| amino-acid racemase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 5.1.1.10 | ||||||||
| CAS no. | 9068-61-5 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, an amino-acid racemase (EC 5.1.1.10) is an enzyme that catalyzes the chemical reaction
- an L-amino acid a D-amino acid
Hence, this enzyme has one substrate, L-amino acid, and one product, D-amino acid.
This enzyme belongs to the family of isomerases, specifically those racemases and epimerases acting on amino acids and derivatives. The systematic name of this enzyme class is amino-acid racemase. This enzyme is also called L-amino acid racemase. This enzyme participates in 4 metabolic pathways: glycine, serine and threonine metabolism, cysteine metabolism, D-glutamine and D-glutamate metabolism, and D-arginine and D-ornithine metabolism. It employs one cofactor, pyridoxal phosphate.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 2FKP, 2GGG, 2GGH, 2GGI, and 2GGJ.
References
- Soda K, Osumi T (1969). "Crystalline amino acid racemase with low substrate specificity". Biochem. Biophys. Res. Commun. 35 (3): 363–8. doi:10.1016/0006-291X(69)90507-5. PMID 5788493.
This page was last edited on 26 August 2023, at 13:08