Suicide inhibition of acetohydroxyacid synthase by hydroxypyruvate

Duggleby, R. G. (2005) Suicide inhibition of acetohydroxyacid synthase by hydroxypyruvate. Journal of Enzyme Inhibition And Medicinal Chemistry, 20 1: 1-4. doi:10.1080/14756360400020553


Author Duggleby, R. G.
Title Suicide inhibition of acetohydroxyacid synthase by hydroxypyruvate
Journal name Journal of Enzyme Inhibition And Medicinal Chemistry   Check publisher's open access policy
ISSN 1475-6366
Publication date 2005-02
Sub-type Article (original research)
DOI 10.1080/14756360400020553
Volume 20
Issue 1
Start page 1
End page 4
Total pages 4
Place of publication Basingstoke, UK
Publisher Taylor & Francis
Collection year 2005
Language eng
Subject C1
270108 Enzymes
780105 Biological sciences
0304 Medicinal and Biomolecular Chemistry
0601 Biochemistry and Cell Biology
Abstract Acetohydroxyacid synthase (Ec 2.2.1.6) catalyses the thiamine diphosphate-dependent reaction between two molecules of pyruvate yielding 2-acetolactacte and CO2. The enzyme will also utilise hydroxypyruvate with a k(cat) value that is 12% of that observed with pyruvate. When hydroxypyruvate is the substrate, the enzyme undergoes progressive inactivation with kinetics that are characteristic of suicide inhibition. It is proposed that the dihydroxyethyl-thiamine diphosphate intermediate can expel a hydroxide ion forming an enol that rearranges to a bound acetyl group.
Keyword Biochemistry & Molecular Biology
Chemistry, Medicinal
Acetohydroxyacid Synthase
Hydroxypyruvate
Suicide Inhibition
Thiamine Diphosphate
Acetolactate Synthase
Pyruvate Decarboxylase
Salmonella-typhimurium
Crystal-structure
Acid Synthase
Active-site
Diphosphate
Substrate
Catalysis
Enzymes
Q-Index Code C1

Document type: Journal Article
Sub-type: Article (original research)
Collections: 2006 Higher Education Research Data Collection
School of Chemistry and Molecular Biosciences
 
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Created: Wed, 15 Aug 2007, 06:33:52 EST