EC Number   |
General Information |
Reference  |
|---|
    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 |
transformation of a H+-ATPase defective strain with a C-terminal truncation of acetohydroxyacid synthase gene ilvBN results in increased valine production from 21.7 mM for wild-type to 46.7 mM and increase in the valine intermediate acetoin. Inserting acetohydroxyacid isomeroreductase gene into the ilvBN plasmid further increases valine producion |
696827 |
| 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 |
| 2.2.1.6 | more |
wild-type and mutant H28A/N484A active site structure analysis, PDB IDs 2PGN and 4D5G |
-, 733089 |
| 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 |
fermentation pathways in Klebsiella pneumoniae, overview. The biosynthesis route of 2,3-BD in Klebsiella pneumoniae proceeds via pyruvate, acetolactate, and acetoin to 2,3-BD. 2,3-BD production from pyruvate involves three enzymes, namely, 2-acetolactate synthase (ALS), 2-acetolactate decarboxylase (ALDC), and acetoin reductase (AR). These enzymes catalyze the production of acetolactate from pyruvate, acetoin from acetolactate, and 2,3-BD from acetoin |
-, 733547 |
| 2.2.1.6 | evolution |
two types of ALSs, anabolic acetohydroxyacid synthase (AHAS) and catabolic ALSs (cALS). The anabolic AHAS is primarily found in plants, fungi, and bacteria, is involved in the biosynthesis of branched-chain amino acids, and contains FAD, whereas the cALS is found only in some bacteria and is involved in the butanediol fermentation pathway. Both of the enzymes are thiamine diphosphate-dependent and require a divalent metal ion for catalytic activity. The catabolic ALS can be distinguished from anabolic AHAS by a low optimal pH of about pH 6.0, FAD-independent functionality, a genetic location within the butanediol operon, and lack of a regulatory subunit. In all of the crystal structures of ThDP-dependent enzymes determined to date, with the exception of glyoxylate carbo-ligase (GCL), a highly conerved glutamate residue is found at hydrogen-bonding distance from the N1' atom of the aminopyrimidine ring of the boundThDP and plays a key role in catalysis. In Enterococcus faecalis it is Glu49 |
733597 |
| 2.2.1.6 | evolution |
the enzyme belongs to the ALS enzyme family that forms a distinct subgroup of ThDP-dependent enzymes. The ALS subfamily differs significantly in structure and possibly in catalytic mechanism, phylogenetic analysis. The ThDP-dependent enzymes cluster into three distinct sequence groups: acetolactate synthases, acetohydroxyacid synthases, and carboxylases. Eventhough ALS and AHAS catalyze the same reaction, they show different cofactors and domain structure: AHAS family enzymes have both catalytic and regulatory subunits, structure comparisons, overview |
-, 733658 |
| 2.2.1.6 | more |
active site structure, catalytically relevant structure-function relationships, overview |
-, 733658 |
