The Enzyme Database

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Accepted name: aspartate racemase
Reaction: L-aspartate = D-aspartate
Other name(s): D-aspartate racemase; McyF
Systematic name: aspartate racemase
Comments: Also acts, at half the rate, on L-alanine.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number: 37237-56-2
1.  Lamont, H.C., Staudenbauer, W.L. and Strominger, J.L. Partial purification and characterization of an aspartate racemase from Streptococcus faecalis. J. Biol. Chem. 247 (1972) 5103–5106. [PMID: 4626916]
2.  Yamauchi, T., Choi, S.Y., Okada, H., Yohda, M., Kumagai, H., Esaki, N. and Soda, K. Properties of aspartate racemase, a pyridoxal 5′-phosphate-independent amino acid racemase. J. Biol. Chem. 267 (1992) 18361–18364. [PMID: 1526977]
3.  Liu, L., Iwata, K., Kita, A., Kawarabayasi, Y., Yohda, M. and Miki, K. Crystal structure of aspartate racemase from Pyrococcus horikoshii OT3 and its implications for molecular mechanism of PLP-independent racemization. J. Mol. Biol. 319 (2002) 479–489. [PMID: 12051922]
4.  Sielaff, H., Dittmann, E., Tandeau De Marsac, N., Bouchier, C., von Döhren, H., Börner, T. and Schwecke, T. The mcyF gene of the microcystin biosynthetic gene cluster from Microcystis aeruginosa encodes an aspartate racemase. Biochem. J. 373 (2003) 909–916. [PMID: 12713441]
5.  Yamashita, T., Ashiuchi, M., Ohnishi, K., Kato, S., Nagata, S. and Misono, H. Molecular identification of monomeric aspartate racemase from Bifidobacterium bifidum. Eur. J. Biochem. 271 (2004) 4798–4803. [PMID: 15606767]
[EC created 1976]

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