90839-57-9Relevant academic research and scientific papers
Steric Course of Ketopantoate Hydroxymethyltransferase in E. coli
Aberhart, D. John,Russell, David J.
, p. 4902 - 4906 (2007/10/02)
The conversion of α-ketoisovaleric acid (α-KIVA) to ketopantoate by the 5,10-methylenetetrahydrofolate-dependent enzyme ketopantoate hydroxymethyltransferase (KHMT) in E. coli has been shown to proceed in a retention mode at the β-position of α-KIVA. 5,10-methylenetetrahydrofolate formed in vivo by serine hydroxymethyltransferase (SHMT) from stereospecifically deuterated (3S-d1) serine was converted by KHMT into an ca. 3:1 ratio of deuterated ketopantoates with the 4S isomer predominating.The results indicate that KHMT and SHMT have the same overall steric course in E. coli.
