In enzymology, a N-methyl-L-amino-acid oxidase (EC 1.5.3.2) is an enzyme that catalyzes the chemical reaction
N-methyl-L-amino-acid oxidase | |||||||||
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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 | ||||||||
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- an N-methyl-L-amino acid + H2O + O2 an L-amino acid + formaldehyde + H2O2
The 3 substrates of this enzyme are N-methyl-L-amino acid, H2O, and O2, whereas its 3 products are L-amino acid, formaldehyde, and H2O2.
It has 2 cofactors: FAD, and Flavoprotein.
Nomenclature
editThis 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
editFurther reading
edit- Moritani M (1952). "Demethylase. IV. Kinetics and reaction mechanism". Hukuoka Acta Med. 43: 651–658.
- Moritani M (1952). "Demethylase. V. Specificity and its relation to amino acid oxidase". Hukuoka Acta Med. 43: 731–735.
- 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. PMID 13192101.