The enzyme catalyzes the deamination of cytidine or deoxycytidine to form uridine or deoxyuridine. It is a zinc-dependent enzyme (PMID16784234).
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| ZN 296 x | ZN | zinc | zinc | mononuclear | Increases acidity Increases nucleophilicity Coordinates substrate |
*It refers to the MACiE reference pdb: 1ctt
| Metal/s Properties in Resting State | ||||||
| ZN 296 x | Resting state enzyme (1r5t) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | tetrahedral | |||||
| Coordination Number | 4 | |||||
| Notes | - | |||||
| References |
| -Xiang S, Short SA, Wolfenden R, Carter CW Jr The structure of the cytidine deaminase-product complex provides evidence for efficient proton transfer and ground-state destabilization. Biochemistry. 1997 Apr 22;36(16):4768-74.(MEDLINE:9125497) |
| - Some information have been also deduced from the MACiE mechanism model |