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Literature summary 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

Application

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

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.2.1.6 crystal structure analysis Saccharomyces cerevisiae

Protein Variants

EC Number Protein Variants Comment Organism
2.2.1.6 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
2.2.1.6 W464L the mutant of isozyme AHAS II has lost the preference for 2-ketobutyrate as second substrate Escherichia coli

Inhibitors

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

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.2.1.6 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
-
?
2.2.1.6 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
-
?
2.2.1.6 pyruvate + 2-oxobutyrate Escherichia coli stereospecific reaction (S)-acetohydroxybutyrate + CO2
-
?

Organism

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

Reaction

EC Number Reaction Comment Organism Reaction ID
2.2.1.6 2 pyruvate = 2-acetolactate + CO2 catalytic mechanism and active site structure, covalent intermediates Saccharomyces cerevisiae
2.2.1.6 2 pyruvate = 2-acetolactate + CO2 catalytic mechanism, covalent intermediates Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.2.1.6 additional information substrate specificity ratios of isozymes I-III, substrate recognition mechanism, overview Escherichia coli ?
-
?
2.2.1.6 pyruvate stereospecific reaction Escherichia coli (S)-2-acetolactate + CO2
-
?
2.2.1.6 pyruvate stereospecific reaction Saccharomyces cerevisiae (S)-2-acetolactate + CO2
-
?
2.2.1.6 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
-
?
2.2.1.6 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
-
?
2.2.1.6 pyruvate + 2-oxobutyrate stereospecific reaction Escherichia coli (S)-acetohydroxybutyrate + CO2
-
?
2.2.1.6 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

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

Cofactor

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