Journal of the American Chemical Society p. 4902 - 4906 (1984)
Update date:2022-09-26
Topics: Steric hindrance Enzyme Kinetics Experimental Design coli Binding site Cofactor
Aberhart, D. John
Russell, David J.
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.
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