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 | 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 Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | kinetics of isozymes | Escherichia coli |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
isozymes AHAS I-III | - |
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 |
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 | 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 | Comment | Organism |
---|---|---|
acetohydroxyacid synthase | - |
Escherichia coli |
AHAS | - |
Escherichia coli |
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 |