L-amino-acid oxidase
| L-amino-acid oxidase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.4.3.2 | ||||||||
| CAS number | 9000-89-9 | ||||||||
| 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 / EGO | ||||||||
| |||||||||
In enzymology, a L-amino-acid oxidase (EC 1.4.3.2) is an enzyme that catalyzes the chemical reaction
- an L-amino acid + H2O + O2
a 2-oxo acid + NH4 + H2O2
The 3 substrates of this enzyme are L-amino acid, H2O, and O2, whereas its 3 products are the corresponding α-keto acid (2-oxo acid), NH4, and H2O2. For example, the enzyme will convert L-alanine into pyruvic acid (2-oxopropanoic acid).
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is L-amino-acid:oxygen oxidoreductase (deaminating). This enzyme is also called ophio-amino-acid oxidase. This enzyme participates in 8 metabolic pathways: alanine and aspartate metabolism, methionine metabolism, valine, leucine and isoleucine degradation, tyrosine metabolism, phenylalanine metabolism, tryptophan metabolism, phenylalanine, tyrosine and tryptophan biosynthesis, and alkaloid biosynthesis. It employs one cofactor, FAD.
Structural studies
As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes 1F8R, 1F8S, 1REO, 1TDK, 1TDN, 1TDO, 2IID, 2JAE, 2JB1, 2JB2, and 2JB3.
References
- Boyer, P. D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 7, Academic Press, New York, 1963, p. 609–648.
- Wellner D. and Meister A. (1960). "Crystalline L-amino acid oxidase of Crotalus adamanteus". J. Biol. Chem. 235: 2013–2018. PMID 13843884.