flavin-adenine-dinucleotide has been researched along with hydroxypyruvic-acid* in 1 studies
1 other study(ies) available for flavin-adenine-dinucleotide and hydroxypyruvic-acid
| Article | Year |
|---|---|
Suicide inhibition of acetohydroxyacid synthase by hydroxypyruvate.
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. Topics: Acetolactate Synthase; Catalysis; Escherichia coli; Flavin-Adenine Dinucleotide; Kinetics; Pyruvates; Recombinant Proteins; Substrate Specificity; Thiamine Pyrophosphate | 2005 |