PMID:15895677
| Citation |
Duggleby, RG (2005) Suicide inhibition of acetohydroxyacid synthase by hydroxypyruvate. J Enzyme Inhib Med Chem 20:1-4 |
|---|---|
| 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. |
| Links |
PubMed Online version:10.1080/14756360400020553 |
| Keywords |
Acetolactate Synthase/antagonists & inhibitors; Acetolactate Synthase/metabolism; Catalysis; Escherichia coli/enzymology; Flavin-Adenine Dinucleotide/metabolism; Kinetics; Pyruvates/pharmacology; Recombinant Proteins/antagonists & inhibitors; Recombinant Proteins/metabolism; Substrate Specificity; Thiamine Pyrophosphate/analogs & derivatives; Thiamine Pyrophosphate/metabolism |
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