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Literature summary for 1.4.3.4 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
Search for more literature for 1.4.3.4

Inhibitors

Inhibitors Comment Organism Structure
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
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
phenylhydrazine weak binding; weak binding Homo sapiens

KM Value [mM]

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

Organism

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

Posttranslational Modification

Posttranslational Modification Comment Organism
flavoprotein
-
 Homo sapiens

Synonyms

Synonyms Comment Organism
MAO A
-
 Homo sapiens
MAO B
-
 Homo sapiens
monoamine oxidase A
-
 Homo sapiens
monoamine oxidase B
-
 Homo sapiens

pH Optimum

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

Cofactor

Cofactor Comment Organism Structure
flavin
-
 Homo sapiens

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.015
-
 Phenylethylhydrazine pH 7.5, MAO-B, determined from competitive inhibition data of substrate oxidation at 25°C Homo sapiens
0.026
-
 benzylhydrazine pH 7.5, MAO-B, determined from competitive inhibition data of substrate oxidation at 25°C Homo sapiens
0.047
-
 Phenylethylhydrazine pH 7.5, MAO-A, determined from competitive inhibition data of substrate oxidation at 25°C Homo sapiens
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
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
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
0.205
-
 phenylhydrazine pH 7.5, MAO-A, determined from competitive inhibition data of substrate oxidation at 25°C Homo sapiens
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
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
1.95
-
 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
2.096
-
 benzylhydrazine pH 7.5, MAO-A, determined from competitive inhibition data of substrate oxidation at 25°C Homo sapiens