EC Number   |
Protein Variants |
Reference |
|---|
  1.14.14.28 | A102D |
hydroxylation activity of purified LadA mutant on hexadecane is 2.1fold higher than that of the wild-type enzyme. Hexadecane degradation rate is 2.3fold higher than that of the wild-type enzyme. A Pseudomonas fluorescens KOB2DELTA1 strain expressing the LadA mutant grows more rapidly with hexadecane than the strain expressing wild-type LadA, confirming the enhanced activity of LadA mutant in vivo. Mutant enzyme with the same size as the wild-type LadA protein. Compared to the wild-type enzyme, the mutant enzyme utilizes a narrower spectrum of n-alkanes, including C16 to C28 |
-, 737528 |
| 1.14.14.28 | A102D/F146C/L320V/N376I |
mutant enzyme completely loses the catalytic activity |
737528 |
| 1.14.14.28 | A102D/F146C/N376I |
mutant enzyme completely loses the catalytic activity |
737528 |
| 1.14.14.28 | A102D/L320V |
mutant enzyme completely loses the catalytic activity |
737528 |
| 1.14.14.28 | A102E |
hydroxylation activity of purified LadA mutant on hexadecane is 2.2fold higher than that of the wild-type enzyme. Hexadecane degradation rate is 2.2fold higher than that of the wild-type enzyme. A Pseudomonas fluorescens KOB2DELTA1 strain expressing the LadA mutant grows more rapidly with hexadecane than the strain expressing wild-type LadA, confirming the enhanced activity of LadA mutant in vivo. Mutant enzyme with the same size as the wild-type LadA protein |
-, 737528 |
| 1.14.14.28 | C14A |
point mutation completely abolishes the catalytic activity |
-, 736632 |
| 1.14.14.28 | F146C |
mutant enzyme completely loses the catalytic activity |
-, 737528 |
| 1.14.14.28 | F146C/L320V/N376I |
mutant enzyme completely loses the catalytic activity |
737528 |
| 1.14.14.28 | F146C/N376I |
hydroxylation activity of purified LadA mutant on hexadecane is 2.9fold higher than that of the wild-type enzyme. Hexadecane degradation rate is 2.9fold higher than that of the wild-type enzyme. A Pseudomonas fluorescens KOB2DELTA1 strain expressing the LadA mutant grows more rapidly with hexadecane than the strain expressing wild-type LadA, confirming the enhanced activity of LadA mutant in vivo. Mutant enzyme with the same size as the wild-type LadA protein |
737528 |
| 1.14.14.28 | F146E/N376I |
hydroxylation activity of purified LadA mutant on hexadecane is 2.0fold higher than that of the wild-type enzyme. Hexadecane degradation rate is 2.7fold higher than that of the wild-type enzyme. A Pseudomonas fluorescens KOB2DELTA1 strain expressing the LadA mutant grows more rapidly with hexadecane than the strain expressing wild-type LadA, confirming the enhanced activity of LadA mutant in vivo. Mutant enzyme with the same size as the wild-type LadA protein. Compared to the wild-type enzyme, the mutant enzyme utilizes a narrower spectrum of n-alkanes, including C15 to C28 |
737528 |
