Aspartate racemase
In enzymology, an aspartate racemase (EC 5.1.1.13) is an enzyme that catalyzes the chemical reaction
- L-aspartate D-aspartate
| aspartate racemase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 5.1.1.13 | ||||||||
| CAS number | 37237-56-2 | ||||||||
| 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 | ||||||||
| |||||||||
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.
Structural studies
As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1IU9, 1JFL, and 2DX7.
References
- Lamont HC, Staudenbauer WL, Strominger JL (1972). "Partial purification and characterization of an aspartate racemase from Streptococcus faecalis". J. Biol. Chem. 247 (16): 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 (26): 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 (2): 479–89. doi:10.1016/S0022-2836(02)00296-6. PMID 12051922.
- Sielaff H, Dittmann E, Tandeau de Marsac N, Bouchier C, Von Döhren H, Börner T, Schwecke T (2003). "The mcyF gene of the microcystin biosynthetic gene cluster from Microcystis aeruginosa encodes an aspartate racemase". Biochem. J. 373 (Pt 3): 909–16. doi:10.1042/BJ20030396. PMC 1223527. 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 (23–24): 4798–803. doi:10.1111/j.1432-1033.2004.04445.x. PMID 15606767.
This article is issued from Wikipedia. The text is licensed under Creative Commons - Attribution - Sharealike. Additional terms may apply for the media files.