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B6db references: 21110263

type Journal Article
authors Tai, C. H.; Cook, P. F.
title Pyridoxal 5'-phosphate-dependent alpha,beta-elimination reactions: mechanism of O-acetylserine sulfhydrylase
journal Acc Chem Res
ui 21110263
year (2001)
volume 34
number 1
pages 49-59.
keywords Cysteine Synthase/*metabolism
abstract O-Acetylserine sulfhydrylase catalyzes the replacement of the beta- acetoxy group of O-acetyl-L-serine with sulfide to generate L-cysteine. The reaction represents the final step in the biosynthesis of L- cysteine in enteric bacteria and plants. A quinonoid intermediate has not been detected using a variety of kinetic and spectroscopic probes for the wild-type or mutant enzymes, ruling out an E1 mechanism. The structure of the external Schiff base intermediate indicates an anti elimination. O-Acetylserine sulfhydrylase is the only known pyridoxal 5'-phosphate-dependent enzyme that catalyzes a beta-elimination reaction to have an anti E2 mechanism.
last changed 2003/03/17 14:53

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