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Literature summary for 2.2.1.6 extracted from

  • McCourt, J.A.; Duggleby, R.G.
    How an enzyme answers multiple-choice questions (2005), Trends Biochem. Sci., 30, 222-225.
    View publication on PubMed
Search for more literature for 2.2.1.6

Application

Application Comment Organism
drug development AHAS is the target of the sulfonylurea and imidazolinone herbicides Escherichia coli
drug development AHAS is the target of the sulfonylurea and imidazolinone herbicides Saccharomyces cerevisiae

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structure analysis Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
additional information isozyme AHAS II mutants of residues Phe109, Met250, Arg276 and Trp464 are nearly inactive in (S)-2-acetolactate formation, but show increased activity with pyruvate and benzaldehyde compared to the wild-type isozyme Escherichia coli
W464L the mutant of isozyme AHAS II has lost the preference for 2-ketobutyrate as second substrate Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
branched-chain amino acids feedback inhibition, differential inhibition of isozymes, overview Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pyruvate Escherichia coli the enzyme is the first common enzyme in the pathway for the biosynthesis of branched-chain amino acids, overview (S)-2-acetolactate + CO2
-
 ?
pyruvate Saccharomyces cerevisiae the enzyme is the first common enzyme in the pathway for the biosynthesis of branched-chain amino acids, overview (S)-2-acetolactate + CO2
-
 ?
pyruvate + 2-oxobutyrate Escherichia coli stereospecific reaction (S)-acetohydroxybutyrate + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 isozymes I-III
-
Saccharomyces cerevisiae P07342
-
-

Reaction

Reaction Comment Organism Reaction ID
2 pyruvate = 2-acetolactate + CO2 catalytic mechanism and active site structure, covalent intermediates Saccharomyces cerevisiae
a
2 pyruvate = 2-acetolactate + CO2 catalytic mechanism, covalent intermediates Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information substrate specificity ratios of isozymes I-III, substrate recognition mechanism, overview Escherichia coli ?
-
 ?
pyruvate stereospecific reaction Escherichia coli (S)-2-acetolactate + CO2
-
 ?
pyruvate stereospecific reaction Saccharomyces cerevisiae (S)-2-acetolactate + CO2
-
 ?
pyruvate the enzyme is the first common enzyme in the pathway for the biosynthesis of branched-chain amino acids, overview Escherichia coli (S)-2-acetolactate + CO2
-
 ?
pyruvate the enzyme is the first common enzyme in the pathway for the biosynthesis of branched-chain amino acids, overview Saccharomyces cerevisiae (S)-2-acetolactate + CO2
-
 ?
pyruvate + 2-oxobutyrate stereospecific reaction Escherichia coli (S)-acetohydroxybutyrate + CO2
-
 ?
pyruvate + benzaldehyde stereospecific reaction, benzaldehyde is an artificial substrate, especially of mutants of isozyme AHAS II residues Phe109, Met250, Arg276 and Trp464 Escherichia coli (R)-phenylacetylcarbinol + CO2
-
 ?

Synonyms

Synonyms Comment Organism
acetohydroxy acid synthase
-
 Escherichia coli
acetohydroxy acid synthase
-
 Saccharomyces cerevisiae
AHAS
-
 Escherichia coli
AHAS
-
 Saccharomyces cerevisiae

Cofactor

Cofactor Comment Organism Structure
FAD
-
 Escherichia coli
FAD
-
 Saccharomyces cerevisiae
thiamine diphosphate
-
 Escherichia coli
thiamine diphosphate
-
 Saccharomyces cerevisiae