4.2.1.130: D-lactate dehydratase
This is an abbreviated version!
For detailed information about D-lactate dehydratase, go to the full flat file.
Word Map on EC 4.2.1.130
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4.2.1.130
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methylglyoxal
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parkinsonism
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glyoxals
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glyoxalases
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methylglyoxalase
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deglycase
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diauxic
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horikoshii
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agriculture
- 4.2.1.130
- methylglyoxal
- parkinsonism
- glyoxals
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glyoxalases
- methylglyoxalase
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deglycase
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diauxic
- horikoshii
- agriculture
Reaction
Synonyms
DJ-1, DJ-1 glyoxalase, DJ-1a, DJ-1b, DJ-1c, DJ-1e, DJ-1f, GLO3, glutathione-independent glyoxalase, glutathione-independent glyoxalase III, glyoxalase III, glyoxylase III, GSH-independent glyoxalase III, hchA, heat shock protein 31, Hsp31, Hsp3101, Hsp3102, hsp3106, Hsp31p glyoxalase III, More, PfpI, protein DJ-1 homolog A, protein DJ-1 homolog B, protein DJ-1 homolog C, protein DJ-1 homolog E, protein DJ-1 homolog F, SAV0551, SpDJ-1, yajL, yhbO
ECTree
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General Information
General Information on EC 4.2.1.130 - D-lactate dehydratase
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evolution
malfunction
metabolism
physiological function
additional information
detailed phylogenetic analysis of GLOIII, DJ-1 and HSP31 proteins in fungi, overview
evolution
detailed phylogenetic analysis of GLOIII, DJ-1 and HSP31 proteins in fungi, overview
evolution
fungal Hsp31 proteins are the major glyoxalases III GLO3 that may have some role in protecting cells from reactive carbonyl species toxicity in fungi. The GLO3 activity of Hsp31 proteins may have evolved independently from GLO3 activity of DJ-1 proteins. DJ-1 and Hsp31 proteins belong to different subfamilies of the DJ-1/Hsp31/PfpI superfamily, which encompasses a wide variety of functionally diverse proteins, detailed phylogenetic analysis of DJ-1 and Hsp31 proteins, distribution of Hsp31 proteins in fungi, overview
evolution
fungal Hsp31 proteins are the major glyoxalases III GLO3 that may have some role in protecting cells from reactive carbonyl species toxicity in fungi. The GLO3 activity of Hsp31 proteins may have evolved independently from GLO3 activity of DJ-1 proteins. DJ-1 and Hsp31 proteins belong to different subfamilies of the DJ-1/Hsp31/PfpI superfamily, which encompasses a wide variety of functionally diverse proteins, detailed phylogenetic analysis of DJ-1 and Hsp31 proteins, distribution of Hsp31 proteins in fungi, overview
evolution
the enzyme belongs to the DJ-1 superfamily. DJ-1 superfamily proteins share the structural similarity, comprising central beta-strands surrounded by alpha-helices. Based on their primary sequences and 3D structures, the DJ-1 superfamily members are classified into three groups: DJ-1/YajL, YhbO/PfpI, and Hsp31/Ydr533C. The configuration of the active site of hDJ-1 is very different from that of Arabidopsis taliana atDJ-1d, apparently lacking some catalytic residues
evolution
the enzyme belongs to the DJ-1/PfpI superfamily. Unlike the homologues from other species, all the Arabidopsis thaliana genes have two tandem domains, which may have been created by gene duplication. The six AtDJ-1 proteins (a-f) are characterized
evolution
the enzyme PfpI belongs to the PfpI/Hsp31/DJ-1 superfamily
evolution
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fungal Hsp31 proteins are the major glyoxalases III GLO3 that may have some role in protecting cells from reactive carbonyl species toxicity in fungi. The GLO3 activity of Hsp31 proteins may have evolved independently from GLO3 activity of DJ-1 proteins. DJ-1 and Hsp31 proteins belong to different subfamilies of the DJ-1/Hsp31/PfpI superfamily, which encompasses a wide variety of functionally diverse proteins, detailed phylogenetic analysis of DJ-1 and Hsp31 proteins, distribution of Hsp31 proteins in fungi, overview
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evolution
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the enzyme belongs to the DJ-1/PfpI superfamily. Unlike the homologues from other species, all the Arabidopsis thaliana genes have two tandem domains, which may have been created by gene duplication. The six AtDJ-1 proteins (a-f) are characterized
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the stationary-phase Escherichia coli cells becomes more susceptible to methylglyoxal when hchA is deleted
malfunction
glyoxalase activity is completely abolished in the gene hchA-deficient strain. Stationary-phase Escherichia coli cells become more susceptible to methylgloxal when gene hchA is deleted, which can be complemented by an expression of plasmid-encoded hch. Accumulation of intracellular methylglyoxal in hchA-deficient strains
malfunction
the absence of the HSP31 gene sensitizes cells to oxidative, osmotic and thermal stresses, to potentially toxic products of glycolysis, such as methylglyoxal and acetic acid, and to the diauxic shift
malfunction
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the absence of the HSP31 gene sensitizes cells to oxidative, osmotic and thermal stresses, to potentially toxic products of glycolysis, such as methylglyoxal and acetic acid, and to the diauxic shift
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overexpression of Hsp31 in tobacco imparts robust stress tolerance against diverse biotic stress inducers such as viruses, bacteria and fungi, in addition to tolerance against a range of abiotic stress inducers
metabolism
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overexpression of Hsp31 in tobacco imparts robust stress tolerance against diverse biotic stress inducers such as viruses, bacteria and fungi, in addition to tolerance against a range of abiotic stress inducers
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glutathione-dependent glyoxalase pathway, i.e. glyoxalase I/II, is the most important route for the in vivo detoxification of methylglyoxal. Glyoxalase III may play a critical role in conditions with limiting carbon source. The enzyme may play an important role in protecting stationary-phase cells against carbonyl toxicity
physiological function
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in enteric bacteria methylglyoxal is detoxified by the glutathione-dependent glyoxalase I/II system, by glyoxalase III, and by aldehyde reductase and alcohol dehydrogenase. Glyoxalase III might be important for survival of non-growing Escherichia coli cultures
physiological function
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the defensive glyoxalase III is inactivated by the oxidative stress imposed by the lack of superoxide dismutase, thereby exacerbating the deleterious effect of sugar oxidation
physiological function
glyoxalase III is responsible for the detoxification of reactive carbonyl species, e.g. methylglyoxal and glyoxal, via the GSH-independent pathway, overview
physiological function
glyoxalase III is responsible for the detoxification of reactive carbonyl species, e.g. methylglyoxal and glyoxal, via the GSH-independent pathway, overview
physiological function
enzyme Hsp31 is a heat-inducible molecular chaperone. Hsp31 also displays glyoxalase activity that catalyses the conversion of methylglyoxal to D-lactate without an additional cofactor
physiological function
human DJ-1 (hDJ-1) is associated with autosomal recessive Parkinson's disease unction as a molecular chaperone as well as a transcriptional regulator
physiological function
the apparent glyoxalase activities of DJ-1 and Hsp31 reflect their deglycase activities. YhbO also displays apparent glyoxalase activities which reflect their deglycase activities, EC 3.5.1.124. The kinetics of methylglyoxal degradation by YhbO display a lag, which is likely required for spontaneous formation of the substrate, glycated YhbO. The stimulation by bovine serum albumin of the degradation of methylglyoxal and glyoxal by the deglycases is consistent with their substrates being glycated proteins (glycated YhbO, YajL or BSA) instead of glyoxals, in accordance with YhbO being a protein deglycase rather than a glyoxalase
physiological function
the apparent glyoxalase activities of DJ-1 and Hsp31 reflect their deglycase activities. YhbO also displays apparent glyoxalase activities which reflect their deglycase activities, EC 3.5.1.124. The stimulation by bovine serum albumin of the degradation of methylglyoxaland glyoxal by the deglycases is consistent with their substrates being glycated proteins (glycated YhbO, YajL or BSA) instead of glyoxals, in accordance with YajL being a protein deglycase rather than a glyoxalase
physiological function
the enzyme prevents acrylamide formation in vivo, acrylamide formation in the glyoxal/asparagine mixture is reduced by 72% by PfpI
physiological function
the enzyme is important for survival in the stationary phase of growth and under oxidative stress. It eliminates various toxic products of glycolysis
physiological function
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the enzyme is important for survival in the stationary phase of growth and under oxidative stress. It eliminates various toxic products of glycolysis
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physiological function
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the defensive glyoxalase III is inactivated by the oxidative stress imposed by the lack of superoxide dismutase, thereby exacerbating the deleterious effect of sugar oxidation
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two Schizosaccharomyces pombe Hsp31 proteins (Hsp3101 and Hsp3102) and one Saccharomyces cerevisiae Hsp31 protein (ScHsp31) display significantly higher in vitro GLO3 activity than Schizosaccharomyces pombe DJ-1 (SpDJ-1)
additional information
two Schizosaccharomyces pombe Hsp31 proteins (Hsp3101 and Hsp3102) and one Saccharomyces cerevisiae Hsp31 protein (ScHsp31) display significantly higher in vitro GLO3 activity than Schizosaccharomyces pombe DJ-1 (SpDJ-1)
additional information
two Schizosaccharomyces pombe Hsp31 proteins (Hsp3101 and Hsp3102) and one Saccharomyces cerevisiae Hsp31 protein (ScHsp31) display significantly higher in vitro GLO3 activity than Schizosaccharomyces pombe DJ-1 (SpDJ-1)
additional information
two Schizosaccharomyces pombe Hsp31 proteins (Hsp3101 and Hsp3102) and one Saccharomyces cerevisiae Hsp31 protein (ScHsp31) display significantly higher in vitro GLO3 activity than Schizosaccharomyces pombe DJ-1 (SpDJ-1)
additional information
two Schizosaccharomyces pombe Hsp31 proteins (Hsp3101 and Hsp3102) and one Saccharomyces cerevisiae Hsp31 protein (ScHsp31) display significantly higher in vitro GLO3 activity than Schizosaccharomyces pombe DJ-1 (SpDJ-1)
additional information
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both DJ-1 and Hsp31 proteins possess the Glu-Cys-His catalytic triad, Glu16-Cys111-His130 in SpDJ-1
additional information
both DJ-1 and Hsp31 proteins possess the Glu-Cys-His catalytic triad, Glu16-Cys111-His130 in SpDJ-1
additional information
both DJ-1 and Hsp31 proteins possess the Glu-Cys-His catalytic triad, Glu16-Cys111-His130 in SpDJ-1
additional information
both DJ-1 and Hsp31 proteins possess the Glu-Cys-His catalytic triad, Glu16-Cys111-His130 in SpDJ-1
additional information
both DJ-1 and Hsp31 proteins possess the Glu-Cys-His catalytic triad, Glu16-Cys111-His130 in SpDJ-1
additional information
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Hsp31 has a putative catalytic triad consisting of Asp214, His186, and Cys185. The nucleophilic cysteine Cys185 and adjacent glutamic acid Glu77 residues are critical in enzyme catalysis, forming the core of the active site
additional information
Hsp31 has a putative catalytic triad consisting of Asp214, His186, and Cys185. The nucleophilic cysteine Cys185 and adjacent glutamic acid Glu77 residues are critical in enzyme catalysis, forming the core of the active site
additional information
human enzyme DJ-1 covalently bound to glyoxylate, an analogue of methylglyoxal, forms a hemithioacetal that presumably mimics an intermediate structure in catalysis of methylglyoxal to lactate. Reaction stereospecificity modelling by a molecular modeling simulation with methylglyoxal hemithioacetal superimposed on the glyoxylate hemithioacetal. The mechanism of DJ-1 glyoxalase provides a basis for understanding the His residue-based stereospecificity, overview. Enzyme structure comparisons, the presence of the conserved Glu and Cys residues is critical for the glyoxalase activity of hDJ-1
additional information
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human enzyme DJ-1 covalently bound to glyoxylate, an analogue of methylglyoxal, forms a hemithioacetal that presumably mimics an intermediate structure in catalysis of methylglyoxal to lactate. Reaction stereospecificity modelling by a molecular modeling simulation with methylglyoxal hemithioacetal superimposed on the glyoxylate hemithioacetal. The mechanism of DJ-1 glyoxalase provides a basis for understanding the His residue-based stereospecificity, overview. Enzyme structure comparisons, the presence of the conserved Glu and Cys residues is critical for the glyoxalase activity of hDJ-1
additional information
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both DJ-1 and Hsp31 proteins possess the Glu-Cys-His catalytic triad, Glu16-Cys111-His130 in SpDJ-1
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