EC number:3.1.2.6
| ID: | 3.1.2.6 |
|---|---|
| Description: | Hydroxyacylglutathione hydrolase. |
| Alternative Name: |
Glyoxalase II. |
| Cath: | 3.40.50.880; 3.60.15.10; |
3D structure
Click one PDB to see exact 3D structure provided by NGL.
Note: Use your mouse to drag, rotate, and zoom in and out of the structure. Mouse-over to identify atoms and bonds. Mouse controls documentation.References
External Links
| UniProtKB Enzyme Link: | UniProtKB 3.1.2.6 |
| BRENDA Enzyme Link: | BRENDA 3.1.2.6 |
| KEGG Enzyme Link: | KEGG3.1.2.6 |
| BioCyc Enzyme Link: | BioCyc 3.1.2.6 |
| ExPASy Enzyme Link: | ExPASy3.1.2.6 |
| EC2PDB Enzyme Link: | EC2PDB 3.1.2.6 |
| ExplorEnz Enzyme Link: | ExplorEnz 3.1.2.6 |
| PRIAM enzyme-specific profiles Link: | PRIAM 3.1.2.6 |
| IntEnz Enzyme Link: | IntEnz 3.1.2.6 |
| MEDLINE Enzyme Link: | MEDLINE 3.1.2.6 |
| RHEA:25245 | (R)-S-lactoylglutathione + H2O = (R)-lactate + glutathione + H(+) |
| RULE(radius=1) | [*:1]-[S;H0;+0:2]-[C;H0;+0:3](=[*:4])-[*:5].[OH2;+0:6]>>[*:1]-[SH;+0:2].[*:4]=[C;H0;+0:3](-[*:5])-[OH;+0:6] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Purification and characterization of S-2-hydroxyacylglutathione hydrolase (glyoxalase II) from human liver. | Uotila L | 1973 Sep 25 | 4745654 |
| Preparation and assay of glutathione thiol esters. Survey of human liver glutathione thiol esterases. | Uotila L | 1973 Sep 25 | 4200890 |
| Deciphering the role of the type II glyoxalase isoenzyme YcbL (GlxII-2) in Escherichia coli. | Reiger M, Lassak J, Jung K | 2015 Jan | 25670698 |
| Escherichia coli glyoxalase II is a binuclear zinc-dependent metalloenzyme. | O'Young J, Sukdeo N, Honek JF | 2007 Mar 1 | 17196158 |
| Spectrophotometric measurements of the metabolic formation and degradation of thiol esters and enediol compounds. | RACKER E | 1952 Nov | 13032160 |
| RHEA:21864 | an S-(2-hydroxyacyl)glutathione + H2O = a 2-hydroxy carboxylate + glutathione + H(+) |
| RULE(radius=1) | [*:1]-[C;H0;+0:2](=[*:3])-[S;H0;+0:4]-[*:5].[OH2;+0:6]>>[*:1]-[C;H0;+0:2](=[*:3])-[OH;+0:6].[*:5]-[SH;+0:4] |
| Reaction |  |
| Core-to-Core | No scaffolds atoms were exchanged as a result of the reaction |
References
| Title | Authors | Date | PubMed ID |
|---|---|---|---|
| Deciphering the role of the type II glyoxalase isoenzyme YcbL (GlxII-2) in Escherichia coli. | Reiger M, Lassak J, Jung K | 2015 Jan | 25670698 |
| The metal ion requirements of Arabidopsis thaliana Glx2-2 for catalytic activity. | Limphong P, McKinney RM, Adams NE, Makaroff CA, Bennett B, Crowder MW | 2010 Feb | 19834746 |
| Escherichia coli glyoxalase II is a binuclear zinc-dependent metalloenzyme. | O'Young J, Sukdeo N, Honek JF | 2007 Mar 1 | 17196158 |
| Structural studies on a mitochondrial glyoxalase II. | Marasinghe GP, Sander IM, Bennett B, Periyannan G, Yang KW, Makaroff CA, Crowder MW | 2005 Dec 9 | 16227621 |
| Arabidopsis glyoxalase II contains a zinc/iron binuclear metal center that is essential for substrate binding and catalysis. | Zang TM, Hollman DA, Crawford PA, Crowder MW, Makaroff CA | 2001 Feb 16 | 11085979 |