EC Number |
Protein Variants |
Reference |
---|
1.13.11.20 | C164A |
mutation of C164 shows a about 20% abatement of enzymatic activity |
674873 |
1.13.11.20 | C164A |
mutations of nonessential residues has little effect |
695529 |
1.13.11.20 | C164S |
mutation of C164 shows a about 20% abatement of enzymatic activity |
674873 |
1.13.11.20 | C93A |
C93 mutation reduces activity to 50%, zinc content of about 45%, specific activity of Cys-93 mutants is proportional to the measured iron content. |
674873 |
1.13.11.20 | C93A |
site-directed mutagenesis, CDO activity of the C93A variant increases with a much lower rate of iron supplementation and consequently a much higher concentration is required to approximate saturation, it has a 18fold higher Kd value |
741585 |
1.13.11.20 | C93A |
site-directed mutagenesis, mutation of the active site residue, no crosslink formation resulting in reduced activity compared to the wild-type enzyme. The mutant variant structure has a new chloride ion coordinating the active site iron. Cys binding is also different from wild-type CDO, and no Cys-persulfenate forms in the C93A active site at pH 6.2 or pH 8.0 |
743088 |
1.13.11.20 | C93E |
mutation to the corresponding residue of cupin to reestablish the common 3-His/1-Glu metal ligand of the cupin superfamily. Mutant shows dioxygen consumption, which, is not coupled with L-cysteine oxidation. Substrate analogues (D-cysteine, cysteamine, and 3-mercaptopropionate) show variable coordinations to the iron center, but are not viable substrates for the variant |
764172 |
1.13.11.20 | C93G |
site-directed mutagenesis |
742264 |
1.13.11.20 | C93G |
site-directed mutagenesis, structure comparison to the wild-type enzyme |
741904 |
1.13.11.20 | C93S |
C93 mutation reduces activity to 50%, zinc content of about 45%, specific activity of Cys-93 mutants is proportional to the measured iron content. |
674873 |