Chlamydomonas reinhardtii
protein M
L-amino-acid oxidase

substrate: S-ribosyl-L-homocysteine


organism: Aspergillus niger

proof_lines:
monoamine oxidase (MAO-N)
1,2,3,4-tetrahydronaphthylamines (THNs)
1,2,3,4-tetrahydronaphthalen-1-amine


proof_lines:
monoamine oxidase (MAO-N)
indanylamines
2,3-dihydro-1H-inden-1-amine


organism: Crotalus durissus cumanensis

substrate_name: L-Leucine

substrate: L-Leucine


organism: Platichthys stellatus

substrate_name: L-lysine

proof_lines: psLAAO1 Km kcat/Km

substrate: L-lysine


organism: Mus musculus

substrate_name: phenylalanine (at 37 degrees Celsius)

substrate: phenylalanine (at 37 degrees Celsius)


organism: Rattus norvegicus

substrate_name: S-adenosyl-L-homocysteine

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

substrate: S-adenosyl-L-homocysteine


enzyme_display_name: pyridoxal 5'-phosphate synthase

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R95C to reconstruct the assayed variant sequence.

enzyme: pyridoxal 5'-phosphate synthase


organism: Protobothrops mucrosquamatus

substrate_name: L-leucine

sequence: ADNKNPLEECFRETNYEEFLEIAR

wild_type_sequence: ADNKNPLEECFRETNYEEFLEIAR

column_label: Abstract reports for oxidative deamination of Leu the Km and Vmax were 1.17 mM and 9.9 units/mg protein.

raw_value_unit_evidence: Km raw_value=1.17 mM raw_unit=mM

row_label: L-amino acid oxidase from Trimeresurus mucrosquamatus venom / L-leucine

table_label: PubMed XML abstract PMID 3188059

substrate: L-leucine


enzyme_display_name: L-amino oxidase

organism: Trimeresurus purpureomaculatus

column_label: Section 2.3 reports Vmax and Km values of 16.77 mM/min and 4.376, respectively, obtained from the Michaelis-Menten model for purified LAAO at every L-leucine substrate concentration.

raw_value_unit_evidence: Km raw_value=4.376 raw_unit=mM

row_label: CP-LAAO purified from Cryptelytrops purpureomaculatus venom / L-leucine

table_label: Section 2.3 L-amino Acid Oxidase Assay and Figure 2 Michaelis-Menten model

enzyme: L-amino oxidase


enzyme_display_name: L-amino-acid oxidase

organism: Crotalus atrox

substrate_name: L-Met

proof_lines: kinetic contents of L-amino acid oxidase

enzyme: L-amino-acid oxidase

substrate: L-Met


organism: Gloydius halys

substrate_name: L-Leu

substrate: L-Leu


enzyme_display_name: D-amino-acid oxidase

substrate_name: D-Alanine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y238S with inferred residue-numbering offset -15 to reconstruct the assayed variant sequence.

column_label: PDF text lines 337-359 contain the D-alanine turnover section and Table 3. The Y238S row has kcat 120 and Km,D-Ala 7.8 under the stated assay conditions.

normalized_value_unit_evidence: kcat 120 s^-1; Km 7.8 mM; kcat/Km derived from the same printed cells as 120 / 7.8 = 15.384615384615385 s^-1 mM^-1.

raw_value_unit_evidence: Table 3 Y238S row reports kcat 120 s^-1 and Km,D-Ala 7.8 mM. The paper text identifies Y238S as a mutant of RgDAAO and the assay substrate as D-alanine.

table_label: Table 3. Comparison of the steady-state coefficients obtained from stopped-flow experiments of wild-type and Y238 mutants of D-amino acid oxidase

enzyme: D-amino-acid oxidase

substrate: D-Alanine


substrate_name: kynuramine

proof_lines:
Raw SKiD Env: Temp=30C, pH=7.2
Raw SKiD Env: Temp=-----, pH=7.5
Raw SKiD Env: Temp=-----, pH=-----

substrate: kynuramine


organism: Caenorhabditis elegans

substrate_name: D-Histidine

proof_lines: D-Arg D-His

substrate: D-Histidine


substrate_name: D-Phenylalanine

proof_lines:
D-Arg
D-His
functional DAO

substrate: D-Phenylalanine


substrate_name: D-Serine

proof_lines:
D-Ser
human DAO

substrate: D-Serine


organism: Cyprinus carpio


proof_lines: Structure of human monoamine oxidase A at 2.2-A resolution


organism: Sus scrofa

substrate_name: H2O; D-Alanine; O2

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

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

substrate: H2O; D-Alanine; O2


substrate_name: D-Pro

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

proof_lines:
wild-type enzyme
wild-type

substrate: D-Pro


substrate_name: D-Val

substrate: D-Val


substrate_name: D-Phe

substrate: D-Phe


substrate_name: D-Ala

substrate: D-Ala


substrate_name: D-Lys

substrate: D-Lys


substrate_name: D-Met

substrate: D-Met


substrate_name: D-Arg

substrate: D-Arg


substrate_name: D-Ser

substrate: D-Ser


substrate_name: benzylamine

substrate: benzylamine


substrate_name: p-nitrobenzylamine

substrate: p-nitrobenzylamine


substrate_name: p-trifluoromethyl-benzylamine

substrate: p-trifluoromethyl-benzylamine


proof_lines:
pH 7.5, 25°C, mutant enzyme Y435F
monoamine oxidase B mutant Y435F


assay_conditions_summary: pH 7.5; 298.15 K; buffer 50 mM phosphate

proof_lines: wild type isoform MAO B, at 25°C in 50 mM phosphate buffer (pH 7.5)


substrate_name: p-nitrophenylethylamine

substrate: p-nitrophenylethylamine


substrate_name: D-Alanine

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

proof_lines:
D-amino acid oxidase
human DAO
C. elegans DAO

substrate: D-Alanine


substrate_name: D-Arginine

proof_lines:
D-arginine
human DAO
C. elegans DAO

substrate: D-Arginine


substrate_name: D-Histidine

proof_lines:
D-histidine
human DAO
C. elegans DAO

substrate: D-Histidine


proof_lines:
wild-type enzyme
wild-type
pH 8.3, 37°C, wild-type enzyme


sequence_variant_note: Resolved canonical sequence from manual_literature_uniprot_resolution and applied mutation signature Y402A to reconstruct the assayed variant sequence.


substrate_name: tryptamine

substrate: tryptamine


substrate_name: serotonin

substrate: serotonin


substrate_name: tyramine

substrate: tyramine


sequence_variant_note: Resolved canonical sequence from manual_literature_uniprot_resolution and applied mutation signature Y402F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from manual_literature_uniprot_resolution and applied mutation signature Y410A to reconstruct the assayed variant sequence.


substrate_name: D-Ile

substrate: D-Ile


substrate_name: D-Leu

substrate: D-Leu


substrate_name: D-Tyr

substrate: D-Tyr


substrate_name: D-Phe

substrate: D-Phe


substrate_name: D-Pro

substrate: D-Pro


substrate_name: D-Val

substrate: D-Val


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


substrate_name: D-phenylalanine

proof_lines:
wild-type, 30°C, pH 8.0
wild-type enzyme
wild-type

substrate: D-phenylalanine


proof_lines: mutant Y228L/R283G, pH 8, 25°C. The kcat/Km profile exhibits a maximum at pH 10


organism: Escherichia coli

substrate_name: pyridoxine 5'-phosphate

substrate: pyridoxine 5'-phosphate


assay_conditions_summary: pH 8.5; 310.15 K; buffer phosphate and HEPES

proof_lines: recombinant enzyme, in phosphate and HEPES buffer at pH 7.6


proof_lines: pH 7.6, 37°C, mutant enzyme N84W/K145A/F177A


proof_lines: pH 7.6, 37°C, mutant enzyme N84A/K145A/F177A


proof_lines: pH 7.6, 37°C, mutant enzyme R23L/R24L/R215L


proof_lines:
pH 7.6, 37°C, mutant enzyme R23L-R24L
pH 7.6, 37°C, mutant enzyme R23L/R24L


organism: Homo sapiens

substrate_name: benzylamine

substrate: benzylamine


assay_conditions_summary: pH 7.2; 303.15 K; buffer 50 mM phosphate


substrate_name: Phenylethylamine

substrate: Phenylethylamine


substrate_name: kynuramine

substrate: kynuramine


proof_lines:
pH 7.2, 30°C, wild-type enzyme
monoamine oxidase A wild-type enzyme


proof_lines: mutant enzyme I199A, at 25°C in 50 mM phosphate buffer (pH 7.5)


substrate_name: phenylbutylamine

substrate: phenylbutylamine


substrate_name: D-cysteine

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

substrate: D-cysteine


substrate_name: D-alanine

proof_lines:
wild-type, pH 8.5, 25°C
wild-type, pH 8.0, 25°C
wild-type

substrate: D-alanine


substrate_name: D-serine

substrate: D-serine


substrate_name: n-butylamine

smiles: CCCCN

substrate: n-butylamine


substrate_name: alpha-methylbenzylamine

substrate: alpha-methylbenzylamine


substrate_name: amylamine

smiles: CCCCCN

substrate: amylamine


enzyme_display_name: glutamate dehydrogenase [NAD(P)+]

proof_lines: inhibition of microtubules to membrane-bound liver enzyme

enzyme: glutamate dehydrogenase [NAD(P)+]


substrate_name: FAD

assay_conditions_summary: cofactor FAD

substrate: FAD


substrate_name: D-Norvaline

substrate: D-Norvaline


substrate_name: methylene blue

substrate: methylene blue


substrate_name: D-norleucine

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

substrate: D-norleucine


substrate_name: tryptamine

substrate: tryptamine


substrate_name: tyramine

substrate: tyramine


substrate_name: dopamine

substrate: dopamine


assay_conditions_summary: pH 7.5; 298.15 K; buffer 50 mM potassium phosphate assay

proof_lines:
at pH 7.5 and 25°C
in presence of 3 mM KCN
in presence of 2 mM KCN


substrate_name: D-leucine

substrate: D-leucine


substrate_name: D-methionine

substrate: D-methionine


substrate_name: D-valine

substrate: D-valine


substrate_name: D-phenylalanine

substrate: D-phenylalanine


substrate_name: D-tyrosine

substrate: D-tyrosine


substrate_name: D-phenylglycine

substrate: D-phenylglycine


substrate_name: pyridoxine 5'-phosphate

substrate: pyridoxine 5'-phosphate


proof_lines:
wild type enzyme, at pH 8.0 and 37°C
pH 7.6, 37°C, wild-type enzyme


proof_lines: pH 7.6, 37°C, wild-type enzyme, HEPES buffer

proof_lines: pH 7.6, 37°C, wild-type enzyme, TRIS buffer


proof_lines:
at pH 7.5 and 25°C
at pH 9.0 and 25°C


substrate_name: pyridoxamine 5'-phosphate

substrate: pyridoxamine 5'-phosphate


mutation_signature: Δ1

mutation_type: deletion


substrate_name: Unknown

proof_lines: pH 8.5, 25°C, pyridoxine 5'-phosphate as substrate, wild-type enzyme

substrate: Unknown


proof_lines: pH 8.5, 25°C, pyridoxine 5'-phosphate as substrate, mutant enzyme DELTA1-56


substrate_name: D-serine

substrate: D-serine


substrate_name: D-alanine

substrate: D-alanine


substrate_name: D-proline

substrate: D-proline


substrate_name: D-Met

substrate: D-Met


substrate_name: D-Ala

substrate: D-Ala


substrate_name: D-Phe

substrate: D-Phe


substrate_name: D-Ser

substrate: D-Ser


substrate_name: benzylamine

proof_lines: isoform MAO A, in 50 mM potassium phosphate assay buffer (pH 7.5), at 25°C

substrate: benzylamine


substrate_name: kynuramine

substrate: kynuramine


substrate_name: Phenylethylamine

substrate: Phenylethylamine


substrate_name: serotonin

substrate: serotonin


substrate_name: D-phenylalanine

substrate: D-phenylalanine


substrate_name: D-methionine

substrate: D-methionine


substrate_name: ethylamine

smiles: CCN

substrate: ethylamine


substrate_name: n-butylamine

substrate: n-butylamine


substrate_name: pyridoxine 5'-phosphate

substrate: pyridoxine 5'-phosphate


substrate_name: pyridoxamine 5'-phosphate

proof_lines:
pH 7.6, 37°C
measured in hemolysate

substrate: pyridoxamine 5'-phosphate


substrate_name: Unknown

proof_lines: pH and temperature not specified in the publication

substrate: Unknown


proof_lines:
pH 8.5, 25°C
apparent value, at 25°C
at pH 7.0 and 25°C


substrate_name: D-Asp

proof_lines:
pH 8.5, 25°C
at pH 7.0 and 25°C

substrate: D-Asp


substrate_name: D-Pro

proof_lines:
pH 8.5, 25°C
at pH 7.0 and 25°C
pH 8.3, 25°C

substrate: D-Pro


organism: Ophiophagus hannah

substrate_name: L-histidine

substrate: L-histidine


substrate_name: L-lysine

substrate: L-lysine


substrate_name: L-isoleucine

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

substrate: L-isoleucine


substrate_name: D-tryptophan

substrate: D-tryptophan


assay_conditions_summary: pH 7; 298.15 K; buffer 50 mM sodium diphosphate

proof_lines: in 50 mM sodium diphosphate buffer (pH 8.3) at 25°C


substrate_name: D-tyrosine

substrate: D-tyrosine


substrate_name: hexamethyleneimine

substrate: hexamethyleneimine


substrate_name: heptamethyleneimine

substrate: heptamethyleneimine


substrate_name: D-kynurenine

substrate: D-kynurenine


substrate_name: D-cycloserine

substrate: D-cycloserine


substrate_name: D-cysteine

substrate: D-cysteine


proof_lines:
pH 7.8, 30°C, variant D11
pH 7.8, 30°C, enzyme variant D9


proof_lines: recombinant enzyme after cleavage from fusion protein


substrate_name: L-Ala

proof_lines:
at pH 7.0 and 37°C
apparent value, at 25°C
at pH 9.8 and 37°C

substrate: L-Ala


substrate_name: L-Pro

proof_lines:
at pH 8.5 and 37°C
at pH 7.5 and 37°C
at pH 8.0 and 37°C

substrate: L-Pro


substrate_name: L-Asp

substrate: L-Asp


organism: Bos taurus

substrate_name: Phenylethylamine

substrate: Phenylethylamine


enzyme_display_name: alanine dehydrogenase

organism: Halobacterium salinarum

substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

enzyme: alanine dehydrogenase

substrate: NAD+


substrate_name: pyruvate

substrate: pyruvate


organism: Crotalus adamanteus

substrate_name: L-phenylalanine

substrate: L-phenylalanine


substrate_name: L-propargylglycine

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

substrate: L-propargylglycine


substrate_name: L-Trp

substrate: L-Trp


substrate_name: L-Phe

substrate: L-Phe


substrate_name: L-Met

substrate: L-Met


substrate_name: dopamine

substrate: dopamine


substrate_name: serotonin

proof_lines:
11°C
monoamine oxidase A
monoamine oxidase B

substrate: serotonin


proof_lines: pH 7.5, MAO-A incorporated into phospholipid nanodisks


substrate_name: kynuramine

substrate: kynuramine


substrate_name: D-alanine

substrate: D-alanine


substrate_name: NADH

assay_conditions_summary: pH 8; 298.15 K; cofactor NADH

substrate: NADH


enzyme_display_name: dihydrofolate reductase

proof_lines: recombinant wild-type enzyme, pH 7.4, 37°C

proof_lines: pH 7.4, 37°C, wild-type enzyme and mutant N64F

enzyme: dihydrofolate reductase


substrate_name: Unknown

proof_lines:
wild-type, pH 7.6, 23°C
pH 7.4, 37°C, wild-type enzyme
wild-type, pH 7.0, 25°C

substrate: Unknown


proof_lines: mutant enzyme L415M/S443R/A456G, 50 mM triethanolamine pH 8.0, 100 mM ammonium acetate, 0.1 mM NADH, and 2 mM EDTA, pH 8.0 at 25°C


substrate_name: NADPH

assay_conditions_summary: pH 6.7; 298.15 K; cofactor NADPH

substrate: NADPH


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


substrate_name: D-serine

assay_conditions_summary: pH 8.5; 298.15 K; buffer 50 mM sodium diphosphate

proof_lines:
pH 8.5, 25°C, recombinant EGFP-DAAO
pH 8.3, 25°C
pH 8.5, 25°C

substrate: D-serine


proof_lines: pH 8.5, 25°C, recombinant wild-type DAAO


substrate_name: dihydrofolate

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

proof_lines:
pH 7.5, 25°C, cosubstrate: NADPH
pH 7.5, 25°C

substrate: dihydrofolate


proof_lines: pH 7.5, 25°C, cosubstrate: dihydrofolate

proof_lines: for native and recombinant enzymes, monophasic


enzyme_display_name: pyrroline-5-carboxylate reductase

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADH

enzyme: pyrroline-5-carboxylate reductase


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH


enzyme_display_name: 6,7-dihydropteridine reductase

substrate_name: tetrahydrobiopterin

enzyme: 6,7-dihydropteridine reductase

substrate: tetrahydrobiopterin


assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADPH

proof_lines: wild-type, cosubstrate NADPH, pH 7.5, 37°C

proof_lines: pH 7.5, 37°C, recombinant wild-type enzyme, with NADPH


enzyme_display_name: primary-amine oxidase

substrate_name: tyramine

proof_lines: recombinant enzyme expressed in CHO cells

enzyme: primary-amine oxidase

substrate: tyramine


substrate_name: tryptamine

substrate: tryptamine


substrate_name: folate

substrate: folate


proof_lines:
pH 6.0
recombinant enzyme
pH 7.4, 37°C


assay_conditions_summary: pH 8; 303.15 K; cofactor NADP+

proof_lines: pH 8.0, 30°C, at saturating concentrations of NADP+ (6.0 mM)

proof_lines: pH 8.0, 30°C, at saturating concentrations of NAD+ (1.0 mM)


organism: Lathyrus oleraceus

substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

substrate: NADP+


substrate_name: tetrahydropteroylglutamic acid

substrate: tetrahydropteroylglutamic acid


substrate_name: benzylamine

substrate: benzylamine


substrate_name: hexakis(benzylammonium) decavanadate (V) dihydrate


assay_conditions_summary: pH 7.2; 310.15 K; buffer 100 mM potassium phosphate

proof_lines: cobalt-substituted wild type enzyme, with putrescine as cosubstrate, in 100 mM potassium phosphate buffer, pH 7.2, 37°C

proof_lines: copper-reconstituted wild type enzyme, with putrescine as cosubstrate, in 100 mM potassium phosphate buffer, pH 7.2, 37°C


substrate_name: putrescine

smiles: C(CCN)CN

proof_lines: copper-reconstituted wild type enzyme, in 100 mM potassium phosphate buffer, pH 7.2, 37°C

substrate: putrescine


proof_lines:
pH 7.4, 37°C, enzyme from brain
pH 7.4, 37°C, enzyme from liver
monoamine oxidase B


proof_lines:
pH 7.4, 37°C, enzyme from brain
pH 7.4, 37°C, enzyme from liver


enzyme_display_name: D-aspartate oxidase

substrate_name: D-Aspartate

assay_conditions_summary: pH 8.3; 310.15 K; buffer 40 mM sodium diphosphate

proof_lines: wild type enzyme fused N-terminally with glutathione S-transferase, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)

proof_lines: His-tagged wild type enzyme, at 37°C in 40 mM sodium diphosphate buffer (pH 8.3)

enzyme: D-aspartate oxidase

substrate: D-Aspartate


substrate_name: N-Methyl-D-aspartate

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

substrate: N-Methyl-D-aspartate


organism: Mycobacterium tuberculosis

substrate_name: NAD+

assay_conditions_summary: pH 6.4; 295.15 K; cofactor NAD+

proof_lines: pH 6.4, 22°C, recombinant His6-tagged enzyme

proof_lines: pH and temperature not specified in the publication

substrate: NAD+


smiles: N


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

proof_lines: with NADH as cosubstrate, at 25°C and 100 mM HEPES, pH 7.5

proof_lines: with NAPH as cosubstrate, at 25°C and 100 mM HEPES, pH 7.5


proof_lines: Km less than 0.001 mM, at 25°C and 100 mM HEPES, pH 7.5


substrate_name: NADH


substrate_name: pyruvate

substrate: pyruvate


enzyme_display_name: formyltetrahydrofolate dehydrogenase

organism: Oryctolagus cuniculus

enzyme: formyltetrahydrofolate dehydrogenase


assay_conditions_summary: pH 7.2; 310.15 K; cofactor NADH

proof_lines:
recombinant enzyme
enzyme from brain
37°C, pH 7.2

substrate: NADH


substrate_name: NADPH

assay_conditions_summary: pH 7.2; 310.15 K; cofactor NADPH

proof_lines:
recombinant enzyme
37°C, pH 7.2


organism: Papio sp.


organism: Plasmodium falciparum

substrate_name: Unknown

proof_lines:
wild-type, pH 7.0, 25°C
wild-type, 25°C, pH 7.0
wild-type, pH 5.0, 25°C

substrate: Unknown


organism: Paenarthrobacter nicotinovorans

substrate_name: sarcosine

smiles: CNCC(=O)O

assay_conditions_summary: pH 10

proof_lines: pH 10, temperature not specified in the publication

substrate: sarcosine


organism: Pneumocystis jirovecii

proof_lines: His-tagged human-derived enzyme, pH 7.65


assay_conditions_summary: pH 7.65; cofactor NADPH

substrate: NADPH


enzyme_display_name: diaminopimelate dehydrogenase

organism: Porphyromonas gingivalis

assay_conditions_summary: pH 10.5; 298.15 K; cofactor NADP+

enzyme: diaminopimelate dehydrogenase


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


organism: Plasmodium vivax

proof_lines:
wild-type
wild-type enzyme


organism: Priestia megaterium

assay_conditions_summary: cofactor NADH


enzyme_display_name: flavin reductase (NADH)

organism: Pseudomonas putida

enzyme: flavin reductase (NADH)


substrate_name: FAD

substrate: FAD


enzyme_display_name: glutamate synthase (NADPH)

organism: Pseudomonas aeruginosa

substrate_name: L-glutamine

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

assay_conditions_summary: cofactor NADPH

enzyme: glutamate synthase (NADPH)

substrate: L-glutamine


enzyme_display_name: methylamine dehydrogenase (amicyanin)

organism: Pseudomonas sp.

smiles: C(CCCCCCN)CCCCCN

enzyme: methylamine dehydrogenase (amicyanin)


substrate_name: 12-aminododecanoic acid

smiles: C(CCCCCC(=O)O)CCCCCN

substrate: 12-aminododecanoic acid


assay_conditions_summary: pH 8; 308.15 K; cofactor NADPH

proof_lines: pH 8.0, 35°C, with substrate DELTA1-pyrroline-2-carboxylate

proof_lines: pH 8.0, 35°C, with substrate DELTA1-piperideine-2-carboxylate


assay_conditions_summary: pH 10; 308.15 K; cofactor NADP+

proof_lines: pH 10.0, 35°C, with substrate L-pipecolate


organism: Rattus norvegicus


proof_lines:
37°C
37°C, 60 min preincubation
37°C, no preincubation

substrate: hexakis(benzylammonium) decavanadate (V) dihydrate


enzyme_display_name: dihydromonapterin reductase

enzyme: dihydromonapterin reductase


assay_conditions_summary: pH 7; cofactor NADP+

proof_lines: with 10-formyl-5,8-dideazafolate as substrate

proof_lines: with 10-formyltetrahydrofolate as substrate


assay_conditions_summary: pH 7

proof_lines:
at pH 7
racemic


proof_lines:
native liver enzyme
recombinant liver enzyme
NADH-specific liver enzyme


proof_lines:
mixed inhibition
noncompetitive inhibition
competitive inhibition


substrate_name: D-Asp

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

substrate: D-Asp


enzyme_display_name: pyridoxal 5'-phosphate synthase

organism: Saccharomyces cerevisiae

substrate_name: pyridoxamine 5'-phosphate

proof_lines: enzyme species FI which is assumed to be an artefact of the purification procedure

enzyme: pyridoxal 5'-phosphate synthase

substrate: pyridoxamine 5'-phosphate


substrate_name: pyridoxine 5'-phosphate

substrate: pyridoxine 5'-phosphate


enzyme_display_name: glutamate synthase (NADH)

enzyme: glutamate synthase (NADH)


proof_lines:
with N10-formyldihydrofolate
with 7,8-dihydrofolate
with NADPH


enzyme_display_name: saccharopine dehydrogenase (NAD+, L-lysine-forming)

assay_conditions_summary: pH 7; 298.15 K; cofactor NAD+


substrate_name: saccharopine

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

enzyme: saccharopine dehydrogenase (NAD+, L-lysine-forming)

substrate: saccharopine


organism: Staphylococcus aureus


enzyme_display_name: D-amino-acid oxidase

organism: Sus scrofa

substrate_name: D-valine

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

enzyme: D-amino-acid oxidase

substrate: D-valine


substrate_name: D-serine

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

proof_lines:
wild-type
wild-type enzyme
pH 8.3, 37°C, wild-type enzyme

substrate: D-serine


enzyme_display_name: diamine oxidase

proof_lines: pH 7.9, 30°C, higher KM-value compared with N-methylputrescine or cadaverine as substrates, Vmax: 21.9 pkat

enzyme: diamine oxidase


substrate_name: N-methylputrescine

smiles: CNCCCCN

proof_lines: pH 7.9, 30°C, lowest KM-value compared with putrescine or cadaverine as substrates, Vmax: 23.3 pkat

substrate: N-methylputrescine


substrate_name: benzaldehyde

substrate: benzaldehyde


substrate_name: cadaverine

smiles: C(CCN)CCN

proof_lines: pH 7.9, 30°C, higher KM-value compared with N-putrescine or cadaverine as substrates, Vmax: 20.5 pkat

substrate: cadaverine


proof_lines:
racemic, fluorimetric assay
racemic, spectrophotometric assay
(-)-isomer


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

proof_lines:
spectrophotometric assay
fluorimetric assay

substrate: NADP+


enzyme_display_name: monoamine oxidase

substrate_name: Phenylethylamine

enzyme: monoamine oxidase

substrate: Phenylethylamine


substrate: Unknown


organism: Trypanosoma cruzi


substrate_name: NADPH

assay_conditions_summary: pH 7; 301.15 K; cofactor NADPH

substrate: NADPH


assay_conditions_summary: pH 6.7; 298.15 K; cofactor NADPH

proof_lines: cosubstrate 5,10-methylenetetrahydrofolate, pH 7.2, 25°C


assay_conditions_summary: pH 7.2; 298.15 K; cofactor NADPH

proof_lines:
cosubstrate NADPH, pH 7.2, 25°C
cosubstrate NADH, pH 7.2, 25°C
pH 7.2, 30°C


enzyme_display_name: aspartate dehydrogenase

organism: Archaeoglobus fulgidus

assay_conditions_summary: 323.15 K; cofactor NADH

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

enzyme: aspartate dehydrogenase


enzyme_display_name: glutamate dehydrogenase (NADP+)

organism: Aspergillus niger

assay_conditions_summary: pH 8; 301.15 K; cofactor NADPH

enzyme: glutamate dehydrogenase (NADP+)


proof_lines: mutant enzyme W230I/W430R, pH and temperature not specified in the publication


organism: Azospirillum brasilense

assay_conditions_summary: pH 8.5; 298.15 K; buffer Hepes, pH 8; cofactor NADPH

proof_lines: holoenzyme, buffer: Hepes, pH 8.5 or 7.5

proof_lines: dimeric enzyme, at 25°C in 50 mM HEPES/KOH buffer, pH 7.5, 1 M NaCl, in the presence of 2.5 mM 2-oxoglutarate, and 0.1 mM NADPH


substrate_name: thio-NADPH

proof_lines: in the presence of 2.5 mM 2-oxo-glutarate and 5 mM L-glutamine, the apparent maximal velocity is 54% that obtained in the presence of NADPH

proof_lines: in the presence of 2.5 mM 2-oxo-glutarate and 5 mM L-glutamine, the apparent maximal velocity is 3.7% that obtained in the presence of NADPH

proof_lines: inhibitor of the holoenzyme, competitive with NADPH

substrate: thio-NADPH


enzyme_display_name: FMN reductase (NADPH)

organism: Bacillus cereus

assay_conditions_summary: pH 7.2; 310.15 K; cofactor NADPH

enzyme: FMN reductase (NADPH)


enzyme_display_name: L-aspartate oxidase

organism: Arabidopsis thaliana

substrate_name: L-aspartate

enzyme: L-aspartate oxidase

substrate: L-aspartate


enzyme_display_name: glycine oxidase

organism: Bacillus subtilis

substrate_name: glycine

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

proof_lines: pH 8.5, 37°C, mutant enzyme T42A/C245S/L301V

enzyme: glycine oxidase

substrate: glycine


assay_conditions_summary: pH 7.5; 298.15 K; buffer 50 mM HEPES/KOH; cofactor NADPH

proof_lines: dimeric enzyme, at 25°C in 50 mM HEPES/KOH buffer, pH 7.5, 1 M NaCl, in the presence of 10 mM L-glutamine, and 0.1 mM NADPH

proof_lines: hexameric enzyme, at 25°C in 50 mM HEPES/KOH buffer, pH 7.5, 1 M NaCl, in the presence of 10 mM L-glutamine, and 0.1 mM NADPH


enzyme_display_name: primary-amine oxidase

organism: Bos taurus

substrate_name: Benzylamine; H2O; O2

enzyme: primary-amine oxidase

substrate: Benzylamine; H2O; O2


enzyme_display_name: glutamate dehydrogenase [NAD(P)+]

enzyme: glutamate dehydrogenase [NAD(P)+]


substrate_name: NAD+

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

proof_lines:
pH 8.0, 25°C, recombinant enzyme
pH 8.0, 25°C, native enzyme

substrate: NAD+


enzyme_display_name: pyrroline-5-carboxylate reductase

enzyme: pyrroline-5-carboxylate reductase


enzyme_display_name: alanine dehydrogenase

substrate_name: L-Ala

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

proof_lines:
at pH 8.6
at pH 7.4

enzyme: alanine dehydrogenase

substrate: L-Ala


substrate_name: benzylamine

substrate: benzylamine


enzyme_display_name: 6,7-dihydropteridine reductase

substrate_name: tetrahydrobiopterin

proof_lines: NADH-specific liver enzyme, cofactor NADPH

proof_lines: NADH-specific liver enzyme, cofactor NADH

proof_lines: NADPH-specific liver enzyme, cofactor NADPH

enzyme: 6,7-dihydropteridine reductase

substrate: tetrahydrobiopterin


substrate_name: kynuramine

substrate: kynuramine


enzyme_display_name: D-aspartate oxidase

substrate_name: D-glutamate

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

proof_lines:
at pH 8.3
at pH 7.4

enzyme: D-aspartate oxidase

substrate: D-glutamate


substrate_name: dihydrobiopterin

substrate: dihydrobiopterin


proof_lines: reduction of quinonoid 7,8-dihydro-6-methylpterin, NADPH-specific enzyme

proof_lines: NADPH specific liver enzyme, substrate 6-methyl-tetrahydropterin

proof_lines: reduction of quinonoid 7,8-dihydropterin, NADPH-specific enzyme


enzyme_display_name: dihydrofolate reductase

assay_conditions_summary: pH 5

enzyme: dihydrofolate reductase


organism: Candida albicans

substrate_name: Unknown


enzyme_display_name: L-amino-acid oxidase

organism: Crotalus adamanteus

enzyme: L-amino-acid oxidase


organism: Burkholderia cepacia

proof_lines:
strain PC 174
strain PC 178


organism: Corynebacterium sp. P-1

proof_lines: pH and temperature not specified in the publication


organism: Drosophila melanogaster

substrate_name: L-proline

substrate: L-proline


organism: Enterococcus faecalis

substrate_name: NADPH; Dihydrofolate; H+

assay_conditions_summary: cofactor NADPH

substrate: NADPH; Dihydrofolate; H+


organism: Cyprinus carpio

substrate_name: D-alanine

proof_lines:
apparent value, at 25°C
pH 8.0, 37°C

substrate: D-alanine


organism: Equus caballus


organism: Escherichia coli

proof_lines: wild type enzyme, at 15°C, pH not specified in the publication


substrate_name: Dihydrofolate; H+; NADH

assay_conditions_summary: pH 7.5; 295.15 K; cofactor NADH

proof_lines: pH 7.5, temperature not specified in the publication

substrate: Dihydrofolate; H+; NADH


organism: Enterococcus faecium


enzyme_display_name: dihydromonapterin reductase

enzyme: dihydromonapterin reductase


enzyme_display_name: pyridoxal 5'-phosphate synthase

smiles: O=O

enzyme: pyridoxal 5'-phosphate synthase


assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

proof_lines: chimera with Homo sapiens enzyme, pH 7, 25°C

proof_lines: chimera with Haemophilus influenzae enzyme, pH 7, 25°C


substrate_name: NADPH

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH

proof_lines: pH 7.5, temperature not specified in the publication, cosubstrate: 10-formyl-dihydrofolate


substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


enzyme_display_name: glutamate synthase (NADPH)

enzyme: glutamate synthase (NADPH)

substrate: Unknown


proof_lines: NH3-dependent glutamate synthase and apoglutamate synthase


substrate_name: pyridoxal 5'-phosphate

proof_lines: recombinant enzyme after cleavage from fusion protein

substrate: pyridoxal 5'-phosphate


substrate_name: dihydrofolate

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

substrate: dihydrofolate


organism: Glycine max

substrate: NADPH


substrate_name: L-aspartate

proof_lines:
oxygen electron acceptor
fumarate electron acceptor
at aspartate concentration 1-20 mM

substrate: L-aspartate


enzyme_display_name: leucine dehydrogenase

organism: Heyndrickxia coagulans

enzyme: leucine dehydrogenase


enzyme_display_name: monoamine oxidase

organism: Homo sapiens

substrate_name: p-tyramine

enzyme: monoamine oxidase

substrate: p-tyramine


enzyme_display_name: D-amino-acid oxidase

substrate_name: Gly

proof_lines:
pH 8.3, 25°C
pH 8.5, 25°C
at pH 7.0 and 25°C

enzyme: D-amino-acid oxidase

substrate: Gly


substrate_name: benzylamine

proof_lines:
recombinant MAO-B
pH 7.4, 30°C, oxidative half-reaction
pH 7.4, 30°C, reductive half-reaction

substrate: benzylamine


substrate_name: hexakis(benzylammonium) decavanadate (V) dihydrate


substrate_name: tyramine

substrate: tyramine


assay_conditions_summary: pH 8

proof_lines: hGDH1, pH 8.0, temperature not specified in the publication

proof_lines: hGDH2, pH 8.0, temperature not specified in the publication

proof_lines: hGDH2, pH 7.5, temperature not specified in the publication


substrate_name: D-Dopa

assay_conditions_summary: pH 8.3; 298.15 K; buffer 50 mM sodium diphosphate

proof_lines: in 50 mM sodium diphosphate buffer (pH 8.3) at 25°C

substrate: D-Dopa


proof_lines:
isoform MAO B, at pH 7.4 and 37°C
isoform MAO A, at pH 7.4 and 37°C
pH 7.0, 37°C


enzyme_display_name: formyltetrahydrofolate dehydrogenase

enzyme: formyltetrahydrofolate dehydrogenase


substrate_name: pyridoxine 5'-phosphate

proof_lines:
mutant enzyme R95C, at pH 8.0 and 37°C
pH 7.6, 37°C, mutant enzyme R95C

substrate: pyridoxine 5'-phosphate


substrate_name: quinonoid 7,8-(6H)-dihydropterin

assay_conditions_summary: pH 7.2; 293.15 K; cofactor NADH

proof_lines:
at 20°C
recombinant enzyme
at 25°C

substrate: quinonoid 7,8-(6H)-dihydropterin


substrate_name: Unknown

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


substrate_name: glycine

proof_lines: pH 7.0, 25°C, recombinant individually expressed wild-type enzyme in presence of lipoic acid

proof_lines: pH 7.0, 25°C, recombinant individually expressed wild-type enzyme in presence of lipoylated H-protein

substrate: glycine


proof_lines:
recombinant enzyme
pH 7.4, 25°C
pH 7.3, 22.6°C


enzyme_display_name: flavin reductase (NADH)

organism: Lactobacillus johnsonii

substrate_name: FMN

assay_conditions_summary: pH 7; 310.15 K; cofactor NADH

enzyme: flavin reductase (NADH)

substrate: FMN


organism: Lathyrus oleraceus

smiles: C(C#CCN)N


substrate_name: tryptamine

substrate: tryptamine


organism: Mesocricetus auratus

substrate_name: Phenylethylamine

substrate: Phenylethylamine


organism: Methylorubrum extorquens


organism: Mycobacterium sp.

proof_lines:
dimeric enzyme
tetrameric enzyme


organism: Mus musculus

proof_lines:
pH 8.3, 37°C
at pH 8.3 and 37°C


substrate_name: D-Asp

substrate: D-Asp


organism: Mycobacterium tuberculosis

proof_lines: in 25 mM potassium phosphate, pH 7.8 and 25°C


substrate: Unknown


substrate_name: L-alanine

proof_lines: pH 6.4, 22°C, recombinant His6-tagged enzyme

proof_lines: pH and temperature not specified in the publication

substrate: L-alanine


substrate_name: L-Phe

substrate: L-Phe


organism: Ophiophagus hannah

substrate_name: L-leucine

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

substrate: L-leucine


organism: Oryctolagus cuniculus

proof_lines: with excess substrate, reaction cycle in combination with C1-tetrahydrofolate synthase, lower value than for dehydrogenase alone


organism: Papio sp.


organism: Plasmodium berghei

proof_lines:
trimethoprim-sensitive strain
trimethoprim-resistant sdtrain
trimethoprim-resistant strain


organism: Pneumocystis jirovecii

proof_lines:
pH 7.4, 37°C, wild-type enzyme
wild-type enzyme, pH 7.4, 37°C


organism: Priestia megaterium


substrate_name: pyruvate

proof_lines: wild type enzyme, in 1 M NH4Cl/NH3, pH 7.4, at 25°C

substrate: pyruvate


organism: Rattus norvegicus

substrate_name: p-tyramine

substrate: p-tyramine


substrate_name: tetrahydrofolate

substrate: tetrahydrofolate


assay_conditions_summary: pH 7.5; 298.15 K; buffer 50 mM potassium phosphate assay

proof_lines: isoform MAO A, in 50 mM potassium phosphate assay buffer (pH 7.5), at 25°C


substrate_name: tetrahydrobiopterin

substrate: tetrahydrobiopterin


organism: Rhodococcus sp. (in: high G+C Gram-positive bacteria)

substrate_name: L-Lys

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

substrate: L-Lys


organism: Rhodococcus sp. AIU LAB-3


enzyme_display_name: saccharopine dehydrogenase (NAD+, L-lysine-forming)

organism: Saccharomyces cerevisiae

substrate_name: L-lysine

substrate: L-lysine


substrate_name: quinonoid dihydrobiopterin

proof_lines:
enzyme form III
enzyme form I
enzyme form II

substrate: quinonoid dihydrobiopterin


enzyme_display_name: glutamate synthase (NADH)

substrate_name: NADH

enzyme: glutamate synthase (NADH)

substrate: NADH


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

substrate: NADP+


assay_conditions_summary: cofactor FMN

substrate: FMN


substrate_name: Unknown


organism: Salmonella enterica subsp. enterica serovar Typhimurium


organism: Sus scrofa

substrate_name: cephalosporin C

substrate: cephalosporin C


proof_lines: apparent value, using D-glutamate as substrate

proof_lines: apparent value, using D-aspartate as substrate

proof_lines: apparent value, using N-methyl-D-aspartate as substrate


organism: Staphylococcus aureus

proof_lines: 30°C, pH not specified in the publication


enzyme_display_name: diamine oxidase

substrate_name: histamine

proof_lines:
free enzyme
at pH 7.4
at pH 6.3

enzyme: diamine oxidase

substrate: histamine


enzyme_display_name: primary-amine oxidase

proof_lines:
vs. O2, deduced from slope
vs. benzylamine
vs. O2, deduced from intercept

enzyme: primary-amine oxidase


substrate_name: NADP+; H2O; 10-Formyltetrahydrofolate

proof_lines: (-)-isomer (+)-isomer

substrate: NADP+; H2O; 10-Formyltetrahydrofolate


assay_conditions_summary: pH 8.3; 298.15 K; cofactor FAD

proof_lines:
at pH 8.3 and 25°C
with D-alanine


proof_lines: mutant Y228L/F242I/R283G, pH not specified in the publication, temperature not specified in the publication


substrate_name: benzylamine

assay_conditions_summary: pH 9

proof_lines: enzyme from cultured aortic smooth muscle cells, Km decreases with increasing pH

substrate: benzylamine


assay_conditions_summary: pH 7; 298.15 K; cofactor NADH

enzyme: saccharopine dehydrogenase (NAD+, L-lysine-forming)


organism: Trypanosoma cruzi

substrate: Unknown


substrate_name: D-tryptophan

proof_lines:
immobilized enzyme
free enzyme

substrate: D-tryptophan


organism: Azospirillum brasilense

proof_lines: inhibitor of the NADPH: iodonitrotetrazolium oxidoreductase reaction of wild type-beta subunit


organism: Escherichia coli

substrate_name: L-glutamine

substrate: L-glutamine


enzyme_display_name: diaminopimelate dehydrogenase

organism: Lysinibacillus sphaericus

proof_lines: competitive inhibition of L-2-amino-6-oxoheptanedioate

proof_lines: noncompetitive inhibition of meso-diaminopimelate

enzyme: diaminopimelate dehydrogenase


enzyme_display_name: glutamate dehydrogenase [NAD(P)+]

organism: Homo sapiens

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

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

assay_conditions_summary: cofactor NAD+

enzyme: glutamate dehydrogenase [NAD(P)+]

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


organism: Sulfitobacter sp.

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

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


substrate_name: NADP+; 5,10-Methylenetetrahydrofolate

substrate: NADP+; 5,10-Methylenetetrahydrofolate


enzyme_display_name: alanine dehydrogenase

organism: Thermus thermophilus

substrate_name: L-Ala

enzyme: alanine dehydrogenase

substrate: L-Ala


organism: Mesocricetus auratus

substrate_name: H2O; Serotonin; O2

substrate: H2O; Serotonin; O2


enzyme_display_name: putrescine oxidase

organism: Kocuria rosea

enzyme: putrescine oxidase


substrate_name: tyramine

substrate: tyramine


substrate_name: cadaverine

substrate: cadaverine


organism: Lens culinaris


smiles: C(CBr)N


enzyme_display_name: polyvinyl-alcohol oxidase

organism: Stenotrophomonas rhizophila

substrate_name: polyvinyl alcohol

proof_lines: pH 7.2, 30°C, presence of pyrroloquinoline quinone

proof_lines: pH 7.2, 30°C, absence of pyrroloquinoline quinone

enzyme: polyvinyl-alcohol oxidase

substrate: polyvinyl alcohol


enzyme_display_name: D-arabinono-1,4-lactone oxidase

organism: Leishmania donovani

enzyme: D-arabinono-1,4-lactone oxidase


enzyme_display_name: phloroglucinol reductase

organism: Coprococcus sp.

substrate_name: phloroglucinol

enzyme: phloroglucinol reductase

substrate: phloroglucinol


substrate_name: NADPH

substrate: NADPH


enzyme_display_name: dimethylamine dehydrogenase

organism: Hyphomicrobium sp.

substrate_name: Dimethylamine

smiles: CNC

enzyme: dimethylamine dehydrogenase

substrate: Dimethylamine


substrate_name: N,N,N,N-tetramethyl-o-phenylenediamine

substrate: N,N,N,N-tetramethyl-o-phenylenediamine


substrate_name: phenazine methosulfate

substrate: phenazine methosulfate


enzyme_display_name: sarcosine dehydrogenase

organism: Macaca mulatta

substrate_name: sarcosine

smiles: CNCC(=O)O

enzyme: sarcosine dehydrogenase

substrate: sarcosine


organism: Eubacterium oxidoreducens

substrate_name: NADP+

assay_conditions_summary: pH 7.2; cofactor NADP+

substrate: NADP+


substrate_name: dihydrophloroglucinol

substrate: dihydrophloroglucinol


enzyme_display_name: trimethylamine dehydrogenase

organism: methylotrophic bacterium

substrate_name: trimethylamine

smiles: CN(C)C

proof_lines: electron acceptor: phenazine methosulfate

enzyme: trimethylamine dehydrogenase

substrate: trimethylamine


substrate_name: ethyldimethylamine

smiles: CCN(C)C

substrate: ethyldimethylamine


smiles: CN(C)CCCl


smiles: CN(C)CCO


substrate_name: diethylmethylamine

smiles: CCN(C)CC

substrate: diethylmethylamine


smiles: CN(C)CCN


substrate_name: triethylamine

smiles: CCN(CC)CC

substrate: triethylamine


substrate_name: Diethylamine

smiles: CCNCC

substrate: Diethylamine


organism: Pseudomonas putida


substrate_name: potassium ferricyanide

substrate: potassium ferricyanide


substrate_name: N-Methylalanine

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

substrate: N-Methylalanine


substrate_name: N-methyl-L-valine

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

substrate: N-methyl-L-valine


substrate_name: N-Methyl-L-leucine

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

substrate: N-Methyl-L-leucine


enzyme_display_name: Polyvinylalcohol dehydrogenase

substrate_name: polyvinyl alcohol

smiles: C=CO

enzyme: Polyvinylalcohol dehydrogenase

substrate: polyvinyl alcohol


enzyme_display_name: proline dehydrogenase

organism: Pyrobaculum calidifontis

substrate_name: L-hydroxyproline

assay_conditions_summary: pH 8; 323.15 K; buffer 200 mM Tris-HCl

proof_lines: in 200 mM Tris-HCl buffer (pH 8.0), at 50°C

enzyme: proline dehydrogenase

substrate: L-hydroxyproline


substrate_name: L-proline

substrate: L-proline


proof_lines: with L-hydroxyproline as cosubstrate, in 200 mM Tris-HCl buffer (pH 8.0), at 50°C

proof_lines: with L-proline as cosubstrate, in 200 mM Tris-HCl buffer (pH 8.0), at 50°C


organism: Clostridium formicaceticum

substrate_name: benzyl viologen

substrate: benzyl viologen


organism: Neomoorella thermoacetica

proof_lines: pH 7.5, 45°C, recombinant enzyme, with 5-methyltetrahydrofolate


proof_lines: pH 7.5, 45°C, recombinant enzyme, with benzyl viologen


enzyme_display_name: dimethylglycine dehydrogenase

organism: Chromohalobacter israelensis

enzyme: dimethylglycine dehydrogenase


substrate_name: N,N-dimethylglycine

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

substrate: N,N-dimethylglycine


organism: Pyrococcus furiosus

proof_lines: PF1246 (alpha4beta4-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C

proof_lines: PF1798 (alphabetagammadelta-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C


organism: Thermococcus kodakarensis

proof_lines: TK0117 (alpha4beta4-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C

proof_lines: TK0122 (alphabetagammadelta-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C


organism: Pyrococcus horikoshii

proof_lines: pH and temperature not specified in the publication

proof_lines: PF1364 (alpha4beta4-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C

proof_lines: PH1751 (alphabetagammadelta-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C


organism: Thermococcus profundus

proof_lines: TPpdhB2 (alpha4beta4-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C

proof_lines: TPpdhB (alphabetagammadelta-type beta subunit of L-proline dehydrogenase) in 200 mM Tris-HCl (pH 8.0), at 50°C