EC Number   |
General Information |
Reference |
|---|
    2.2.1.6 | metabolism |
acetohydroxyacid synthase is the key enzyme in branched chain amino acid biosynthesis pathway, overview |
733241 |
| 2.2.1.6 | metabolism |
acetohydroxyacid synthase or asacetolactate synthase catalyzes the first step in the biosynthe-sis of branched-chain amino acids such as isoleucine, leucine, and valine. This reaction involves synthesizing either (2S)-acetolactate from two molecules of pyruvate or (2S)-2-aceto-2-hydroxybutyrate from pyruvate and 2-oxobutyrate |
-, 733747 |
| 2.2.1.6 | evolution |
acetolactate synthase and pyruvate decarboxylase are both thiamine diphosphate-dependent enzymes that use pyruvate as a substrate, but they produce different products.Whereas pyruvate decarboxylase catalyzes the non-oxidative decarboxylation of pyruvate to acetaldehyde, acetolactate synthase, which is involved in the biosynthesis of branched amino acids (Val, Leu, Ile), catalyzes the carboligation between two pyruvate molecules to form an acetolactate molecule and carbon dioxide, structural and functional similarities of the enzymes, overview |
-, 735039 |
| 2.2.1.6 | metabolism |
acetolactate synthase catalyses the first common step in leucine, isoleucine and valine biosynthesis |
-, 734734 |
| 2.2.1.6 | metabolism |
acetolactate synthase is a thiamine diphosphate-dependent enzyme that is involved in the biosynthesis of branched amino acids (Val, Leu, Ile), catalyzing the carboligation between two pyruvate molecules to form an acetolactate molecule and carbon dioxide |
-, 735039 |
| 2.2.1.6 | more |
active site structure, catalytically relevant structure-function relationships, overview |
-, 733658 |
| 2.2.1.6 | physiological function |
catabolic acetolactate synthase from Enterococcus faecalis is a FAD-independent enzyme, which catalyzes the condensation of two molecules of pyruvate to produce acetolactate |
733987 |
| 2.2.1.6 | physiological function |
complete inactivation of the acetolactate synthase in Corynebacterium glutamicum DM1729 and DM1933 by deletion of the ilvB gene, encoding the catalytic subunit, leads to L-valine, L-isoleucine, and L-leucine auxotrophy and to improved L-lysine production |
695780 |
| 2.2.1.6 | physiological function |
deletion of gene ilv2 encoding acetolactate synthase results in loss of viability during isoleucine and valine starvation due to 2-oxobutanoate accumulation. Rapamycin further decreases vialbility of the mutant. Recovery from starvation is influenced by the carbon source present during recovery |
700065 |
| 2.2.1.6 | physiological function |
deletion of gene ilv2 encoding acetolactate synthase results in significant attenuation of virulence and a grater than 100fold reduction in viability after only four hours of isoleucine and valine starvation due to 2-oxobutanoate accumulation. Rapamycin increases vialbility of both ilv1 and ilv2 mutants. Recovery from starvation is influenced by the carbon source present during starvation |
700065 |
