Any feedback?
Please rate this page
(search_result.php)
(0/150)

BRENDA support

Refine search

Search Protein Variants

show results
Don't show organism specific information (fast!)
Search organism in taxonomic tree (slow, choose "exact" as search mode, e.g. "mammalia" for rat,human,monkey,...)
(Not possible to combine with the first option)
Refine your search

Search term:

Results 1 - 10 of 26 > >>
EC Number Protein Variants Commentary Reference
Show all pathways known for 1.13.11.20Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.20C164A mutation of C164 shows a about 20% abatement of enzymatic activity 674873
Show all pathways known for 1.13.11.20Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.20C164A mutations of nonessential residues has little effect 695529
Show all pathways known for 1.13.11.20Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.20C164S mutation of C164 shows a about 20% abatement of enzymatic activity 674873
Show all pathways known for 1.13.11.20Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.20C93A 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
Show all pathways known for 1.13.11.20Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.20C93A 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
Show all pathways known for 1.13.11.20Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.20C93A 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
Show all pathways known for 1.13.11.20Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.20C93E 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
Show all pathways known for 1.13.11.20Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.20C93G site-directed mutagenesis 742264
Show all pathways known for 1.13.11.20Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.20C93G site-directed mutagenesis, structure comparison to the wild-type enzyme 741904
Show all pathways known for 1.13.11.20Display the word mapDisplay the reaction diagram Show all sequences 1.13.11.20C93S 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
Results 1 - 10 of 26 > >>