The enzyme catalyse the hydrolysis of dipeptides. It is an homodimer and each subunit binds two zinc ions in a dinuclear site (PMID12144777)
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| ZN 401 A | ZN | zinc | zinc | dinuclear | Increases acidity Coordinates substrate Increases nucleophilicity |
| ZN 402 A | ZN | zinc | zinc | dinuclear | Coordinates substrate Increases acidity Increases nucleophilicity |
*It refers to the MACiE reference pdb: 1itq
| Metal/s Properties in Resting State | ||||||
| ZN 401 A | Resting state enzyme (1itq) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | trigonalBipyramidal | |||||
| Coordination Number | 6 | |||||
| Notes | - | |||||
| ZN 402 A | Resting state enzyme (1itq) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | trigonalBipyramidal | |||||
| Coordination Number | 5 | |||||
| Notes | - | |||||
| References |
| -Nitanai Y, Satow Y, Adachi H, Tsujimoto M Crystal structure of human renal dipeptidase involved in beta-lactam hydrolysis. J Mol Biol. 2002 Aug 9;321(2):177-84.(MEDLINE:12144777) |
| - Some information have been also deduced from the MACiE mechanism model |