Crystal Structure of O-actetyl Homoserine Sulfhydrylase From Thermus Thermophilus HB8,OAH2.Crystal Structure of O-actetyl Homoserine Sulfhydrylase From Thermus Thermophilus HB8,OAH2.
Structural highlights
2cb1 is a 1 chain structure with sequence from Thermus thermophilus HB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
METY2_THET8 Catalyzes the conversion of O-acetyl-L-homoserine (OAH) into homocysteine in the methionine biosynthesis pathway. Has weak activity with O-acetyl-L-serine, O-phospho-L-serine, L-serine, O-succinyl-L-homoserine and L-homoserine. Shows a very low CTT gamma-synthase activity.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
References
↑Iwama T, Hosokawa H, Lin W, Shimizu H, Kawai K, Yamagata S. Comparative characterization of the oah2 gene homologous to the oah1 of Thermus thermophilus HB8. Biosci Biotechnol Biochem. 2004 Jun;68(6):1357-61. PMID:15215603 doi:10.1271/bbb.68.1357
