EC Number   |
Metals/Ions |
Reference |
|---|
   3.7.1.24 | Co2+ |
specifically and significantly activates the enzyme, shows a hyperbolic saturation curve in the micromolar range, binding to the enzyme might induce a conformational change that increases the catalytic effect of Zn2+ or might forma a distinct catalytic site besides that for Zn2+ |
733528 |
| 3.7.1.24 | more |
the enzyme has a 168HXHXD172 metal binding motif. Poor effects on enzyme activity by Ca2+, Ni2+, Fe3+, Zn2+, and Mg2+ |
733528 |
| 3.7.1.24 | Zn2+ |
a zinc hydrolase, located at the bottom of a deep narrow pocket of the enzyme molecule, coordinated by H129, E160, H270, and E274 |
733528 |
| 3.7.1.24 | Zn2+ |
a Zn-dependent C-C hydrolase, bound in the active site, chelated by four amino acid side-chains, His270, His129, Glu274 and Glu160, might also have structural role in Phlg |
735304 |
| 3.7.1.24 | Zn2+ |
a Zn-dependent C-C hydrolase, the metal ion may play an essential role in catalysis and is identified as bound inside the hydrophobic/amphiphilic pocket, coordinated by His129(beta5), Glu160(beta6), His270(alpha10), Glu274(alpha10), and a water molecule with pentagonal bipyramidal coordination geometry. It may play an important structural role in stabilizing the PhlG catalytic domain by holding the strands beta5 and beta6 and the helix alpha10 together |
734165 |
| 3.7.1.24 | Zn2+ |
dependent on |
752294 |
