Any feedback?
Literature summary for 1.4.3.4 extracted from
- Purification and properties of pig liver mitochondrial monoamine oxidase (1971), Arch. Biochem. Biophys., 146, 410-412.
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Km of membrane-bound and Triton X-100-solubilized enzyme | Sus scrofa |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| mitochondrion | - |
Sus scrofa | 5739 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Cu2+ | negligible amounts in the purified enzym | Sus scrofa |  |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 115000 | - |
gel filtration, lowest molecular weight determined, variations due to different states of aggregation | Sus scrofa |
Organic Solvent Stability
| Organic Solvent | Comment | Organism |
|---|---|---|
| additional information | when enzyme liberated by methyl ethyl ketone extraction Km about 3times lower than that for enzyme bound to the mitochondria or solubilzed by Triton X-100 | Sus scrofa |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Sus scrofa | - |
- |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| additional information | enzyme is bound to the mitochondria by acidic phospholipids, soluble enzyme can form complexes with such phospholipids | Sus scrofa |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Sus scrofa |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| liver | - |
Sus scrofa | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
- |
Sus scrofa |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| benzylamine + H2O + O2 | - |
Sus scrofa | benzaldehyde + NH3 + H2O2 | - |
? | |
| kynuramine + H2O + O2 | - |
Sus scrofa | 3-(2-aminophenyl)-3-oxopropanal + NH3 + H2O2 | - |
? | |
| RCH2NH2 + H2O + O2 | no activity with spermidine | Sus scrofa | RCHO + NH3 + H2O2 | - |
? | |
| RCH2NH2 + H2O + O2 | no activity with histamine | Sus scrofa | RCHO + NH3 + H2O2 | - |
? | |
| RCH2NH2 + H2O + O2 | no activity with spermine | Sus scrofa | RCHO + NH3 + H2O2 | - |
? | |
| RCH2NH2 + H2O + O2 | phenylethylhydrazine | Sus scrofa | RCHO + NH3 + H2O2 | - |
? | |
| RCH2NH2 + H2O + O2 | isoamylamine | Sus scrofa | RCHO + NH3 + H2O2 | - |
? | |
| RCH2NH2 + H2O + O2 | 3-hydroxytyramine | Sus scrofa | RCHO + NH3 + H2O2 | - |
? | |
| RCH2NH2 + H2O + O2 | amylamine | Sus scrofa | RCHO + NH3 + H2O2 | - |
? | |
| serotonin + H2O + O2 | - |
Sus scrofa | (5-hydroxy-1H-indol-3-yl)acetaldehyde + NH3 + H2O2 | - |
? | |
| tryptamine + H2O + O2 | - |
Sus scrofa | 1H-indol-3-yl-acetaldehyde + NH3 + H2O2 | - |
? | |
| tyramine + H2O + O2 | - |
Sus scrofa | (4-hydroxyphenyl)acetaldehyde + NH3 + H2O2 | - |
? | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 8.7 | - |
tyramine as substrate | Sus scrofa |
| 9.2 | - |
benzylamine as substrate | Sus scrofa |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 7 | 11 | about 50% of activity maximum at pH 7 and 11 | Sus scrofa |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| flavin | flavoprotein | Sus scrofa | |
| flavin | 1 mol FAD per 115000 g of protein | Sus scrofa | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
