EC Number |
Protein Variants |
Reference |
---|
3.7.1.7 | C241A/C248A |
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme |
733273 |
3.7.1.7 | more |
the mutants show reduced kcat/Km for 4-nitrophenyl acetate, indicating the importance of Trp255 in sequestering the active site from solvent. The significantly lower activity for 4-nitrophenyl butyrate can be a result of product inhibition. The mutant activity is retained with 4-nitrophenyl caprylate and 4-nitrophenyl laurate as the substrates, reflecting the amphipathic nature of the cleft |
-, 733273 |
3.7.1.7 | S172A |
site-directed mutagenesis, the mutant shows 20% activity compared to the wild-type enzyme |
-, 733273 |
3.7.1.7 | S172A |
site-directed mutagenesis, the mutant shows 20% activity compared to the wild-type enzyme, structure comarison with the wild-type enzyme |
-, 733656 |
3.7.1.7 | S172C |
site-directed mutagenesis |
-, 733273 |
3.7.1.7 | S172C |
site-directed mutagenesis, the mutant shows less than 10% activity compared to the wild-type enzyme, structure comarison with the wild-type enzyme |
-, 733656 |
3.7.1.7 | W255A |
site-directed mutagenesis |
-, 733273 |
3.7.1.7 | W255F |
site-directed mutagenesis |
733273 |
3.7.1.7 | W255Y |
site-directed mutagenesis |
-, 733273 |