EC Number   |
Protein Variants |
Reference |
|---|
    6.3.4.14 | C230A |
kinetic data, 50fold increased Km for ATP, no effect on the formation of carboxybiotin |
654575 |
| 6.3.4.14 | E211A |
300fold decreased maximal velocity of the biotin-dependent ATPase reaction, 100fold decreased ATP synthesis reaction with carbamoyl phosphate and ADP, abolished substrate-induced synergism by biotin, kinetic data |
-, 654566 |
| 6.3.4.14 | E23R |
mutant enzyme is monomeric in solution, mutant shows 3fold loss in catalytic activity, mutant enzyme forms the correct dimer at high concentrations. kcat/Km for ATP-hydrolysis is 2.6fold lower than wild-type value |
675923 |
| 6.3.4.14 | E23R |
the mutant protein has a kcat value about 30% that of the wild type enzyme |
727765 |
| 6.3.4.14 | E276Q |
kinetic data, ATP binding residue, reduced maximal velocity, increased Km for ATP |
656008 |
| 6.3.4.14 | E288A |
300fold decreased maximal velocity of the biotin-dependent ATPase reaction, 100fold decreased ATP synthesis reaction with carbamoyl phosphate and ADP, abolished substrate-induced synergism by biotin, kinetic data |
-, 654566 |
| 6.3.4.14 | E288K |
completely inactive mutant, hybrid dimer composed of one subunit having the active site mutation and a second with a wild-type active site: 285fold decreased activity, reduced rate of fatty acid synthesis |
656018 |
| 6.3.4.14 | E288K |
inactive active-site mutant |
693839 |
| 6.3.4.14 | E288K |
mutant with completely abolished ability to hydrolyze ATP |
655978 |
| 6.3.4.14 | E296A |
50fold decrease in catalytic efficiency, crystallization data |
704465 |
