The enzyme catalyzes the hydrolysis of the C-N bond in beta-lactam compounds determining the inactivation of such antibiotics. Members of the beta-lactamase family have been grouped into four classes (A, B, C, D). Class B members employ either one (see M0016 entry) or two zinc ions in a dinuclear site (see M0015 entry) to effect beta-lactam cleavage (PMID10508665).
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| ZN 2 A | ZN | zinc | zinc | mononuclear | Coordinates substrate Increases electrophilicity Electrostatic stabiliser |
*It refers to the MACiE reference pdb: 1bc2
| Metal/s Properties in Resting State | ||||||
| ZN 2 A | Resting state enzyme (1x8g) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | tetrahedral | |||||
| Coordination Number | 4 | |||||
| Notes | - | |||||
| References |
| -Garau G, Bebrone C, Anne C, Galleni M, Frère JM, Dideberg O A metallo-beta-lactamase enzyme in action: crystal structures of the monozinc carbapenemase CphA and its complex with biapenem. J Mol Biol. 2005 Jan 28;345(4):785-95.(MEDLINE:15588826) |
| - Some information have been also deduced from the MACiE mechanism model |