@article{ref1,
title="Suicide inhibition of acetohydroxyacid synthase by hydroxypyruvate",
journal="Journal of enzyme inhibition and medicinal chemistry",
year="2005",
author="Duggleby, Ronald G.",
volume="20",
number="1",
pages="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.<p /><p>Language: en</p>",
language="en",
issn="1475-6366",
doi="10.1080/14756360400020553",
url="http://dx.doi.org/10.1080/14756360400020553"
}