N-methyl-L-amino-acid oxidase
| N-methyl-L-amino-acid oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.5.3.2 | ||||||||
| CAS no. | 9029-23-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
N-methyl-L-amino-acid oxidase (EC 1.5.3.2) is an enzyme that catalyzes the general chemical reaction
- an N-methyl-L-amino acid + H2O + O2 an L-amino acid + formaldehyde + H2O2
Not all amino acids are equally effective as substrates but N-methyltryptophan (L-abrine) is an example which gives a rapid and nearly complete reaction in vitro.[1]
The enzyme is a flavoprotein that uses flavin adenine dinucleotide as its cofactor. It requires oxygen, which is converted to hydrogen peroxide, while the methyl group becomes formaldehyde.[2]
Nomenclature
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH group of donors with oxygen as acceptor. The systematic name of this enzyme class is N-methyl-L-amino-acid:oxygen oxidoreductase (demethylating). Other names in common use include N-methylamino acid oxidase, and demethylase.
References
- ^ Moritani M, Tung TC, Fujii S, Mito H, Izumiya N, Kenmochi K, Hirohata R (August 1954). "Specificity of rabbit kidney demethylase". The Journal of Biological Chemistry. 209 (2): 485–92. doi:10.1016/S0021-9258(18)65475-4. PMID 13192101.
- ^ Enzyme 1.5.3.2 at KEGG Pathway Database.