Search Metals/Ions

2.4.1.10

Ca2+

activates both transfructosylation and hydrolytic activities

2.4.1.10

Ca2+

activates, recombinant enzyme

2.4.1.10

Ca2+

Ca2+ play an important structural role. At 45°C 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 40°C. In the absence of Ca2+ ions, the optimal temperature is 30°C; stimulates activity, Asp500 residues play an important role in Ca2+ binding

2.4.1.10

Ca2+

dependent on for tertiary structure, can partially be replaced by Sr2+, not Mg2+, Sr2+, Ba2+, and Mn2+

2.4.1.10

Ca2+

Mg2+, Zn2+, Mn2+, Fe2+ have no effect

2.4.1.10

Co2+

activates strongly, recombinant enzyme

2.4.1.10

Co2+

slightly activating

2.4.1.10

Fe2+

4fold increase in activity at 5 mM

2.4.1.10

Fe3+

dependent on for tertiary structure, can partially be replaced by Sr2+, not Mg2+, Ba2+, and Mn2+

2.4.1.10

Mg2+

activates both transfructosylation and hydrolytic activities