EC Number   |
Protein Variants |
Reference |
|---|
    1.3.1.24 | C280A |
although modification of either of the two cysteines located near the C-terminus significantly reduces activity with both cofactors, these mutations do not inactivate the enzyme, mutation of both C-terminal cysteines causes inactivation of the enzyme, comparison of Km values suggests that Cys 280 principally functions in substrate binding |
437824 |
| 1.3.1.24 | C281A/C292A/C293A |
C-terminal fragment 272-296 in which cysteine residues are replaced by alanine do not interact with Goodpasture antigen-binding protein whereas wild-type C-terminal fragment 276-296 does |
725479 |
| 1.3.1.24 | C281A/C292A/C293A |
mutant is defective for protein-protein-dependent interaction and haematin binding |
685007 |
| 1.3.1.24 | C291A |
although modification of either of the two cysteines located near the C-terminus significantly reduces activity with both cofactors, these mutations do not inactivate the enzyme, mutation of both C-terminal cysteines causes inactivation of the enzyme, comparison of Km values suggests that Cys 291 is predominantly involved in cofactor binding. |
437824 |
| 1.3.1.24 | C73A |
the modification of the amino-proximal cysteine, which is flanked by a tyrosine residue, completely inactivates the enzyme with NADH at pH 6.75 and NADPH at pH 8.7 |
437824 |
| 1.3.1.24 | E47A |
mutant, does affect the edge of the beta2 strand of substrate and cofactor binding in the pocket, which likely influences the strength of their interaction with BVR |
698922 |
| 1.3.1.24 | E97A |
mutant, data strongly support this site as important for conversion of biliverdin to bilirubin and for transmission of signaling by BVR |
698922 |
| 1.3.1.24 | G17A |
does not effectively bind ATP, hence kinase-dead, is not as effective as the wild-type in potentiating protein kinase C activity |
674899 |
| 1.3.1.24 | G17A |
mutant is defective for ATP binding |
685007 |
| 1.3.1.24 | H132A |
the mutant exhibits an increased Km value for NADPH compared to the wild type enzyme |
740322 |
