NDLI: Structure and mechanism of O-acetylserine sulfhydrylase.

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Structure and mechanism of O-acetylserine sulfhydrylase.

Content Provider	Semantic Scholar
Author	Rabeh, Wael M. Cook, Paul F.
Copyright Year	2004
Abstract	The O-acetylserine sulfhydrylase (OASS) from Salmonella typhimurium catalyzes a beta-replacement reaction in which the beta-acetoxy group of O-acetyl-L-serine (OAS) is replaced by bisulfide to give L-cysteine and acetate. The kinetic mechanism of OASS is ping-pong with a stable alpha-aminoacrylate intermediate. The enzyme is a homodimer with one pyridoxal 5'-phosphate (PLP) bound per subunit deep within the protein in a cleft between the N- and C-terminal domains of each of the monomers. All of the active site residues are contributed by a single subunit. The enzyme cycles through open and closed conformations as it catalyzes its reaction with structural changes largely limited to a subdomain of the N-terminal domain. The elimination of acetic acid from OAS is thought to proceed via an anti-E2 mechanism, and the only catalytic group identified to date is lysine 41, which originally participates in Schiff base linkage to PLP. The transition state for the elimination of acetic acid is thought to be asynchronous and earlier for Cbeta-O bond cleavage than for Calpha-H bond cleavage.
Starting Page	44
Ending Page	45
Page Count	2
File Format	PDF HTM / HTML
Alternate Webpage(s)	http://www.jbc.org/content/early/2004/04/08/jbc.R400001200.full.pdf
PubMed reference number	15073190v1
Volume Number	279
Issue Number	26
Journal	The Journal of biological chemistry
Language	English
Access Restriction	Open
Subject Keyword	Acetate Acetic Acid Acid-Base Equilibrium Cysteine Synthase Degenerative polyarthritis Estradiol Excretory function Kinetics L-Serine Dehydratase Lysine PLP1 protein, human PTHLH protein, human Pyridoxal Phosphate alpha-Mannosidosis monomer newton peptidyl-L-cysteine methyl disulfide biosynthetic process from peptidyl-cysteine
Content Type	Text
Resource Type	Article

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