EC Number |
Metals/Ions |
Reference |
---|
3.5.1.23 | Ba2+ |
better activator than Mg2+ |
657260 |
3.5.1.23 | Ca2+ |
- |
680936, 696396, 699000 |
3.5.1.23 | Ca2+ |
a calcium or magnesium ion is presumed to be important for stabilizing the two domains |
733408 |
3.5.1.23 | Ca2+ |
ACER isoform activities are enhanced by Ca2+ |
719197 |
3.5.1.23 | Ca2+ |
ACER3 has a catalytic Zn2+ binding site in its core and a Ca2+ binding site physically and functionally connected to the Zn2+, two residues appear to play critical roles in physically linking the Ca2+ and the Zn2+ sites, W20 and E33. E33 carboxylate interacts with the Ca2+ ion and is in close proximity to H81TM2 side chain, while H81TM2 coordinates the Zn2+, Ca2+-binding site within the N-terminus, structure overview. The Ca2+ ion is coordinated by six oxygens from the D19 carboxylate (bidentate), the W20 backbone carbonyl, the E22 backbone carbonyl, the N24 side chain carbonyl, and the E33 carboxylate (monodentate) |
754856 |
3.5.1.23 | Ca2+ |
activates |
667523, 733984, 755487 |
3.5.1.23 | Ca2+ |
activates, required by ACER2 for both its in vitro and cellular activities. Cellular ACER2 activity is inhibited by depletion of Ca2+ from Golgi lumen |
712496 |
3.5.1.23 | Ca2+ |
after EDTA treatment, Ca2+ reestablishes activity completely |
171990 |
3.5.1.23 | Ca2+ |
Ca2+-dependent, better activator than Mg2+ |
657260 |
3.5.1.23 | Ca2+ |
enhances activity |
700748 |