The enzyme catalyzes the hydrolysis of beta-aspartyl dipeptides. It binds two divalent metal ions in a dinuclear site (PMID15882050).
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| ZN 800 x | ZN | zinc | divalent cation | dinuclear | Coordinates substrate Increases nucleophilicity Increases electrophilicity |
| ZN 801 x | ZN | zinc | divalent cation | dinuclear | Coordinates substrate Increases nucleophilicity |
*It refers to the MACiE reference pdb: 1onw
| Metal/s Properties in Resting State | ||||||
| ZN 800 x | Resting state enzyme (1onw) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | trigonalBipyramidal | |||||
| Coordination Number | 5 | |||||
| Notes | - | |||||
| ZN 801 x | Resting state enzyme (1onw) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | tetrahedral | |||||
| Coordination Number | 4 | |||||
| Notes | - | |||||
| References |
| -MartÃ-Arbona R, Fresquet V, Thoden JB, Davis ML, Holden HM, Raushel FM Mechanism of the reaction catalyzed by isoaspartyl dipeptidase from Escherichia coli. Biochemistry. 2005 May 17;44(19):7115-24.(MEDLINE:15882050) |