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2,4-Dinitrophenylhydrazine
inactivation; inactivation
4-hydroxymercuribenzoate
inactivates the enzyme, reversible by dithiothreitol and other thiol-group-containing compounds
5,5'-dithiobis-(2-nitrobenzoate)
0.4 mM, 15 min, complete inactivation. 5 mM DTT restores activity almost completely
Borate
boric acid/borate buffer is moderately inhibitory
Cu2+
maximal inhibition below 0.025 mM
EDTA
an extensive dialysis of Hsp31 with 10 mM EDTA does not significantly decrease the glyoxalase III activity of more than 30%
glyceraldehyde
about 60% inhibition at 10 mM
glycolaldehyde
about 60% inhibition at 10 mM
glyoxylate
determmination of an enzyme crystal structure with the inhibitor bound to the active Cys residue of the enzyme as a hemithioacetal, detailed binding structure analysis, overview
hydrogen peroxide
-
sensitivity of glyoxalase III is special and might relate to the thiol group that is essential for its activity and possibly to the binding of iron adjacent to the active site thiol
N-ethylmaleimide
0.4 mM, 15 min, complete inactivation. 5 mM DTT restores activity almost completely
p-hydroxymercuribenzoate
0.4 mM, 15 min, complete inactivation. 5 mM DTT restores activity almost completely
superoxide
-
sensitivity of glyoxalase III is special and might relate to the thiol group that is essential for its activity and possibly to the binding of iron adjacent to the active site thiol
Zn2+
maximal inhibition above 0.3 mM, 10% inhibition at 0.025 mM, more than 50% inhibition at 0.1 mM
additional information
-
glutathione analogues, which are inhibitors of glyoxalase I, do not inhibit glyoxalase III, but the enzyme is sensitive to thiol-blocking reagents; S-methylglutathione and S-octylglutathione, even at concentrations of 20 mM and 0.25 mM respectively, have no inhibitory effect on Escherichia coli glyoxalase III
-
additional information
glutathione analogues, which are inhibitors of glyoxalase I, do not inhibit glyoxalase III, but the enzyme is sensitive to thiol-blocking reagents; S-methylglutathione and S-octylglutathione, even at concentrations of 20 mM and 0.25 mM respectively, have no inhibitory effect on Escherichia coli glyoxalase III
-
additional information
-
the effects of some metal ions might be due to a change in oxidation state of enzyme
-
additional information
the effects of some metal ions might be due to a change in oxidation state of enzyme
-
additional information
poor or no inhibition by acrolein, acetaldehyde, propionaldehyde, butyraldehyde, valeraldehyde, acetol, 2,3-butanedione, dihydroxyacetone, 1,2-propanediol, and oxalic acid
-
additional information
-
poor or no inhibition by acrolein, acetaldehyde, propionaldehyde, butyraldehyde, valeraldehyde, acetol, 2,3-butanedione, dihydroxyacetone, 1,2-propanediol, and oxalic acid
-
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156.9
2-oxopropanal
pH 7.5, 37°C
0.19 - 1900
methylglyoxal
13
Phenylglyoxal
pH and temperature not specified in the publication
additional information
additional information
-
0.19
methylglyoxal
pH 7.5, temperature not specified in the publication, mutant enzyme H184A
1.43
methylglyoxal
pH 7.5, temperature not specified in the publication, wild-type enzyme
1.5
methylglyoxal
recombinant ScHsp31, pH and temperature not specified in the publication
10.8
methylglyoxal
recombinant wild-type SpDJ-1, pH and temperature not specified in the publication
31.1
methylglyoxal
recombinant Hsp3101, pH and temperature not specified in the publication
37.3
methylglyoxal
recombinant mutant SpDJ-1 H130A, pH and temperature not specified in the publication
58
methylglyoxal
recombinant Hsp3102, pH and temperature not specified in the publication
900
methylglyoxal
30°C, pH not specified in the publication, wild-type enzyme
1900
methylglyoxal
30°C, pH not specified in the publication, mutant enzyme L166P
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
cooperative mechanism, Eadie-Hofstee plots for hDJ-1 indicate mono- and bi-phasic curves, which are analyzed by using the Hill equation and gives a coefficient (n) of 1.0. KInetics, overview
-
additional information
additional information
-
cooperative mechanism, Eadie-Hofstee plots for hDJ-1 indicate mono- and bi-phasic curves, which are analyzed by using the Hill equation and gives a coefficient (n) of 1.0. KInetics, overview
-
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0.0055
substrate methylglyoxal, pH 6.8, 37°C
0.0062
substrate methylglyoxal, pH 6.8, 37°C
0.013
substrate methylglyoxal, pH 6.8, 37°C
0.015
substrate methylglyoxal, pH 6.8, 37°C
0.033 - 0.054
crude enzyme extracts, pH 8.0, 37°C
0.25
substrate glyoxal, pH 6.8, 37°C
0.31
substrate glyoxal, pH 6.8, 37°C
0.254
pH 7.5, temperature not specified in the publication
0.254
purified native enzyme, pH 7.5, 37°C
additional information
the enzyme DJ-1C shows very low enzyme activity
additional information
the enzyme DJ-1C shows very low enzyme activity
additional information
the enzyme DJ-1C shows very low enzyme activity
additional information
the enzyme DJ-1C shows very low enzyme activity
additional information
the enzyme DJ-1C shows very low enzyme activity
additional information
-
the enzyme DJ-1C shows very low enzyme activity
additional information
the enzyme DJ-1E shows very low activity with substrate glyoxal
additional information
the enzyme DJ-1E shows very low activity with substrate glyoxal
additional information
the enzyme DJ-1E shows very low activity with substrate glyoxal
additional information
the enzyme DJ-1E shows very low activity with substrate glyoxal
additional information
the enzyme DJ-1E shows very low activity with substrate glyoxal
additional information
-
the enzyme DJ-1E shows very low activity with substrate glyoxal
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evolution
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
-
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/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
-
malfunction
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
-
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
-
metabolism
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
-
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
-
physiological function
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
-
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
-
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
-
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
-
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
-
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
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
-
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
-
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
-
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
-
both DJ-1 and Hsp31 proteins possess the Glu-Cys-His catalytic triad, Glu16-Cys111-His130 in SpDJ-1
-
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monomer
enzyme structure comparisons, overview
dimer
2 * 41400, about, sequence calculation
dimer
2 * 41900, about, sequence calculation
dimer
-
2 * 41900, about, sequence calculation
-
dimer
-
2 * 41400, about, sequence calculation
-
dimer
2 * 40000, SDS-PAGE
dimer
2 * 41000, about, SDS-PAGE
trimer
3 * 41600, about, sequence calculation
trimer
3 * 42700, about, sequence calculation
trimer
3 * 43100, about, sequence calculation
trimer
-
3 * 41600, about, sequence calculation
-
trimer
-
3 * 43100, about, sequence calculation
-
trimer
-
3 * 42700, about, sequence calculation
-
additional information
three-dimensional structure comparisons of DJ-1 proteins from Arabidopsis taliana, molecular modelling, overview. Secondary structure content estimated by circular dichroism
additional information
three-dimensional structure comparisons of DJ-1 proteins from Arabidopsis taliana, molecular modelling, overview. Secondary structure content estimated by circular dichroism
additional information
three-dimensional structure comparisons of DJ-1 proteins from Arabidopsis taliana, molecular modelling, overview. Secondary structure content estimated by circular dichroism
additional information
three-dimensional structure comparisons of DJ-1 proteins from Arabidopsis taliana, molecular modelling, overview. Secondary structure content estimated by circular dichroism
additional information
three-dimensional structure comparisons of DJ-1 proteins from Arabidopsis taliana, molecular modelling, overview. Secondary structure content estimated by circular dichroism
additional information
-
three-dimensional structure comparisons of DJ-1 proteins from Arabidopsis taliana, molecular modelling, overview. Secondary structure content estimated by circular dichroism
additional information
-
three-dimensional structure comparisons of DJ-1 proteins from Arabidopsis taliana, molecular modelling, overview. Secondary structure content estimated by circular dichroism
-
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C185A
mutation almost completely abolishes glyoxalase activity
E77A
mutation almost completely abolishes glyoxalase activity
H184A
kcat/KM is 3.6fold lower compared to the wild-type value
H186A
mutant enzyme shows approximately 17% remaining activity
L166P
the Km-value for methylglyoxal of the mutant enzyme is about 2fold higher compared to the wild-type enzyme
C111A
site-directed mutagenesis, catalytically inactive mutant
E16A
site-directed mutagenesis, catalytically inactive mutant
H130A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
C190A
diminished glyoxalase III activity
E81A
diminished glyoxalase III activity
H191A
marginal glyoxalase III activity
C190A
-
diminished glyoxalase III activity
-
E81A
-
diminished glyoxalase III activity
-
H191A
-
marginal glyoxalase III activity
-
additional information
-
mutagenesis studies based on evaluation of conserved catalytic residues reveals that the Cys185 and Glu77 are essential for catalysis, whereas His186 is less crucial for enzymatic function, although it participates in the catalytic process
additional information
mutagenesis studies based on evaluation of conserved catalytic residues reveals that the Cys185 and Glu77 are essential for catalysis, whereas His186 is less crucial for enzymatic function, although it participates in the catalytic process
additional information
-
generation of a hchA-deficient strain from Escherichia coli strain MG1655
additional information
generation of a hchA-deficient strain from Escherichia coli strain MG1655
additional information
overexpression of Saccharomyces cerevisiae ScHSP31 confers methylglyoxal and glyoxal resistance on either wild-type Schizosaccharomyces pombe cells or GLO1 deletion cells of Schizosaccharomyces pombe
additional information
-
overexpression of Saccharomyces cerevisiae gene ScHSP31 can confer methylglyoxal and glyoxal resistance on either wild-type Schizosaccharomyces pombe cells or GLO1-deletion of Schizosaccharomyces pombe
additional information
overexpression of Saccharomyces cerevisiae gene ScHSP31 can confer methylglyoxal and glyoxal resistance on either wild-type Schizosaccharomyces pombe cells or GLO1-deletion of Schizosaccharomyces pombe
additional information
overexpression of Saccharomyces cerevisiae gene ScHSP31 can confer methylglyoxal and glyoxal resistance on either wild-type Schizosaccharomyces pombe cells or GLO1-deletion of Schizosaccharomyces pombe
additional information
overexpression of Saccharomyces cerevisiae gene ScHSP31 can confer methylglyoxal and glyoxal resistance on either wild-type Schizosaccharomyces pombe cells or GLO1-deletion of Schizosaccharomyces pombe
additional information
-
overexpression of Schizosaccharomyces pombe hsp3101 confers methylglyoxal and glyoxal resistance on either wild-type Schizosaccharomyces pombe cells or GLO1 deletion cells of Schizosaccharomyces pombe
additional information
overexpression of Schizosaccharomyces pombe hsp3101 confers methylglyoxal and glyoxal resistance on either wild-type Schizosaccharomyces pombe cells or GLO1 deletion cells of Schizosaccharomyces pombe
additional information
overexpression of Schizosaccharomyces pombe hsp3101 confers methylglyoxal and glyoxal resistance on either wild-type Schizosaccharomyces pombe cells or GLO1 deletion cells of Schizosaccharomyces pombe
additional information
overexpression of Schizosaccharomyces pombe hsp3101 confers methylglyoxal and glyoxal resistance on either wild-type Schizosaccharomyces pombe cells or GLO1 deletion cells of Schizosaccharomyces pombe
additional information
-
overexpression of Schizosaccharomyces pombe hsp3102 confers methylglyoxal and glyoxal resistance on either wild-type Schizosaccharomyces pombe cells or GLO1 deletion cells of Schizosaccharomyces pombe
additional information
overexpression of Schizosaccharomyces pombe hsp3102 confers methylglyoxal and glyoxal resistance on either wild-type Schizosaccharomyces pombe cells or GLO1 deletion cells of Schizosaccharomyces pombe
additional information
overexpression of Schizosaccharomyces pombe hsp3102 confers methylglyoxal and glyoxal resistance on either wild-type Schizosaccharomyces pombe cells or GLO1 deletion cells of Schizosaccharomyces pombe
additional information
overexpression of Schizosaccharomyces pombe hsp3102 confers methylglyoxal and glyoxal resistance on either wild-type Schizosaccharomyces pombe cells or GLO1 deletion cells of Schizosaccharomyces pombe
additional information
-
overexpression of Schizosaccharomyces pombe hsp3101 confers methylglyoxal and glyoxal resistance on either wild-type Schizosaccharomyces pombe cells or GLO1 deletion cells of Schizosaccharomyces pombe
-
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DJ-1 gene is subcloned from pLenti6-DJ-1-V5-WT plasmid into the pRetroX-Tight-Puro Advanced vector. The confirmed clone is transfected into HEK-293 cells
expression in Nicotiana tabacum cv. Wisconsin. 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. During stress, Hsp31 is targeted to mitochondria and induces expression of key stress-related genes
expression of C-terminally GFP-tagged SpDJ-1, expression of wild-type and mutant SpDj-1 proteins in Escherichia coli strain BL21(DE3), detailed phylogenetic analysis of GLOIII, DJ-1 and HSP31 proteins, overview
gene DJ1A, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of HIs-tagged enzyme in Escherichia coli strain BL21 (DE3)
gene DJ1B, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of HIs-tagged enzyme in Escherichia coli strain BL21 (DE3)
gene DJ1C, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of HIs-tagged enzyme in Escherichia coli strain BL21 (DE3)
gene DJ1E, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of HIs-tagged enzyme in Escherichia coli strain BL21 (DE3)
gene DJ1F, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of HIs-tagged enzyme in Escherichia coli strain BL21 (DE3)
gene hsp3101 encoding a Hsp31 protein, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis, recombinant overexpression of Schizosaccharomyces pombe hsp3101 in Schizosaccharomyces pombe wild-type cells or GLO1 deletion cells
gene hsp3101, expression of C-terminally GFP-tagged HSP31 proteins, expression of HSP3101 protein in Escherichia coli strain BL21(DE3), detailed phylogenetic analysis of GLOIII, DJ-1 and HSP31 proteins, overview
gene hsp3102 encoding a Hsp31 protein, sequence comparisons, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant overexpression of Schizosaccharomyces pombe hsp3101 in Schizosaccharomyces pombe wild-type cells or GLO1 deletion cells
gene hsp3106 encoding DJ-1 protein, DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic analysis
gene PARK7, sequence comparisons
gene ScHSP31 encoding Hsp31 protein, sequence comparisons, DNA and amino acid sequence determination and analysis, phylogenetic analysis, recombinant overexpression of Schizosaccharomyces pombe hsp3101 in Schizosaccharomyces pombe wild-type cells or GLO1 deletion cells
gene ScHSP31, expression in Escherichia coli strain BL21(DE3), detailed phylogenetic analysis of GLOIII, DJ-1 and HSP31 proteins, overview. Overexpression of ScHSP31 can confer methylglyoxal and glyoxal resistance on either wild-type Schizosaccharomyces pombe cells or GLO1-deletion of Schizosaccharomyces pombe
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glyoxalase III is a stationary-phase enzyme. Its activity reaches a maximum at the entry into the stationary phase and remained high for at least 20 h. Glyoxalase III is regulated by rpoS
-
glyoxalase III is not elevated in Escherichia coli cells deleted for glyoxalase I
no induction of glyoxalase III by growth in the presence of methylglyoxal. Paraquat, which can increase the aerobic production of superoxide, suppresses glyoxalase III in JI132
strong induction of this gene is caused by high concentrations of ethanol and other products of glycolysis. HSP31 gene expression is controlled by multiple transcription factors, including Yap1p, Cad1p, Msn2p, Msn4p, Haa1p and Hsf1p. These transcription factors mediate the HSP31 promoter responses to oxidative, osmotic and thermal stresses, to potentially toxic products of glycolysis, such as methylglyoxal and acetic acid, and to the diauxic shift
the enzyme is heat-inducible
glyoxalase III is not elevated in Escherichia coli cells deleted for glyoxalase I
-
glyoxalase III is not elevated in Escherichia coli cells deleted for glyoxalase I
-
-
no induction of glyoxalase III by growth in the presence of methylglyoxal. Paraquat, which can increase the aerobic production of superoxide, suppresses glyoxalase III in JI132
-
no induction of glyoxalase III by growth in the presence of methylglyoxal. Paraquat, which can increase the aerobic production of superoxide, suppresses glyoxalase III in JI132
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strong induction of this gene is caused by high concentrations of ethanol and other products of glycolysis. HSP31 gene expression is controlled by multiple transcription factors, including Yap1p, Cad1p, Msn2p, Msn4p, Haa1p and Hsf1p. These transcription factors mediate the HSP31 promoter responses to oxidative, osmotic and thermal stresses, to potentially toxic products of glycolysis, such as methylglyoxal and acetic acid, and to the diauxic shift
strong induction of this gene is caused by high concentrations of ethanol and other products of glycolysis. HSP31 gene expression is controlled by multiple transcription factors, including Yap1p, Cad1p, Msn2p, Msn4p, Haa1p and Hsf1p. These transcription factors mediate the HSP31 promoter responses 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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