Alanine Racemase

AKA: L-Alanine Racemase.
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Example(s):
- Enterococcus Gallinarum http://www.uniprot.org/uniprot/Q9X3P3
- PMID 10209740: “Sequence determination of a region downstream from the vanXYc gene in Enterococcus gallinarum BM4174 revealed an open reading frame, designated vanT, that encodes a 698-amino-acid polypeptide with an amino-terminal domain containing 10 predicted transmembrane segments . The protein contained a highly conserved pyridoxal phosphate attachment site in the C-terminal domain, typical of alanine racemases. The protein was overexpressed in Escherichia coli, and serine racemase activity was detected in the membrane but not in the cytoplasmic fraction after centrifugation of sonicated cells, whereas alanine racemase activity was located almost exclusively in the cytoplasm .”
See: Enterococcus Gallinarum.

References

(Wikipedia, 2009) ⇒ http://en.wikipedia.org/wiki/Alanine_racemase
- In enzymology, an alanine racemase (EC 5.1.1.1) is an enzyme that catalyzes the chemical reaction
  - L-alanine \rightleftharpoons D-alanine
- Hence, this enzyme has one substrate, L-alanine, and one product, D-alanine.
  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 alanine racemase. This enzyme is also called L-alanine racemase. This enzyme participates in alanine and aspartate metabolism and D-alanine metabolism. It employs one cofactor, pyridoxal phosphate. At least one compound, 3-Fluoro-D-alanine is known to inhibit this enzyme.