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Hydroxyacylglutathione hydrolase

glyoxalase II, GLO2, HAGH
The enzyme encoded by this gene is classified as a thiolesterase and is responsible for the hydrolysis of S-lactoyl-glutathione to reduced glutathione and D-lactate. Two transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Apr 2010] (from NCBI)
Top mentioned proteins: Lactoylglutathione Lyase, ACID, CAN, HAD, catalase
Papers on glyoxalase II
Promiscuous metallo-β-lactamases: MIM-1 and MIM-2 may play an essential role in quorum sensing networks.
Mitić et al., Ireland. In J Inorg Biochem, Jan 2016
Although both sequence comparison and homology modeling indicate that these proteins are homologous to well-known MBLs such as AIM-1, the sequence analysis also indicated that MIM-1 and MIM-2 share similarities with N-acyl homoserine lactonases (AHLases) and glyoxalase II (GLX-II).
Methylglyoxal, the foe and friend of glyoxalase and Trx/TrxR systems in HT22 nerve cells.
Maher et al., Florianópolis, Brazil. In Free Radic Biol Med, Dec 2015
At low concentrations of MGO (0.3mM), GLO2 is strongly induced, but at high MGO (0.75mM) concentrations, GLO1 is inhibited and GLO2 is downregulated.
Presence of unique glyoxalase III proteins in plants indicates the existence of shorter route for methylglyoxal detoxification.
Singla-Pareek et al., New Delhi, India. In Sci Rep, Dec 2015
Glyoxalase pathway, comprising glyoxalase I (GLY I) and glyoxalase II (GLY II) enzymes, is the major pathway for detoxification of methylglyoxal (MG) into D-lactate involving reduced glutathione (GSH).
Inhibitory Effect of Isoflavones from Erythrina poeppigiana on the Growth of HL-60 Human Leukemia Cells through Inhibition of Glyoxalase I.
Kaneda et al., In Nat Prod Commun, Sep 2015
GLO I catalyzes the reaction to transform hemimercaptal, a compound formed from methylglyoxal (MG) and reduced glutathione, into S-D-lactoylglutathione, which is then converted to D-lactic acid by glyoxalase II.
High glucose, glucose fluctuation and carbonyl stress enhance brain microvascular endothelial barrier dysfunction: Implications for diabetic cerebral microvasculature.
Aw et al., Shreveport, United States. In Redox Biol, Aug 2015
Significantly, glyoxalase II activity was attenuated in hyperglycemic cells.
Glutathione-induced drought stress tolerance in mung bean: coordinated roles of the antioxidant defence and methylglyoxal detoxification systems.
Fujita et al., Dhaka, Bangladesh. In Aob Plants, 2014
The activities of glyoxalase I (Gly I) and glyoxalase II (Gly II) increased due to drought stress.
Improved Salinity Tolerance in Carrizo Citrange Rootstock through Overexpression of Glyoxalase System Genes.
Arce-Johnson et al., Santiago, Chile. In Biomed Res Int, 2014
To improve salinity tolerance, transgenic Carrizo citrange rootstocks that overexpress glyoxalase I and glyoxalase II genes were obtained and their salt stress tolerance was evaluated.
Glyoxalase II promotes "in vitro" S-glutathionylation.
Armeni et al., Ancona, Italy. In Free Radic Biol Med, 2014
S-glutathionylation involves the reversible formation of a mix disulphide-bridge between specific cysteine and a molecule of glutathione, the major non-protein antioxidant compound in the cell.
Glyoxalase diversity in parasitic protists.
Deponte, Heidelberg, Germany. In Biochem Soc Trans, 2014
Our current knowledge of the isomerase glyoxalase I and the thioesterase glyoxalase II is based on a variety of prokaryotic and eukaryotic (model) systems with an emphasis on human glyoxalases.
Activity, regulation, copy number and function in the glyoxalase system.
Thornalley et al., Coventry, United Kingdom. In Biochem Soc Trans, 2014
The human Glo2 gene, HAGH (hydroxyacylglutathione hydrolase), has a regulatory p53-response element.
Prevention of dicarbonyl-mediated advanced glycation by glyoxalases: implication in skin aging.
Petropoulos et al., Saint-Jean-de-Braye, France. In Biochem Soc Trans, 2014
These compounds can be detoxified by the glyoxalase system composed of two enzymes, Glo1 (glyoxalase I) and Glo2 (glyoxalase II).
The glyoxalase pathway in protozoan parasites.
Cordeiro et al., Lisbon, Portugal. In Int J Med Microbiol, 2012
This pathway includes two enzymes, glyoxalase I and glyoxalase II, which convert methylglyoxal to d-lactate by using glutathione as a catalytic cofactor.
Role of advanced glycation endproducts and glyoxalase I in diabetic peripheral sensory neuropathy.
Wright et al., Kansas City, United States. In Transl Res, 2012
The glyoxalase system, composed of the enzymes glyoxalase I (GLO1) and glyoxalase II, is the main detoxification pathway involved in breaking down toxic reactive dicarbonyls before producing carbonyl stress and forming AGEs on proteins, lipids, or nucleic acids.
Human glyoxalase II contains an Fe(II)Zn(II) center but is active as a mononuclear Zn(II) enzyme.
Crowder et al., Oxford, United States. In Biochemistry, 2009
Human glyoxalase II contains an Fe(II)Zn(II) center but is active as a mononuclear Zn(II) enzyme
Alteration of glyoxalase genes expression in response to testosterone in LNCaP and PC3 human prostate cancer cells.
Mearini et al., Perugia, Italy. In Cancer Biol Ther, 2007
In androgen-dependent prostate cancer cells, testosterone upregulates GLO2 mRNA levels. In androgen-independent prostate cancer cells, it downregulates GLO2 mRNA.
Glyoxalase II, a detoxifying enzyme of glycolysis byproduct methylglyoxal and a target of p63 and p73, is a pro-survival factor of the p53 family.
Chen et al., Birmingham, United States. In J Biol Chem, 2006
Data show that the GLX2 gene, which encodes glyoxalase II enzyme, is up-regulated by p63 and p73.
Overexpression of glyoxalase system enzymes in human kidney tumor.
Mearini et al., Perugia, Italy. In Cancer J, 2006
Overexpression of glyoxalase II is associated with kidney tumor
Design and evolution of new catalytic activity with an existing protein scaffold.
Kim et al., Taejŏn, South Korea. In Science, 2006
Using this approach, we were able to introduce beta-lactamase activity into the alphabeta/betaalpha metallohydrolase scaffold of glyoxalase II.
The Human hydroxyacylglutathione hydrolase (HAGH) gene encodes both cytosolic and mitochondrial forms of glyoxalase II.
Pease et al., Leeds, United Kingdom. In J Biol Chem, 2004
hydroxyacylglutathione hydrolase (HAGH) gene encodes both cytosolic and mitochondrial forms of glyoxalase II
Major-histocompatibility-complex extended haplotypes in membranoproliferative glomerulonephritis.
West et al., In N Engl J Med, 1986
The extended haplotype HLA-B8,DR3,SC01,GLO2(glyoxalase I 2) was observed in 9 of 68 disease-associated haplotypes (13 percent), but in only 3 of 205 controls (1 percent) (relative risk, 14.79; P less than 0.001).
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