Cloned (Comment) | Organism |
---|---|
expression of wild-type and mutant enzymes in Escherichia coli strain DH5alpha | Nicotiana tabacum |
Protein Variants | Comment | Organism |
---|---|---|
W573F | site-directed mutagenesis, the mutant shows 69fold reduced activity compared to the wild-type enzyme, substitution of the W573 residue causes significant perturbations in the activation process and in the binding site of thiamine diphosphate | Nicotiana tabacum |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
imazapyr | i.e. 2-(4-isopropyl-4-methyl-5-oxo-2-imidazolin-2-yl)nicotinic acid | Nicotiana tabacum | |
imidazolinone | - |
Nicotiana tabacum | |
sulfonylurea | potently inhibiting herbicide | Nicotiana tabacum |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | steady-state kinetics of recombinant wild-type and mutant enzymes, cofactor binding parameters, overview | Nicotiana tabacum | |
6.53 | - |
pyruvate | pH 7.5, 37°C, recombinant wild-type enzyme | Nicotiana tabacum | |
148 | - |
pyruvate | pH 7.5, 37°C, recombinant mutant W573F | Nicotiana tabacum |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | - |
Nicotiana tabacum |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
pyruvate | Nicotiana tabacum | the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine | 2-acetolactate + CO2 | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Nicotiana tabacum | - |
- |
- |
Purification (Comment) | Organism |
---|---|
recombinant wild-type and mutant enzymes from Escherichia coli strain DH5alpha | Nicotiana tabacum |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
2 pyruvate = 2-acetolactate + CO2 | residue W573 is structurally important for FAD binding, the maintainance of the active site structure, and catalysis | Nicotiana tabacum |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
pyruvate | - |
Nicotiana tabacum | 2-acetolactate + CO2 | - |
? | |
pyruvate | the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine | Nicotiana tabacum | 2-acetolactate + CO2 | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | the mobile loop comprising residues 567-582 on the C-terminus is involved in the binding/stabilization of the active dimer and thiamin diphosphate binding, overview | Nicotiana tabacum |
Synonyms | Comment | Organism |
---|---|---|
acetohydroxy acid synthase | - |
Nicotiana tabacum |
AHAS | - |
Nicotiana tabacum |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Nicotiana tabacum |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
5.4 | - |
pyruvate | pH 7.5, 37°C, recombinant mutant W573F | Nicotiana tabacum | |
16.1 | - |
pyruvate | pH 7.5, 37°C, recombinant wild-type enzyme | Nicotiana tabacum |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Nicotiana tabacum |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
FAD | residues W573 is structurally important for FAD binding | Nicotiana tabacum | |
thiamine diphosphate | the mobile loop comprising residues 567-582 on the C-terminus are involved in the binding/stabilization of the active dimer and thiamin diphosphate binding, overview | Nicotiana tabacum |