CRYSTAL STRUCTURE OF A PUTATIVE SERINE HYDROLASE (YDR428C) FROM SACCHAROMYCES CEREVISIAE AT 1.85 A RESOLUTIONCRYSTAL STRUCTURE OF A PUTATIVE SERINE HYDROLASE (YDR428C) FROM SACCHAROMYCES CEREVISIAE AT 1.85 A RESOLUTION
Structural highlights
1vkh is a 2 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
[KFA_YEAST] Catalyzes the hydrolysis of N-formyl-L-kynurenine to L-kynurenine, the second step in the kynurenine pathway of tryptophan degradation. Kynurenine may be further oxidized to nicotinic acid, NAD(H) and NADP(H). Required for elimination of toxic metabolites.[HAMAP-Rule:MF_03014][1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
↑Wogulis M, Chew ER, Donohoue PD, Wilson DK. Identification of Formyl Kynurenine Formamidase and Kynurenine Aminotransferase from Saccharomyces cerevisiae Using Crystallographic, Bioinformatic and Biochemical Evidence. Biochemistry. 2008 Feb 12;47(6):1608-21. Epub 2008 Jan 19. PMID:18205391 doi:10.1021/bi701172v
