EC Number   |
Protein Variants |
Reference |
|---|
   3.1.1.81 | A206F |
the ratio of kcat/Km for N-butyryl-L-homoserine lactone/N-decanoyl-L-homoserine lactone is 3.34% compared to 2.09% for wild-type enzyme |
749727 |
| 3.1.1.81 | A206I |
the ratio of kcat/Km for N-butyryl-L-homoserine lactone/N-decanoyl-L-homoserine lactone is 0.85% compared to 2.09% for wild-type enzyme |
749727 |
| 3.1.1.81 | A206L |
the ratio of kcat/Km for N-butyryl-L-homoserine lactone/N-decanoyl-L-homoserine lactone is 0.89% compared to 2.09% for wild-type enzyme |
749727 |
| 3.1.1.81 | A206V |
the ratio of kcat/Km for N-butyryl-L-homoserine lactone/N-decanoyl-L-homoserine lactone is 0.17% compared to 2.09% for wild-type enzyme |
749727 |
| 3.1.1.81 | A206W |
site-directed mutagenesis, structure and catalytic mechanism compared to the wild-type, overview |
690981 |
| 3.1.1.81 | A206W |
the ratio of kcat/Km for N-butyryl-L-homoserine lactone/N-decanoyl-L-homoserine lactone is 2.16% compared to 2.09% for wild-type enzyme |
-, 749727 |
| 3.1.1.81 | C258L/I261F/W263A |
site-directed mutagenesis, the mutant is not able to hydrolyze C8-HSL or C10-HSL and its paraoxonase activity is 3fold higher than the lactonase activity on 5-thiobutyl butyrolactone, as opposed to the wild-type paraoxonase activity which is 760fold lower than the lactonase activity. The combination of C258L, I261F, and W263A mutations in the SsoPox triple mutant improves the hydrolytic specific activity in terms of kcat/KM toward paraoxon 12fold, the kcat 294fold compared to wild-type SsoPox, while the KM value increases |
750128 |
| 3.1.1.81 | C258L/I261F/W263A |
the mutant exhibits enhanced phosphotriesterase activity compared to the wild type enzyme |
752216 |
| 3.1.1.81 | D108A |
site-directed mutagenesis, the mutant enzyme shows a reduced Zn2+ content compared to the wild-type enzyme |
666738 |
| 3.1.1.81 | D108E |
site-directed mutagenesis, mutation of a zinc-binding motif residue, the mutant shows 90.8% of wild-type enzyme activity |
666770 |
