EC Number   |
Protein Variants |
Reference |
|---|
    1.3.1.44 | F11K |
kcat slightly decreased compared to wild-type, Km (NADH) decreased compared to wild-type |
724240 |
| 1.3.1.44 | F11K |
the mutant shows 198% activity compared to the wild type enzyme |
724240 |
| 1.3.1.44 | F295A |
mutant shows kinetic behaviour relatively similar to wild-type toward substrates crotonyl-CoA and hexanoyl-CoA |
-, 724351 |
| 1.3.1.44 | I287A |
mutant shows significant decreased kcat values compared to wild-type, mutant exhibit larger increases in catalytic efficiency on the longer hexanoyl-CoA substrate (versus the crotonyl-CoA substrate) of 100 and 17fold compared to that of the wild type (7fold) suggesting suggest these mutations may increase the accessibility of the longer acyl chain to the active site pocket. Mutant shows a much lower Ki (lauroyl-CoA) than wild-type |
-, 724351 |
| 1.3.1.44 | K165A |
site-directed mutagenesis, mutation of putative catalytic residue |
657270 |
| 1.3.1.44 | K165Q |
site-directed mutagenesis, mutation of putative catalytic residue |
657270 |
| 1.3.1.44 | K244A |
inactive |
724240 |
| 1.3.1.44 | K244A |
mutant shows no activity |
724240 |
| 1.3.1.44 | K245A |
kcat slightly decreased compared to wild-type, Km (NADH) increased compared to wild-type |
724240 |
| 1.3.1.44 | K245A |
the mutant shows 67 activity compared to the wild type enzyme |
724240 |
