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B6db references: 20260390

type Journal Article
authors Tai, C. H.; Cook, P. F.
title O-acetylserine sulfhydrylase
journal Adv Enzymol Relat Areas Mol Biol
ui 20260390
year (2000)
volume 74
pages 185-234
abstract 0-Acetylserine sulfhydrylase (OASS) is a pyridoxal 5'-dependent enzyme that synthesizes L-cysteine in enteric bacteria, such as Salmonella typhimurium and Escherichia coli, and plants. OASS is a member of the beta-family of PLP-dependent enzymes that specifically catalyze beta-replacement reactions. Enzymes in this class include the beta-subunit of tryptophan synthase (beta-TRPS), cystathionine beta-synthase, beta-cyanoalanine synthase, and cysteine lyase. Other than OASS, only beta-TRPS has been extensively studied, and thus mechanistic comparisons will be limited to it. This review focuses on the structure that has been solved recently, kinetic and acid-base chemical mechanisms, and spectroscopic studies using P-31 NMR, UV-visible, rapid-scanning stopped-flow phosphorescence, static and time-resolved fluorescence techniques. In addition, kinetic isotope effects and stereochemistry of the OASS reaction are discussed.
last changed 2004/05/12 09:15

B6db references