2.2.1.6	2 pyruvate	-	
2.2.1.6	2 pyruvate	acetohydroxyacid synthase is the enzyme that catalyses the first step in the common pathway of the biosynthesis of the branched chain amino acids, valine, leucine and isoleucine	
2.2.1.6	2 pyruvate	AHAS catalyzes the first common step in the biosynthetic pathway of the branched-amino acids leucine, isoleucine, and valine	
2.2.1.6	2 pyruvate	irreversible decarboxylation of pyruvate	
2.2.1.6	2 pyruvate	the enzyme produces 2-acetolactate in a temperature-dependent manner	
2.2.1.6	2-oxobutyrate	-	
2.2.1.6	2-oxobutyrate + pyruvate	-	
2.2.1.6	2-oxoisovalerate	-	
2.2.1.6	additional information	mechanism of expression regulation, overview	
2.2.1.6	additional information	regulatory role of the proteins of the phosphoenolpyruvate:carbohydrate phosphotransferase system, requirement of the dephospho-form of enzyme IIANtr, encoded by gene ptsN, for derepression of Escherichia coli K-12 ilvBN expression, overview	
2.2.1.6	additional information	the enzyme can act in anabolic or in catabolic function, the first enzyme contains the conserved motif 372RFDDR376, while the latter does not, the conserved motif 372RFDDR376 is a possible determinant of the FAD-dependent and herbicide-resistant properties of tobacco, overview	
2.2.1.6	additional information	acetolactate synthase is the first common enzyme in the biosynthetic pathway of branched-chain amino acids	
2.2.1.6	additional information	AHAS catalyses the first step leading to all three branched-chain amino acids, in the reactions, enzyme-bound thiamine diphosphate reacts with pyruvate, releasing CO2 and forming an acetaldehyde moiety as enzyme-bound hydroxyethyl-ThDP, resonating enamine/alpha-carbanion intermediate	
2.2.1.6	additional information	enzyme AlsS catalyzes the condensation of two pyruvate molecules to acetolactate with thiamine diphosphate and Mg2+ as cofactors. The enzyme also catalyzes the conversion of 2-ketoisovalerate into isobutyraldehyde, the immediate precursor of isobutanol	
2.2.1.6	additional information	non-enzymatic decarboxylation of acetolactate to acetoin	
2.2.1.6	additional information	the enzyme catalyzes the C-C bond cleavage of cyclohexane-1,2-dione to 6-oxohexanoate, EC 3.7.1.11, and the asymmetric benzoin condensation between benzaldehyde and pyruvate	
2.2.1.6	additional information	YerE might posses the ability to activate non-sugar ketones for cross-benzoin condensations, performing enzymatic aldehyde-ketone cross-benzoin condensations	
2.2.1.6	pyruvate	-	
2.2.1.6	pyruvate	first committed step in the biosynthesis of valine and leucine	
2.2.1.6	pyruvate	first step in the biosynthesis of valine, overview	
2.2.1.6	pyruvate	the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine	
2.2.1.6	pyruvate	the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine, overview	
2.2.1.6	pyruvate	the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine, regulation, overview	
2.2.1.6	pyruvate	isoenzyme II is regulated by Leu, Ile and Val	
2.2.1.6	pyruvate	isoenzyme II is regulated by Leu	
2.2.1.6	pyruvate	the enzyme plays a role in not only preventing intracellular acidification but also supplying alpha-acetolactate as an intermediate of branched chain amino acids biosynthesis	
2.2.1.6	pyruvate	production of isoenzyme AHS I is under multivalent control by Val and Leu, production of isoenzyme AHS II is under multivalent control by Ile, Val and Leu	
2.2.1.6	pyruvate	isoenzyme AHAS I enables a bacterium to cope with poor carbon sources, which lead to low endogenous pyruvate concentrations	
2.2.1.6	pyruvate	constitutive high expression, the enzyme is active only under conditions of pyruvate excess	
2.2.1.6	pyruvate	the expression is negatively controlled by Val. Leu and Ile slightly stimulate the enzyme production	
2.2.1.6	pyruvate	catabolic enzyme is involved in 2,3-butanediol pathway	
2.2.1.6	pyruvate	key enzyme in synthesis of branched-chain amino acids	
2.2.1.6	pyruvate	first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile	
2.2.1.6	pyruvate	isoenzyme I is regulated by Leu and Val	
2.2.1.6	pyruvate	the enzyme is the first common enzyme in the pathway for the biosynthesis of branched-chain amino acids, overview	
2.2.1.6	pyruvate + 2-oxobutyrate	stereospecific reaction	
2.2.1.6	pyruvate + 2-oxobutyrate	-	
2.2.1.6	pyruvate + 2-oxobutyrate	first committed step in the biosynthesis of isoleucine	
2.2.1.6	pyruvate + 2-oxobutyrate	irreversible decarboxylation of pyruvate	
2.2.1.6	pyruvate + pyruvate	-