EC Number |
Protein Variants |
Reference |
---|
3.2.2.24 | C102S |
enzyme maintains activity after removal of light, shows a significantly poorer affinity for Mn2+, and higher affinity for the calcium site of the hydroxylapatite column than wild-type |
661730 |
3.2.2.24 | D123A |
reduced catalytic activity and binding of Mn2+ |
646970 |
3.2.2.24 | D243G |
no catalytic activity or binding of Mn2+ |
646970 |
3.2.2.24 | E279R |
catalytic and electron paramagnetic resonance spectral properties like wild type |
646970 |
3.2.2.24 | H142L |
catalytic and electron paramagnetic resonance spectral properties like wild type |
646970 |
3.2.2.24 | H158N |
no catalytic activity or binding of Mn2+ |
646970 |
3.2.2.24 | more |
overexpression of enzyme results in only partial ADP-ribosylation of Fe protein by adding ammonium. Loss of regulation after overespression may be due to titrating out negative regulators |
660835 |
3.2.2.24 | more |
physiological effects of mutants lacking enzyme activity |
489807 |
3.2.2.24 | N100K |
enzyme maintains activity after removal of light and does not respond to addition of NH4Cl, shows a significantly poorer affinity for Mn2+ and higher affinity for the calcium site of the hydroxylapatite column than wild-type |
661730 |
3.2.2.24 | V98L |
enzyme maintains activity after removal of light, and shows higher affinity for the calcium site of the hydroxylapatite column than wild-type |
661730 |