Inhibitors | Comment | Organism | Structure |
---|---|---|---|
Ile | enzyme form AHS I is inhibited. Enzyme form AHS II is not inhibited | Zea mays | |
imazapyr | enzyme form AHS I and AHS II | Zea mays | |
Leu | enzyme form AHS I is inhibited. Enzyme form AHS II is not inhibited | Zea mays | |
sulfometuron-methyl | enzyme form AHS I and AHS II | Zea mays | |
Val | enzyme form AHS I is inhibited. Enzyme form AHS II is not inhibited | Zea mays |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
5 | - |
pyruvate | AHAS I | Zea mays | |
8 | - |
pyruvate | AHAS II | Zea mays |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
55000 | - |
AHAS II, gel filtration | Zea mays |
193000 | - |
AHAS I, gel filtration | Zea mays |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
pyruvate | Zea mays | first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Zea mays | - |
black mexican sweet, two enzyme forms: AHAS I and AHAS II | - |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
cell suspension culture | - |
Zea mays | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
pyruvate | - |
Zea mays | 2-acetolactate + CO2 | - |
? | |
pyruvate | first enzyme unique to biosynthesis of the branched chain amino acids Val, Leu, and Ile | Zea mays | ? | - |
? |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6 | 7 | AHAS I | Zea mays |
7 | - |
AHAS II | Zea mays |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
5.5 | 8 | pH 5.5: about 80% of maximal activity, pH 8.0: about 55% of maximal activity, AHAS I | Zea mays |
6.5 | 7.5 | about 60% of maximal activity at pH 6.5 and pH 7.5, AHAS II | Zea mays |