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Literature summary extracted from

  • Binda, C.; Wang, J.; Li, M.; Hubalek, F.; Mattevi, A.; Edmondson, D.E.
    Structural and mechanistic studies of arylalkylhydrazine inhibition of human monoamine oxidases A and B (2008), Biochemistry, 47, 5616-5625.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.3.4 benzylhydrazine the mode of irreversible MAO inhibition involves covalent modification of the flavin coenzyme, overview; the three-dimensional structures of phenylethylhydrazine- and benzylhydrazine-inhibited MAO B show that alkylation occurs at the N5 position on the re-face of the covalent flavin with loss of the hydrazyl nitrogens, mechanism, the mode of irreversible MAO inhibition involves covalent modification of the flavin coenzyme, overview Homo sapiens
1.4.3.4 Phenylethylhydrazine the mode of irreversible MAO inhibition involves covalent modification of the flavin coenzyme, overview; the three-dimensional structures of phenylethylhydrazine- and benzylhydrazine-inhibited MAO B show that alkylation occurs at the N5 position on the re-face of the covalent flavin with loss of the hydrazyl nitrogens, mechanism, the mode of irreversible MAO inhibition involves covalent modification of the flavin coenzyme, overview Homo sapiens
1.4.3.4 phenylhydrazine weak binding; weak binding Homo sapiens

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.3.4 additional information
-
 additional information steady-state kinetic studies, overview Homo sapiens

Organism

EC Number Organism UniProt Comment Textmining
1.4.3.4 Homo sapiens
-
 isozyme MAO A
-
1.4.3.4 Homo sapiens P27338 MAO-B; isozyme MAO B
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.4.3.4 flavoprotein
-
 Homo sapiens

Synonyms

EC Number Synonyms Comment Organism
1.4.3.4 MAO A
-
 Homo sapiens
1.4.3.4 MAO B
-
 Homo sapiens
1.4.3.4 monoamine oxidase A
-
 Homo sapiens
1.4.3.4 monoamine oxidase B
-
 Homo sapiens

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.3.4 7.5
-
 assay at Homo sapiens

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.3.4 flavin
-
 Homo sapiens

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.4.3.4 0.015
-
 Phenylethylhydrazine pH 7.5, MAO-B, determined from competitive inhibition data of substrate oxidation at 25°C Homo sapiens
1.4.3.4 0.026
-
 benzylhydrazine pH 7.5, MAO-B, determined from competitive inhibition data of substrate oxidation at 25°C Homo sapiens
1.4.3.4 0.047
-
 Phenylethylhydrazine pH 7.5, MAO-A, determined from competitive inhibition data of substrate oxidation at 25°C Homo sapiens
1.4.3.4 0.048
-
 benzylhydrazine pH 7.5, MAO-B, determined from Kitz-Wilson plots of the hydrazine concentration dependence on rates in enzyme inhibition at 15°C Homo sapiens
1.4.3.4 0.05
-
 Phenylethylhydrazine pH 7.5, MAO-A, determined from Kitz-Wilson plots of the hydrazine concentration dependence on rates in enzyme inhibition at 15°C Homo sapiens
1.4.3.4 0.128
-
 Phenylethylhydrazine pH 7.5, MAO-B, determined from Kitz-Wilson plots of the hydrazine concentration dependence on rates in enzyme inhibition at 15°C Homo sapiens
1.4.3.4 0.205
-
 phenylhydrazine pH 7.5, MAO-A, determined from competitive inhibition data of substrate oxidation at 25°C Homo sapiens
1.4.3.4 0.523
-
 phenylhydrazine pH 7.5, MAO-A, determined from Kitz-Wilson plots of the hydrazine concentration dependence on rates in enzyme inhibition at 15°C Homo sapiens
1.4.3.4 0.791
-
 phenylhydrazine pH 7.5, MAO-B, determined from Kitz-Wilson plots of the hydrazine concentration dependence on rates in enzyme inhibition at 15°C Homo sapiens
1.4.3.4 1.95
-
 benzylhydrazine pH 7.5, MAO-A, determined from Kitz-Wilson plots of the hydrazine concentration dependence on rates in enzyme inhibition at 15°C Homo sapiens
1.4.3.4 2.096
-
 benzylhydrazine pH 7.5, MAO-A, determined from competitive inhibition data of substrate oxidation at 25°C Homo sapiens