4.4.1.5: lactoylglutathione lyase
This is an abbreviated version!
For detailed information about lactoylglutathione lyase, go to the full flat file.
Word Map on EC 4.4.1.5
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4.4.1.5
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glycation
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detoxify
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gsh
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dicarbonyls
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erythrocyte
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d-lactate
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adduct
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dismutase
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endproducts
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rage
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s-transferase
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mellitus
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methylglyoxal-induced
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glyoxalases
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byproduct
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hyperglycemia
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glutathione-dependent
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phosphoglucomutase
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metalloenzyme
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hemithioacetal
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mg-induced
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hla-a
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aldose
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3-deoxyglucosone
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enediolate
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d-lactic
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pentosidine
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cyclopentyl
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mdhar
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haptoglobin
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aminoguanidine
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diesters
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monodehydroascorbate
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6-phosphogluconate
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anti-glycation
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dehydroascorbate
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anxiety-like
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gsh-dependent
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pyridoxamine
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analysis
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trypanothione
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medicine
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drug development
- 4.4.1.5
-
glycation
-
detoxify
- gsh
-
dicarbonyls
- erythrocyte
- d-lactate
- adduct
- dismutase
-
endproducts
- rage
- s-transferase
- mellitus
-
methylglyoxal-induced
-
glyoxalases
-
byproduct
- hyperglycemia
-
glutathione-dependent
- phosphoglucomutase
-
metalloenzyme
- hemithioacetal
-
mg-induced
- hla-a
- aldose
- 3-deoxyglucosone
-
enediolate
-
d-lactic
-
pentosidine
-
cyclopentyl
- mdhar
- haptoglobin
- aminoguanidine
- diesters
- monodehydroascorbate
- 6-phosphogluconate
-
anti-glycation
- dehydroascorbate
-
anxiety-like
-
gsh-dependent
- pyridoxamine
- analysis
- trypanothione
- medicine
- drug development
Reaction
Synonyms
aldoketomutase, CLO GlxI, Glb33, GLI, GLO I, GLO-1, GLO-I, Glo1, GloA, GloA1, GloA2, GloA3, GloI, Glx I, Glx-I, Glx1, GLXI, Gly I, gly-I, GLY1, glyoxalase 1, glyoxalase I, glyoxalase-1, glyoxalase-I, glyoxylase I, GmGlyox I, ketone-aldehyde mutase, lactoylglutathione lyase, lactoylglutathione methylglyoxal lyase, LGL, lyase, lactoylglutathione, methylglyoxalase, methylglyoxylase, OsGLYI-11.2, PfGlx I, rhGLO I, S-D-lactoylglutathione methylglyoxal lyase, S-D-lactoylglutathione methylglyoxal lyase (isomerizing), S-D-lactoylglutathione:methylglyoxal lyase, SpGlo1, STM3117, YaiA
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Application
Application on EC 4.4.1.5 - lactoylglutathione lyase
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analysis
drug development
medicine
additional information
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practical experiments for students to determine the effect of exposure to oxidative stress conditions on yeast glyoxalase I, investigation of kinetic parameters
analysis
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flow cytometry method for GLO-1 detection in human leukocytes isolated from peripheral blood samples to investigate GLO-1 expression in leukocyte subsets from type 1 and 2 diabetes mellitus patients. Expression index of GLO-1-positive cells is slightly increased in mononuclear leukocytes from diabetic patients. This result correlates with the increase in GLO-1 activity in the whole blood samples of type 2 diabetes patients
difference of the substrate specificity of the human and the Leishmania enzyme could be used for designing selective inhibitors against the parasite
drug development
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beta-ketoesters function as a possible zinc-chelating component of Glx-I inhibitors
drug development
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design of a metabolically stable glyoxalase-I inhibitor, which may be useful in potentiating the antitumor activity of alpha-ketoaldehydes
drug development
mutually exclusive substrate specificities and substantial differences between the active sites of the Leishmania major and human GLO1 enzymes indicate that selective inhibition of LmGLO1 may be possible
drug development
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cancer therapy, inhibitors of the glyoxalase system would be expected to suppress the growth of cancer cells and could find clinical use as anticancer drug
drug development
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the enzyme is a promising drug target, since the functional monomeric Glo1 from Plasmodium falciparum differs significantly from its human homologue
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decrease of glyoxalase I expression with increasing Alzheimers disease stage might be one reason for methylglyoxal-induced neuronal impairment, apoptosis, and advanced glycation end formation in plaques and tangles
medicine
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glyoxalase I is critical for pericyte survival under hyperglycemic conditions, its inactivation and/or down-regulation by NO donor may contribute to pericyte death by apoptosis during early stages of diabetic retinopathy
medicine
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high degree of similarity between the trypanosomatid and bacterial GLO1 proteins, contrasting substrate specificities of human and trypanosomatid glyoxalase enzymes suggest that the glyoxalase system may be an attractive target for anti-trypanosomal chemotherapy
medicine
possible role of glyoxalase I in the chemoresistance displayed by kidney tumor, possible use of glyoxalase I inhibitors as anticancer drugs, increase in glyoxalase I lowers level of the potent apoptosis activator methylglyoxal
medicine
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role in dental caries, LGL functions in the detoxification of methylglyoxal, resulting in increased aciduricity
medicine
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upregulation of glyoxalase I in diabetes, this upregulation is inadequate to normalize methylglyoxal levels, which can lead to methylglyoxal retention and chemical modification of proteins
medicine
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Glo-I is a molecular target for treatment of Bcr-Abl+ leukemias and, in particular, Abl TKI-resistant quiescent Bcr-Abl+ leukemic cells that have acquired stem-like characteristics in the process of adapting to a hypoxic environment
medicine
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polymorphisms in glyoxalase 1 gene are not associated with the prevalence of hypertension, markers of atherosclerosis and advanced glycation endproducts and are weakly associated with pulse pressure and systolic blood pressure, impaired glucose metabolism and type 2 diabetes mellitus
medicine
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flow cytometry method for GLO-1 detection in human leukocytes isolated from peripheral blood samples to investigate GLO-1 expression in leukocyte subsets from type 1 and 2 diabetes mellitus patients. Expression index of GLO-1-positive cells is slightly increased in mononuclear leukocytes from diabetic patients. This result correlates with the increase in GLO-1 activity in the whole blood samples of type 2 diabetes patients
medicine
treatment of HL-60 cells leads to significant accumulation of substrate methylglyoxal and the caspase 3 activity of the cell lysate increases. Compound shows anti-proliferative activity against HL-60 cells
medicine
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role in dental caries, LGL functions in the detoxification of methylglyoxal, resulting in increased aciduricity
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GloI has two functional active sites with similar catalytic activities and pH profiles but different substrate affinities. Glu91/Glu272 and Glu345/Glu161 are isofunctional to Glu99 and Glu172 in human GloI, respectively. As a consequence, Glu91 and Glu345 are part of active site A between the N- and C-terminal domains, and Glu272 and Glu161 form active site B between the intermediate domains. Both active sites are able to adopt two different conformations and are allosterically coupled
additional information
Pseudomonas aeruginosa possesses GlxI enzymes from two metal activation classes. The gloA1 and gloA2 genes encode non-Zn2+ dependent glyoxalase I enzymes and the gloA3 gene encodes a Zn2+-dependent homolog
additional information
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Pseudomonas aeruginosa possesses GlxI enzymes from two metal activation classes. The gloA1 and gloA2 genes encode non-Zn2+ dependent glyoxalase I enzymes and the gloA3 gene encodes a Zn2+-dependent homolog
additional information
compared to control cells, transgenic cells with Pseudomonas putida glyoxalase I display a significant reduction of 35-43% in intracellular methylglyoxal and a significant decrease of 30% in extracellular methylglyoxal. Expression of Pseudomonas putida glyoxalase I in transgenic Escherichia coli markedly improves cell growth and results in a 50% increase in 1,3-propanediol production
additional information
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compared to control cells, transgenic cells with Pseudomonas putida glyoxalase I display a significant reduction of 35-43% in intracellular methylglyoxal and a significant decrease of 30% in extracellular methylglyoxal. Expression of Pseudomonas putida glyoxalase I in transgenic Escherichia coli markedly improves cell growth and results in a 50% increase in 1,3-propanediol production
additional information
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is able to exist in two alternative domain-swapped forms. Active site and an essential metal binding site are disassembled and reassembled by the process of domain swapping. 3D domain swapping can be regulated by a small organic ligand