Aspartate racemase

From Wikipedia, the free encyclopedia

In enzymology, an aspartate racemase (EC 5.1.1.13) is an enzyme that catalyzes the chemical reaction

L-aspartate $\rightleftharpoons$ D-aspartate

Hence, this enzyme has one substrate, L-aspartate, and one product, D-aspartate.

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 aspartate racemase. Other names in common use include D-aspartate racemase, and McyF. This enzyme participates in alanine and aspartate metabolism.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1IU9, 1JFL, and 2DX7.

[edit] References

IUBMB entry for 5.1.1.13
BRENDA references for 5.1.1.13 (Recommended.)
PubMed references for 5.1.1.13
PubMed Central references for 5.1.1.13
Google Scholar references for 5.1.1.13
Lamont HC, Staudenbauer WL, Strominger JL (1972). "Partial purification and characterization of an aspartate racemase from Streptococcus faecalis". J. Biol. Chem. 247: 5103–6. PMID 4626916.
Yamauchi T, Choi SY, Okada H, Yohda M, Kumagai H, Esaki N, Soda K (1992). "Properties of aspartate racemase, a pyridoxal 5'-phosphate-independent amino acid racemase". J. Biol. Chem. 267: 18361–4. PMID 1526977.
Liu L, Iwata K, Kita A, Kawarabayasi Y, Yohda M, Miki K (2002). "Crystal structure of aspartate racemase from Pyrococcus horikoshii OT3 and its implications for molecular mechanism of PLP-independent racemization". J. Mol. Biol. 319: 479–89. doi:10.1016/S0022-2836(02)00296-6. PMID 12051922.
H, Borner T, Schwecke T (2003). "The mcyF gene of the microcystin biosynthetic gene cluster from Microcystis aeruginosa encodes an aspartate racemase". Biochem. J. 373: 909–16. doi:10.1042/BJ20030396. PMID 12713441.
Yamashita T, Ashiuchi M, Ohnishi K, Kato S, Nagata S, Misono H (2004). "Molecular identification of monomeric aspartate racemase from Bifidobacterium bifidum". Eur. J. Biochem. 271: 4798–803. doi:10.1111/j.1432-1033.2004.04445.x. PMID 15606767.