Structural highlights
Function
[LYSR_OENOB] Catalyzes the interconversion of D-lysine and L-lysine. Can also use arginine and ornithine, but not alanine.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The crystal structure of alanine racemase from Oenococcus oeni has been determined at 1.7 A resolution using the single-wavelength anomalous dispersion (SAD) method and selenium-labelled protein. The protein exists as a symmetric dimer in the crystal, with both protomers contributing to the two active sites. Pyridoxal 5'-phosphate, a cofactor, is bound to each monomer and forms a Schiff base with Lys39. Structural comparison of alanine racemase from O. oeni (Alr) with homologous family members revealed similar domain organization and cofactor binding.
Structure of alanine racemase from Oenococcus oeni with bound pyridoxal 5'-phosphate.,Palani K, Burley SK, Swaminathan S Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jan 1;69(Pt 1):15-9. doi: , 10.1107/S1744309112047276. Epub 2012 Dec 25. PMID:23295479[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kato S, Hemmi H, Yoshimura T. Lysine racemase from a lactic acid bacterium, Oenococcus oeni: structural basis of substrate specificity. J Biochem. 2012 Dec;152(6):505-8. doi: 10.1093/jb/mvs120. Epub 2012 Oct 3. PMID:23035128 doi:http://dx.doi.org/10.1093/jb/mvs120
- ↑ Palani K, Burley SK, Swaminathan S. Structure of alanine racemase from Oenococcus oeni with bound pyridoxal 5'-phosphate. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2013 Jan 1;69(Pt 1):15-9. doi: , 10.1107/S1744309112047276. Epub 2012 Dec 25. PMID:23295479 doi:http://dx.doi.org/10.1107/S1744309112047276
