EC Number |
Natural Substrates |
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2.2.1.6 | more |
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 | more |
acetolactate synthase is the first common enzyme in the biosynthetic pathway of branched-chain amino acids |
2.2.1.6 | more |
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 | more |
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 | more |
non-enzymatic decarboxylation of acetolactate to acetoin |
2.2.1.6 | more |
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 | more |
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 |