Amino-acid racemase
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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.
Contents |
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
- IUBMB entry for 5.1.1.10
- BRENDA references for 5.1.1.10 (Recommended.)
- PubMed references for 5.1.1.10
- PubMed Central references for 5.1.1.10
- Google Scholar references for 5.1.1.10
- Soda K, Osumi T (1969). "Crystalline amino acid racemase with low substrate specificity". Biochem. Biophys. Res. Commun. 35: 363–8. PMID 5788493.
External links
- The CAS registry number for this enzyme class is 9068-61-5.
Gene Ontology (GO) codes
Acknowledgement and Attribution Regarding Sources of Content
Some of the initial content on this page may be incorporated in part from copyleft sources in the public domain including wikis such as Wikipedia and AskDrWiki. Drug information for patients came from the The National Library of Medicine. Infectious disease information may have come from the Centers for Disease Control (CDC). Differential Diagnoses are drawn from clinicians as well as an amalgamation of 3 sources: 1.The Disease Database; 2. Kahan, Scott, Smith, Ellen G. In A Page: Signs and Symptoms. Malden, Massachusetts: Blackwell Publishing, 2004:3; 3. Sailer, Christian, Wasner, Susanne. Differential Diagnosis Pocket. Hermosa Beach, CA: Borm Bruckmeir Publishing LLC, 2002:7 .

