Serine hydroxymethyltransferase: role of the active site lysine in the mechanism of the enzyme.

作者: Douglas Schirch , Sonia Delle Fratte , Sandra Iurescia , Sebastiana Angelaccio , Roberto Contestabile

DOI: 10.1007/978-1-4615-2960-6_148

关键词:

摘要: Serine hydroxymethyltransferase (SHMT) is a pyridoxal phosphate requiring enzyme which catalyzes the reaction shown in Equation 1. This uses both monoglutamate and polyglutamate forms of tetrahydrofolate (H4PteGlun) 5,10-methylenetetrahydrofolate (5,10-CH2-H4PteGlun). In eucaryotic organisms there are cytosolic mitochondrial isoenzymes. The role isoenzyme to provide 5,10-CH2-H4PteGlun for biosynthesis thymidylate, purines, methionine.1

参考文章(7)
M.D. Toney, J.F. Kirsch, The K258R mutant of aspartate aminotransferase stabilizes the quinonoid intermediate. Journal of Biological Chemistry. ,vol. 266, pp. 23900- 23903 ,(1991) , 10.1016/S0021-9258(18)54368-4
V Schirch, S Hopkins, E Villar, S Angelaccio, Serine hydroxymethyltransferase from Escherichia coli: purification and properties. Journal of Bacteriology. ,vol. 163, pp. 1- 7 ,(1985) , 10.1128/JB.163.1.1-7.1985
Tohru Yoshimura, Mohit B. Bhatia, James M. Manning, Dagmar Ringe, Kenji Soda, Partial reactions of bacterial D-amino acid transaminase with asparagine substituted for the lysine that binds coenzyme pyridoxal 5'-phosphate. Biochemistry. ,vol. 31, pp. 11748- 11754 ,(1992) , 10.1021/BI00162A011
Douglas L. Smith, Steven C. Almo, Michael D. Toney, Dagmar Ringe, 2.8-A-resolution crystal structure of an active-site mutant of aspartate aminotransferase from Escherichia coli. Biochemistry. ,vol. 28, pp. 8161- 8167 ,(1989) , 10.1021/BI00446A030