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Literature summary for 2.2.1.6 extracted from

  • Chipman, D.M.; Duggleby, R.G.; Tittmann, K.
    Mechanisms of acetohydroxyacid synthases (2006), Curr. Opin. Chem. Biol., 10, 88.
No PubMed abstract available
Search for more literature for 2.2.1.6

Application

Application Comment Organism
drug development the enzyme is the target of several herbicides, sulfonylureas, imidazolinones and other herbicides, structures of inhibitor-enzyme complexes explain the herbicide-enzyme interaction Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
imidazolinones the imidazolinones behave as non-competitive or uncompetitive inhibitors Escherichia coli
additional information isozyme AHAS II is not feedback inhibited Escherichia coli
sulfonylurea the inhibition by sulfonylurea is non-competitive or nearly competitive with respect to pyruvate Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetics of isozymes Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
pyruvate Escherichia coli
-
 2-acetolactate + CO2
-
 ?
pyruvate + 2-oxobutyrate Escherichia coli
-
 2-aceto-2-hydroxybutyrate + CO2
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 isozymes AHAS I-III
-

Reaction

Reaction Comment Organism Reaction ID
2 pyruvate = 2-acetolactate + CO2 catalytic mechanism via thiamine diphosphate-bound intermediates, structure-activity relationship of isozyme AHAS II Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate
-
 Escherichia coli 2-acetolactate + CO2
-
 ?
pyruvate + 2-oxobutyrate
-
 Escherichia coli 2-aceto-2-hydroxybutyrate + CO2
-
 ?
pyruvate + O2 isozymes AHAS II and AHAS III, oxygen-consuming side reaction Escherichia coli peracetate + CO2
-
 ?

Subunits

Subunits Comment Organism
More pairs of catalytic subunits form an intimate dimer containing two active sites, each of which lies across a dimer interface and involves both monomers, the catalytic subunit of AHAS II is not active alone Escherichia coli

Synonyms

Synonyms Comment Organism
acetohydroxyacid synthase
-
 Escherichia coli
AHAS
-
 Escherichia coli

Cofactor

Cofactor Comment Organism Structure
FAD the flavin plays a crucial role in the structural integrity, and is reduced in the course of catalysis as a result of an internal redox side reaction Escherichia coli
thiamine diphosphate dependent on, the bound cofactor adopts a V-conformation in the active site, fixing the 4'-NH2 group very close to the C2-H of the thiazolium group Escherichia coli