The enzyme catalyzes the Ca2+-dependent hydrolysis of both DNA and RNA at the 5 position of the phosphodiester bond yielding a free 5-hydroxyl group and a 3-phosphate monoester (PMID288045).
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| CA 1 x | CA | calcium | calcium | mononuclear | Coordinates substrate Increases electrophilicity Electrostatic stabiliser |
*It refers to the MACiE reference pdb: 2sns
| Metal/s Properties in Resting State | ||||||
| CA 1 x | Resting state enzyme (1ena) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | unknownGeometry | |||||
| Coordination Number | 5 | |||||
| Notes | - | |||||
| References |
| -Cotton FA, Hazen EE Jr, Legg MJ Staphylococcal nuclease: proposed mechanism of action based on structure of enzyme-thymidine 3',5'-bisphosphate-calcium ion complex at 1.5-A resolution. Proc Natl Acad Sci U S A. 1979 Jun;76(6):2551-5.(MEDLINE:288045) |
| - Some information have been also deduced from the MACiE mechanism model |