EC Number |
Metals/Ions |
Reference |
---|
4.6.1.18 | Cu2+ |
crystal structure |
134558 |
4.6.1.18 | Cu2+ |
enhance interaction with substrate but lower stability |
134521 |
4.6.1.18 | K+ |
increases activity |
134536 |
4.6.1.18 | K+ |
optimum activity at 30-50 mM |
134482 |
4.6.1.18 | more |
no effect of bivalent cations on enzyme |
677904 |
4.6.1.18 | Na+ |
increases activity |
134536 |
4.6.1.18 | Na+ |
NaCl: 0.1-0.25 M optimum concentration |
134538 |
4.6.1.18 | Ni2+ |
- |
134521 |
4.6.1.18 | Ni2+ |
binds the enzyme, crystal structure |
134558 |
4.6.1.18 | sulfate |
13 sulfate anions are identified in the electrondensity map of the two dimers in the asymmetric unit of the crystal, confirming that this ion plays a fundamental role in the crystallization process. Four sulfate ions are positioned at the active sites, as typically observed in several other members of the pancreatic-like superfamily, the remaining anions are located on positive patches of the rod surface |
728871 |