Structural highlights
Function
[SRR_SCHPO] Catalyzes the synthesis of D-serine from L-serine. Has dehydratase activity towards both L-serine and D-serine.[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
Serine racemase synthesizes d-serine, a physiological agonist of the NMDA receptor in mammalian brains. Schizosaccharomyces pombe produces serine racemase (spSR) that is highly similar to the brain enzyme. Our mass-spectrometric and X-ray studies revealed that spSR is modified with its natural substrate serine. spSR remains partially active even though its essential Lys57 inherently forming a Schiff base with the coenzyme pyridoxal 5'-phosphate is converted to N(6)-(R-2-amino-2-carboxyethyl)-l-lysyl (lysino-d-alanyl) residue. This indicates that the alpha-amino group of the d-alanyl moiety of the lysino-d-alanyl residue serves as a catalytic base in the same manner as the epsilon-amino group of Lys57 of the original spSR.
Serine racemase with catalytically active lysinoalanyl residue.,Yamauchi T, Goto M, Wu HY, Uo T, Yoshimura T, Mihara H, Kurihara T, Miyahara I, Hirotsu K, Esaki N J Biochem. 2009 Apr;145(4):421-4. Epub 2009 Jan 20. PMID:19155267[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Goto M, Yamauchi T, Kamiya N, Miyahara I, Yoshimura T, Mihara H, Kurihara T, Hirotsu K, Esaki N. Crystal structure of a homolog of mammalian serine racemase from Schizosaccharomyces pombe. J Biol Chem. 2009 Sep 18;284(38):25944-52. Epub 2009 Jul 28. PMID:19640845 doi:10.1074/jbc.M109.010470
- ↑ Yamauchi T, Goto M, Wu HY, Uo T, Yoshimura T, Mihara H, Kurihara T, Miyahara I, Hirotsu K, Esaki N. Serine racemase with catalytically active lysinoalanyl residue. J Biochem. 2009 Apr;145(4):421-4. Epub 2009 Jan 20. PMID:19155267 doi:10.1093/jb/mvp010
