EC Number   |
Metals/Ions |
Reference |
|---|
   3.4.24.3 | Ca2+ |
4 g-atom Calcium per mol enzyme |
37101 |
| 3.4.24.3 | Ca2+ |
activates |
37101, 37102, 37105, 37110, 668044 |
| 3.4.24.3 | Ca2+ |
Ca-enzyme, alpha: 2.2, beta: 7.9, gamma: 3.1, delta: 3.0, epsilon: 4. 5, zeta: 6.5 mol Ca2+ per mol enzyme |
37096 |
| 3.4.24.3 | Ca2+ |
conformational change of the linker upon calcium binding in the structure of the collagen-binding domain with an N-terminal domain linker from class I collagenase |
655332 |
| 3.4.24.3 | Ca2+ |
interdomain flexibility and the domain arrangement of full-length collagenase H are reversibly regulated by Ca2+ |
733162 |
| 3.4.24.3 | Ca2+ |
required for stability and activity |
37092 |
| 3.4.24.3 | Ca2+ |
the presence of Ca2+ alters the collagen-binding domain enzyme structure upon collagen binding from beta-sandwich to alpha-helix |
753478 |
| 3.4.24.3 | Calcium |
binding of calcium ions triggers the formation of a cis peptide bond in the collagen-binding domain. The calcium ions not only stabilize the cis peptide bond thermodynamically but also catalyze its formation. The free energy barrier to the formation of the cis peptide bond decreases from 21.4 kcal/mol in the absence of calciumions to 10.3 kcal/mol in their presence. The calcium ions electrostatically stabilize the lone pair on the nitrogen atom that forms during the isomerization. Their attraction to acidic amino acid side chains and formation of a hydrogen bond network constrain the peptide backbone in a way that makes it easier for the nitrogen to pyramidalize |
717249 |
| 3.4.24.3 | Co2+ |
activates at low concentration, inhibits at high concentration |
37101 |
| 3.4.24.3 | Li+ |
activates |
668044 |
