EC Number   |
Protein Variants |
Reference |
|---|
    3.1.2.2 | D154A |
kcat/KM for p-nitrophenyl butyrate is 18% of wild-type value. kcat/KM for lauroyl-CoA is 11% of wild-type value. kcat/KM for N-carbobenzoxy-L-tyrosine p-nitrophenyl ester is 29% of wild-type value |
678033 |
| 3.1.2.2 | D17A |
mutant shows no activity |
-, 732090 |
| 3.1.2.2 | D213A |
mutation results in a strong reduction in catalytic activity |
682542 |
| 3.1.2.2 | E39A |
mutation does not affect activity |
682542 |
| 3.1.2.2 | E39D/T198N |
mutant displays a 4fold increase in the catalytic activity compared with wild-type Acot7 |
682542 |
| 3.1.2.2 | E77Q |
mutation decreased the enzyme activity to less than 10fold of wild-type |
-, 679171 |
| 3.1.2.2 | G44A |
kcat/KM for p-nitrophenyl butyrate is 16% of wild-type value. kcat/KM for lauroyl-CoA is 15% of wild-type value. kcat/KM for N-carbobenzoxy-L-tyrosine p-nitrophenyl ester is 25% of wild-type value |
678033 |
| 3.1.2.2 | H157A |
kcat/KM for p-nitrophenyl butyrate is 0.09% of wild-type value |
678033 |
| 3.1.2.2 | H72A |
mutation decreased the enzyme activity to less than 10fold of wild-type |
679171 |
| 3.1.2.2 | L109P |
mutation shifts the substrate-preference from medium-to-long acyl chains to shorter acyl-chains of triglyceride and p-nitrophenyl ester, and increases the preference for aromatic-amino acid-derived esters. kcat for lauroyl-CoA is 17.8fold lower than wild-type value, Km-value for lauroyl-CoA is 1.3fold higher than wild-type value |
678465 |
