EC Number   |
Protein Variants |
Reference |
|---|
   6.2.1.33 | D385A |
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme |
690988 |
| 6.2.1.33 | D402A |
100fold decrease in ratio kcat/Km for CoA |
702299 |
| 6.2.1.33 | D402P |
crystallization data. Mutant adopts the proposed adenylate-forming conformation with very little change to the overall structure.The ability of the mutant to catalyze the adenylate-forming half-reaction is reduced by about 3fold, catalysis of the second half-reaction is reduced by 4 orders of magnitude |
702299 |
| 6.2.1.33 | E306Q |
mutant enzymes G163I, G166I, P168A, K169M and E306Q with reduced catalysis of the adenylation of 4-chlorobenzoate |
-, 776 |
| 6.2.1.33 | E410A |
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme |
690988 |
| 6.2.1.33 | F473A |
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzymem but increased kcat |
690988 |
| 6.2.1.33 | G163I |
mutant enzymes G163I, G166I, P168A, K169M and E306Q with reduced catalysis of the adenylation of 4-chlorobenzoate |
-, 776 |
| 6.2.1.33 | G166I |
mutant enzymes G163I, G166I, P168A, K169M and E306Q with reduced catalysis of the adenylation of 4-chlorobenzoate |
-, 776 |
| 6.2.1.33 | G408A |
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme |
690988 |
| 6.2.1.33 | H207A |
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme |
690988 |
