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 and M0258 entries) to effect beta-lactam cleavage (PMID10508665). This hit refers to L1 metallo-beta-lactamase from Stenotrophomonas maltophilia which is a unique example among beta-lactamases in that it is tetrameric.
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| ZN 270 A | ZN | zinc | zinc | dinuclear | Coordinates substrate Increases nucleophilicity Electrostatic stabiliser Increases acidity |
| ZN 271 A | ZN | zinc | zinc | dinuclear | Coordinates substrate Increases nucleophilicity Electrostatic stabiliser Increases acidity |
*It refers to the MACiE reference pdb: 1sml
| Metal/s Properties in Resting State | ||||||
| ZN 270 A | Resting state enzyme (1sml) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | trigonalBipyramidal | |||||
| Coordination Number | 5 | |||||
| Notes | - | |||||
| ZN 271 A | Resting state enzyme (1sml) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | tetrahedral | |||||
| Coordination Number | 4 | |||||
| Notes | - | |||||
| References |
| -Ullah JH, Walsh TR, Taylor IA, Emery DC, Verma CS, Gamblin SJ, Spencer J The crystal structure of the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia at 1.7 A resolution. J Mol Biol. 1998 Nov 20;284(1):125-36.(MEDLINE:9811546) |