EC Number   |
Protein Variants |
Reference |
|---|
  2.7.2.12 | D272A/R274A/Q323G/M324I |
the mutations decrease kcat in the acetate-forming direction by about 2500-5000fold but have little effect on Km for either substrate compared to the wild type enzyme. This mutant has no detectable activity in the acetyl phosphate-forming direction |
762441 |
| 2.7.2.12 | DELTAG203/Q323G/M324I |
inactive |
762441 |
| 2.7.2.12 | H117A |
mutant is inactive in the direction of acetyl phosphate formation. In the direction of acetate formation, alteration of the His117 results in a 16fold increase in the Km for acetyl phosphate and a 95fold decreased kcat, and for a 1500fold reduction in catalytic efficiency |
722150 |
| 2.7.2.12 | H172A |
mutant is inactive in the direction of acetyl phosphate formation. The His172Ala mutant has a similar Km for acetyl phosphate as wild-type, the kcat value is reduced 970fold |
722150 |
| 2.7.2.12 | I116A |
mutant shows no substantial change in the Km for acetate, mutant has a 26fold decreased kcat. In the direction of acetate formation, the Ile116Ala and Ile116Leu variants both display a mild increase in the Km for acetyl phosphate and decreased kcat, resulting in 22- to 27fold-decreased catalytic efficiencies, respectively |
722150 |
| 2.7.2.12 | I116L |
mutant shows no substantial change in the Km for acetate. In the direction of acetate formation, the Ile116Ala and Ile116Leu variants both display a mild increase in the Km for acetyl phosphate and decreased kcat, resulting in 22- to 27fold-decreased catalytic efficiencies, respectively |
722150 |
| 2.7.2.12 | more |
constructio of an acetate kinase antisense knockout mutant strain |
737773 |
| 2.7.2.12 | Q323A/M324A |
the variant displays similar Km values for acetyl phosphate and slightly decreased Km values for phosphate as the wild type enzyme but the kcat value is decreased 19fold resulting in about 11fold reduced catalytic efficiency. In the direction of acetyl phosphate formation, these variant displays slightly increased Km for acetate but no increase in Km for diphosphate and only mild decrease in kcat |
762441 |
| 2.7.2.12 | Q323G/M324I |
the variant displays similar Km values for acetyl phosphate and slightly decreased Km values for phosphate as the wild type enzyme but the kcat value is decreased 8.3fold resulting in about 7fold reduced catalytic efficiency. In the direction of acetyl phosphate formation, these variant displays slightly increased Km for acetate but no increase in Km for diphosphate and only mild decrease in kcat |
762441 |
| 2.7.2.12 | T223G |
mutant shows significant activity in the acetate-forming direction of the assay but does not display activity in the acyl phosphate-forming direction with any acyl substrate |
722150 |
