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 - 10 of 15 > >>
EC Number
Metals/Ions
Commentary
Reference
Ca2+
dependent on for tertiary structure, can partially be replaced by Sr2+, not Mg2+, Sr2+, Ba2+, and Mn2+
Fe3+
dependent on for tertiary structure, can partially be replaced by Sr2+, not Mg2+, Ba2+, and Mn2+
more
not affected by 5 mM of Ba2+, Zn2+, Hg2+, Ni2+, Mn2+, Cu2+, Co2+, Ca2+, Na2MoO4
Fe2+
4fold increase in activity at 5 mM
Co2+
slightly activating
Ca2+
Ca2+ play an important structural role. At 45C the mutant enzymes D500A and D500N are inactive in the absence of Ca2+ ions, with, respectively, 15% and 45% of wild-type activity remaining in the presence of 1 mM Ca2+. In the presence of 1 mM Ca2+ mutant enzymes display highest activity at 40C. In the absence of Ca2+ ions, the optimal temperature is 30C; stimulates activity, Asp500 residues play an important role in Ca2+ binding
Ca2+
Mg2+, Zn2+, Mn2+, Fe2+ have no effect
Mn2+
The transferase activity of levansucrase in the reaction mixture supplemented with Mn2+ is 100% higher than the enzyme activity in medium without metal ions, the hydrolytic activity of the levansucrase is lowered by 80%
more
enzyme activities of free and immobilized enzymes are not affected by Ca2+
MnCl2
22% activation of the immobilized enzyme at 0.1 mM, 30% activation at 0.1 mM of the free enzyme
Results 1 - 10 of 15 > >>