The enzyme catalyzes the hydrolysis of S-D-lactoylglutathione to form glutathione and D-lactic acid. It uses a dinuclear zinc-binding site to perform the catalysis (PMID10508780).
CATALYTIC METAL(S)
| Metal/Site Information | |||||
| Residue in MACiE* | Atom in MACiE* | Residue Type in MACiE | Physiological Metal |
Site Type |
Function(s) |
| ZN 261 A | ZN | zinc | zinc | dinuclear | Coordinates substrate Increases nucleophilicity Increases acidity |
| ZN 262 A | ZN | zinc | zinc | dinuclear | Coordinates substrate Increases nucleophilicity Increases acidity |
*It refers to the MACiE reference pdb: 1qh5
| Metal/s Properties in Resting State | ||||||
| ZN 261 A | Resting state enzyme (-) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | unknownGeometry | |||||
| Coordination Number | unknown | |||||
| Notes | - | |||||
| ZN 262 A | Resting state enzyme (-) | |||||
| Oxidation State | 2 | |||||
| Coordination Geometry | unknownGeometry | |||||
| Coordination Number | unknown | |||||
| Notes | - | |||||
| References |
| -Cameron AD, Ridderström M, Olin B, Mannervik B Crystal structure of human glyoxalase II and its complex with a glutathione thiolester substrate analogue. Structure. 1999 Sep 15;7(9):1067-78.(MEDLINE:10508780) |
| - Some information have been also deduced from the MACiE mechanism model |