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 Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | steady-state kinetic studies, overview | Homo sapiens |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
isozyme MAO A | - |
Homo sapiens | P27338 | MAO-B; isozyme MAO B | - |
Posttranslational Modification | Comment | Organism |
---|---|---|
flavoprotein | - |
Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
MAO A | - |
Homo sapiens |
MAO B | - |
Homo sapiens |
monoamine oxidase A | - |
Homo sapiens |
monoamine oxidase B | - |
Homo sapiens |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Homo sapiens |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
flavin | - |
Homo sapiens |
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 |