Enzymes
| UniProtKB help_outline | 1,047 proteins |
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- Name help_outline (R)-S-lactoylglutathione Identifier CHEBI:57474 Charge -1 Formula C13H20N3O8S InChIKeyhelp_outline VDYDCVUWILIYQF-CSMHCCOUSA-M SMILEShelp_outline C[C@@H](O)C(=O)SC[C@H](NC(=O)CC[C@H]([NH3+])C([O-])=O)C(=O)NCC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,264 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (R)-lactate Identifier CHEBI:16004 Charge -1 Formula C3H5O3 InChIKeyhelp_outline JVTAAEKCZFNVCJ-UWTATZPHSA-M SMILEShelp_outline C[C@@H](O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 23 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline glutathione Identifier CHEBI:57925 Charge -1 Formula C10H16N3O6S InChIKeyhelp_outline RWSXRVCMGQZWBV-WDSKDSINSA-M SMILEShelp_outline [NH3+][C@@H](CCC(=O)N[C@@H](CS)C(=O)NCC(=O)[O-])C(=O)[O-] 2D coordinates Mol file for the small molecule Search links Involved in 104 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,521 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:25245 | RHEA:25246 | RHEA:25247 | RHEA:25248 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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Preparation and assay of glutathione thiol esters. Survey of human liver glutathione thiol esterases.
Uotila L.
Biochemistry 12:3938-3943(1973) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.
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Deciphering the role of the type II glyoxalase isoenzyme YcbL (GlxII-2) in Escherichia coli.
Reiger M., Lassak J., Jung K.
In Escherichia coli, detoxification of methylglyoxal (MG) requires glyoxalases I and II. Glyoxalase I (gloA/GlxI) isomerizes the hemithioacetal, formed spontaneously from MG and glutathione (GSH) to S-lactoylglutathione (SLG), which is hydrolyzed by glyoxalase II (gloB/GlxII) to lactate and GSH. Y ... >> More
In Escherichia coli, detoxification of methylglyoxal (MG) requires glyoxalases I and II. Glyoxalase I (gloA/GlxI) isomerizes the hemithioacetal, formed spontaneously from MG and glutathione (GSH) to S-lactoylglutathione (SLG), which is hydrolyzed by glyoxalase II (gloB/GlxII) to lactate and GSH. YcbL from Salmonella enterica serovar Typhimurium is an unusual type II glyoxalase whose role in MG detoxification has remained enigmatic. Here we show that YcbL (gloC/GlxII-2) acts as an accessory type II glyoxylase in E. coli. The two isoenzymes have additive effects and ensure maximal MG degradation. << Less
FEMS Microbiol. Lett. 362:1-7(2015) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Purification and characterization of S-2-hydroxyacylglutathione hydrolase (glyoxalase II) from human liver.
Uotila L.
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Escherichia coli glyoxalase II is a binuclear zinc-dependent metalloenzyme.
O'Young J., Sukdeo N., Honek J.F.
Cytotoxic methylglyoxal is detoxified by the two-enzyme glyoxalase system. Glyoxalase I (GlxI) catalyzes conversion of non-enzymatically produced methylglyoxal-glutathione hemithioacetal into its corresponding thioester. Glyoxalase II (Glx II) hydrolyzes the thioester into d-lactate and free gluta ... >> More
Cytotoxic methylglyoxal is detoxified by the two-enzyme glyoxalase system. Glyoxalase I (GlxI) catalyzes conversion of non-enzymatically produced methylglyoxal-glutathione hemithioacetal into its corresponding thioester. Glyoxalase II (Glx II) hydrolyzes the thioester into d-lactate and free glutathione. Glyoxalase I and II are metalloenzymes, which possess mononuclear and binuclear active sites, respectively. There are two distinct classes of GlxI; the first class is Zn2+-dependent and is composed of GlxI from mainly eukaryotic organisms and the second class is composed of non-Zn2+-dependent (but Ni2+ or Co2+-dependent) GlxI enzymes (mainly prokaryotic and leishmanial species). GlxII is typically Zn2+-activated, containing Zn2+ and either Fe3+/Fe2+ or Mn2+ at the active site depending upon the biological source. To address whether two classes of GlxII might exist, glyoxalase II from Escherichia coli was cloned and overexpressed and characterized. Unlike E. coli GlxI, which is non-Zn2+-dependent, Zn2+ activates the E. coli GlxII enzyme, with no evidence for Ni2+ metal utilization. << Less
Arch. Biochem. Biophys. 459:20-26(2007) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.
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Spectrophotometric measurements of the metabolic formation and degradation of thiol esters and enediol compounds.
RACKER E.