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

BRENDA support

Refine search

Search Metals/Ions

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
Image of 2D Structure

Search term:

Results 1 - 5 of 5
EC Number Metals/Ions Commentary Reference
Show all pathways known for 3.5.4.19Display the word mapDisplay the reaction diagram Show all sequences 3.5.4.19Cd2+ 0.95 Cd2+ per enzyme subunit, competes with and replaces Zn2+, binding affects the enzyme structure, three Cd2+ are coordinated by residues Asp85 and Cys86 from one monomer and Cys109 from the other monomer, the fourth Cd2+ is bound by His16 and Asp89 667617
Show all pathways known for 3.5.4.19Display the word mapDisplay the reaction diagram Show all sequences 3.5.4.19Mg2+ required for cataltic activity. The C93 reactivity is modulated by the presence of the Zn2+ and Mg2+ and substantiates the role of this residue as a metal ligand 726992
Show all pathways known for 3.5.4.19Display the word mapDisplay the reaction diagram Show all sequences 3.5.4.19Zn2+ a single tightly bound Zn2+ per subunit 246720
Show all pathways known for 3.5.4.19Display the word mapDisplay the reaction diagram Show all sequences 3.5.4.19Zn2+ metalloprotein. The Zn2+ coordination site involves the three conserved cysteine residues. The C93 reactivity is modulated by the presence of the Zn2+ and Mg2+ and substantiates the role of this residue as a metal ligand 726992
Show all pathways known for 3.5.4.19Display the word mapDisplay the reaction diagram Show all sequences 3.5.4.19Zn2+ required for activity, zinc-metalloenzyme 667617
Results 1 - 5 of 5