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
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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
ECTree
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General Information
General Information on EC 4.4.1.5 - lactoylglutathione lyase
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evolution
malfunction
metabolism
physiological function
additional information
homology-based structural modeling, overview
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evolutionary early prokaryotic gene transfer. The enzyme of kinetoplastid parasites has highly altered substrate-binding site due to the usage of trypanothione instead of glutathione. Trypanothione is entropically favoured in comparison with the formation of glutathione disulfide. In addition, trypanothione is more reactive because of a significantly lower thiol pKa value of 7.4, has an overall positive instead of negative charge and is much bulkier than GSH. Because of the spermidine moiety, the substrate-binding sites are partially neutral or negatively (instead of positively) charged, and the binding sites of kinetoplastid glyoxalases are much wider to accommodate the additional spermidine and second glutathione moiety
evolution
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evolutionary early prokaryotic gene transfer. The enzyme of kinetoplastid parasites has highly altered substrate-binding site due to the usage of trypanothione instead of glutathione. Trypanothione is entropically favoured in comparison with the formation of glutathione disulfide. In addition, trypanothione is more reactive because of a significantly lower thiol pKa value of 7.4, has an overall positive instead of negative charge and is much bulkier than GSH. Because of the spermidine moiety, the substrate-binding sites are partially neutral or negatively (instead of positively) charged, and the binding sites of kinetoplastid glyoxalases are much wider to accommodate the additional spermidine and second glutathione moiety
evolution
-
evolutionary early prokaryotic gene transfer. The enzyme of kinetoplastid parasites has highly altered substrate-binding site due to the usage of trypanothione instead of glutathione. Trypanothione is entropically favoured in comparison with the formation of glutathione disulfide. In addition, trypanothione is more reactive because of a significantly lower thiol pKa value of 7.4, has an overall positive instead of negative charge and is much bulkier than GSH. Because of the spermidine moiety, the substrate-binding sites are partially neutral or negatively (instead of positively) charged, and the binding sites of kinetoplastid glyoxalases are much wider to accommodate the additional spermidine and second glutathione moiety
evolution
-
evolutionary early prokaryotic gene transfer. The enzyme of kinetoplastid parasites has highly altered substrate-binding site due to the usage of trypanothione instead of glutathione. Trypanothione is entropically favoured in comparison with the formation of glutathione disulfide. In addition, trypanothione is more reactive because of a significantly lower thiol pKa value of 7.4, has an overall positive instead of negative charge and is much bulkier than GSH. Because of the spermidine moiety, the substrate-binding sites are partially neutral or negatively (instead of positively) charged, and the binding sites of kinetoplastid glyoxalases are much wider to accommodate the additional spermidine and second glutathione moiety
evolution
-
evolutionary early prokaryotic gene transfer. The enzyme of kinetoplastid parasites has highly altered substrate-binding site due to the usage of trypanothione instead of glutathione. Trypanothione is entropically favoured in comparison with the formation of glutathione disulfide. In addition, trypanothione is more reactive because of a significantly lower thiol pKa value of 7.4, has an overall positive instead of negative charge and is much bulkier than GSH. Because of the spermidine moiety, the substrate-binding sites are partially neutral or negatively (instead of positively) charged, and the binding sites of kinetoplastid glyoxalases are much wider to accommodate the additional spermidine and second glutathione moiety
evolution
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regarding the quaternary structure, the monomeric enzyme probably resulted from a second gene-duplication event in the course of evolution
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GLO I heterozygous mutants exhibit reduced methylglyoxal detoxification
malfunction
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nondiabetic GLO1-knockdown mice demonstrate increased 20S methylglyoxal modification resulting in impaired proteasomal activity
malfunction
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increased methylglyoxal levels, resulting from decreased enzyme activity, induce apoptosis in fully differentiated podocytes, as well as in endothelial cells and macrophages in hypoxic regions of atherosclerotic arteries
malfunction
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increased methylglyoxal levels, resulting from decreased enzyme activity, induce apoptosis in fully differentiated podocytes, as well as in endothelial cells and macrophages in hypoxic regions of atherosclerotic arteries
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glyoxalase I is the first enzyme of the methylglyoxal detoxification pathway
metabolism
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the conversion of methylglyoxal into lactic acid depends on the isomerase Glo1 (glyoxalase I), the thioesterase Glo2 (glyoxalase II) and reduced glutathione (GSH) as a coenzyme, together they compose the glyoxalase system
metabolism
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the enzyme acts in a glyoxalase detoxification system with glyoxalase 2 and glutathione
metabolism
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the enzyme acts in a glyoxalase detoxification system with glyoxalase 2 and trypanothione
metabolism
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the enzyme acts in a glyoxalase detoxification system with glyoxalase 2 and trypanothione
metabolism
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the enzyme acts in a glyoxalase detoxification system with glyoxalase 2 and trypanothione
metabolism
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the enzyme acts in a glyoxalase detoxification system with glyoxalase 2 and trypanothione
metabolism
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the enzyme acts in a glyoxalase detoxification system with glyoxalase 2 and trypanothione
metabolism
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the enzyme acts in a system with glyoxalase 2 and glutathione. The allosteric regulation of the high-activity and the high-affinity conformation of the enzyme might be an adaptation to altered methylglyoxal fluxes
metabolism
the glyoxalase system catalyzes the conversion of toxic, metabolically produced 2-oxoaldehydes, such as methylglyoxal, into their corresponding nontoxic 2-hydroxycarboxylic acids, leading to detoxification of these cellular metabolites
metabolism
the glyoxalase system constitutes the major pathway for the detoxification of metabolically produced cytotoxin methylglyoxal into a non-toxic metabolite D-lactate
metabolism
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the glyoxalase system is composed of glyoxalase I, glyoxalase II, and glutathione as cofactor
metabolism
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the glyoxalase system is composed of glyoxalase I, glyoxalase II, and glutathione as cofactor
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GLOI plays an important role in the plant abiotic stress response
physiological function
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glyoxalase I has renoprotective effects in renal hypoxia such as ischemia/reperfusion injury via a reduction in cytotoxic methylglyoxal level in tubular cell
physiological function
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malaria parasites are expected to require a functional glyoxalase system to prevent the potentially toxic accumulation of methylglyoxal and advanced glycation end-products
physiological function
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methylglyoxal is a key player in vascular dysfunction, particularly due to its capacity to induce the formation of oxidative stress, cell death andendothelial dysfunction, glyoxylase I is the rate-limiting enzyme in the glyoxalase system for detoxifcation of methylglyoxal, accumulation of methylglyoxal and methylglyoxal-derived advanced glycation end-products may be a major contributing factor to atherosclerotic plaque rupture. Intracellular accumulation of methylglyoxal in endothelial cells causes dysfunction as indicated by expression of adhesion molecules such as vascular cell adhesion molecule 1 expression, which can be prevented by Glo1 overexpression
physiological function
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the enzyme is essential and contributes to the detoxification of (exogenous) methylglyoxal
physiological function
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the enzyme is essential and contributes to the detoxification of (exogenous) methylglyoxal
physiological function
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the enzyme is part of the glyoxylate system, whose function is to detoxify reactive metabolites, which mainly accumulate during hyperglycaemic metabolism, major substrate is methylglyoxal. The mean glyoxalase I activity of atherosclerotic tissue from aortic and coronary artery samples is significantly reduced compared with healthy tissue derived from the same vessel, indicating a role for glyoxalase I in atherogenesis, the enzyme plays a role in inflammatory response, hypertension, and diabetic microvascular complications, overview
physiological function
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the enzyme is part of the glyoxylate system, whose function is to detoxify reactive metabolites, which mainly accumulate during hyperglycaemic metabolism, major substrate is methylglyoxal. The mean glyoxalase I activity of atherosclerotic tissue from aortic and coronary artery samples is significantly reduced compared with healthy tissue derived from the same vessel, indicating a role for glyoxalase I in atherogenesis, the enzyme plays a role in inflammatory response, hypertension, and diabetic microvascular complications, overview
physiological function
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the glyoxalase pathway is responsible for conversion of cytotoxic methylglyoxal to D-lactate. Methylglyoxal toxicity arises from its ability to form advanced glycation end products on proteins, lipids and DNA
physiological function
the glyoxalase system catalyzes the conversion of toxic, metabolically produced 2-oxoaldehydes, such as methylglyoxal, into their corresponding nontoxic 2-hydroxycarboxylic acids, leading to detoxification of these cellular metabolites
physiological function
a deletion mutant exhibits a notable growth inhibition coupled with oxidative DNA damage and membrane disruptions. Growth of the mutant in glucose minimal medium does not result in any inhibition. Endogenous expression of recombinant Lgl in serovar Typhi leads to an increased resistance and growth in presence of external methylglyoxal
physiological function
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a mutant deficient in glyoxylase I is more sensitive to methylglyoxal and also more susceptible to human neutrophil killing. Inhibition of neutrophil myeloperoxidase rescues the gloA-deficient mutant. The mutant strain is slower at disseminating into the blood in the murine model
physiological function
overexpression in Vigna mungo driven by a constitutive Cestrum yellow leaf curling viral promoter. Transgenic plants show improved survival under salt stress. The higher level of Glyoxalase I activity in transgenic lines is directly correlated with their ability to withstand salt stress
physiological function
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a mutant deficient in glyoxylase I is more sensitive to methylglyoxal and also more susceptible to human neutrophil killing. Inhibition of neutrophil myeloperoxidase rescues the gloA-deficient mutant. The mutant strain is slower at disseminating into the blood in the murine model
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physiological function
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a deletion mutant exhibits a notable growth inhibition coupled with oxidative DNA damage and membrane disruptions. Growth of the mutant in glucose minimal medium does not result in any inhibition. Endogenous expression of recombinant Lgl in serovar Typhi leads to an increased resistance and growth in presence of external methylglyoxal
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