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Information on EC 4.2.1.130 - D-lactate dehydratase and Organism(s) Escherichia coli and UniProt Accession P45470
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4.2.1.130 D-lactate dehydrataseIUBMB Comments
The enzyme, described from the fungi Candida albicans and Schizosaccharomyces pombe, converts 2-oxopropanal to (R)-lactate in a single glutathione (GSH)-independent step. The other known route for this conversion is the two-step GSH-dependent pathway catalysed by EC 4.4.1.5 (lactoylglutathione lyase) and EC 3.1.2.6 (hydroxyacylglutathione hydrolase).
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Word Map
- 4.2.1.130
- methylglyoxal
- parkinsonism
- glyoxals
-
glyoxalases
- methylglyoxalase
-
deglycase
-
diauxic
- horikoshii
- agriculture
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
hsp31, glyoxalase iii, dj-1a, dj-1b, glutathione-independent glyoxalase, hsp3101, hsp3102, glutathione-independent glyoxalase iii, heat shock protein 31, dj-1 glyoxalase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
glyoxalase III
glyoxylase III
additional information
glyoxylase III
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
SYSTEMATIC NAME
IUBMB Comments
(R)-lactate hydro-lyase
The enzyme, described from the fungi Candida albicans and Schizosaccharomyces pombe, converts 2-oxopropanal to (R)-lactate in a single glutathione (GSH)-independent step. The other known route for this conversion is the two-step GSH-dependent pathway catalysed by EC 4.4.1.5 (lactoylglutathione lyase) and EC 3.1.2.6 (hydroxyacylglutathione hydrolase).
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
methylglyoxal + H2O
(R)-lactate
Hsp31 efficiently detoxifies exogenously added methylglyoxal
-
-
?
methylglyoxal + H2O
(R)-lactate
glyoxalase III does not catalyse the reverse reaction. Glyoxalase III cannot catalyse either the formation or the breakdown of S-D-lactoylglutathione
-
-
ir
phenylglyoxal + H2O
?
the rate with phenylglyoxal is about 15% of that with methylglyoxal
-
-
ir
additional information
?
-
-
purified glyoxalase III can catalyse the conversion of methylglyoxal into S-D-lactoylglutathione in the presence of GSH or S-D-lactoylglutathione into D-lactate, cf. EC 4.4.1.5
-
-
?
additional information
?
-
purified glyoxalase III can catalyse the conversion of methylglyoxal into S-D-lactoylglutathione in the presence of GSH or S-D-lactoylglutathione into D-lactate, cf. EC 4.4.1.5
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
methylglyoxal + H2O
(R)-lactate
Hsp31 efficiently detoxifies exogenously added methylglyoxal
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
EDTA
an extensive dialysis of Hsp31 with 10 mM EDTA does not significantly decrease the glyoxalase III activity of more than 30%
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
-
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
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
-
additional information
glutathione analogues, which are inhibitors of glyoxalase I, do not inhibit glyoxalase III, but the enzyme is sensitive to thiol-blocking reagents
-
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
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
bovine serum albumin
activates the glyoxalase activity of the enzyme with methylglyoxal and glyoxal
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bovine serum albumin
activates the glyoxalase activity of the enzyme with methylglyoxal and glyoxal
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
additional information
additional information
Michaelis-Menten kinetics
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.095
methylglyoxal
pH 7.5, temperature not specified in the publication, mutant enzyme H184A
2.61
methylglyoxal
pH 7.5, temperature not specified in the publication, wild-type enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.5
methylglyoxal
pH 7.5, temperature not specified in the publication, mutant enzyme H184A
1.8
methylglyoxal
pH 7.5, temperature not specified in the publication, wild-type enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.254
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 8
8
glyoxalase III is active over a wide range of pH with no sharp pH optimum
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 10
5 - 9
pH 5.0: about 45% of maximal activity, pH 9.0: about 45% of maximal activity
5 - 10
pH 5.0: sharp decrease in reaction rate below, pH 10.0: activity 20-25% lower than the rate at physiological pH
5 - 10
glyoxalase III is active over a wide range of pH with no sharp pH optimum, sharp decrease in reaction rate occurs below pH 5.0, 20.25% of maximal activity at pH 10.0
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25 - 50
25°C: about 55% of maximal activity, 50°C: about 75% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
additional information
-
glyoxalase III activity is present in all three media in almost equal amounts ranging from 0.033 to 0.054 unit/mg of protein
additional information
glyoxalase III activity is present in all three media in almost equal amounts ranging from 0.033 to 0.054 unit/mg of protein
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
malfunction
physiological function
additional information
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
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
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
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
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme 27.6fold by ammonium sulfate fractionation, heat treatment, gel filtration chromatography, anion exchange chromatography, and hydrophobic interaction chromatography on n-butyl sepharose resin
native enzyme 725fold by ammonium sulfate fractionation, heat treatment, gel filtration, anion exchange chromatography, and affinity chromatography on a 4-hydroxymercuribenzoate-bound resin
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
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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
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Benov, L.; Sequeira, F.; Beema, A.F.
Role of rpoS in the regulation of glyoxalase III in Escherichia coli
Acta Biochim. Pol.
51
857-860
2004
Escherichia coli
Misra, K.; Banerjee, A.B.; Ray, S.; Ray, M.
Glyoxalase III from Escherichia coli: a single novel enzyme for the conversion of methylglyoxal into D-lactate without reduced glutathione
Biochem. J.
305
999-1003
1995
Escherichia coli, Escherichia coli (P31658)
Okado-Matsumoto, A.; Fridovich, I.
The role of alpha,beta-dicarbonyl compounds in the toxicity of short chain sugars
J. Biol. Chem.
275
34853-34857
2000
Escherichia coli, Escherichia coli AB1157
MacLean, M.J.; Ness, L.S.; Ferguson, G.P.; Booth, I.R.
The role of glyoxalase I in the detoxification of methylglyoxal and in the activation of the KefB K+ efflux system in Escherichia coli
Mol. Microbiol.
27
563-571
1998
Escherichia coli, Escherichia coli MJF274
Subedi, K.P.; Choi, D.; Kim, I.; Min, B.; Park, C.
Hsp31 of Escherichia coli K-12 is glyoxalase III
Mol. Microbiol.
81
926-936
2011
Escherichia coli, Escherichia coli (P31658)
Abdallah, J.; Mihoub, M.; Gautier, V.; Richarme, G.
The DJ-1 superfamily members YhbO and YajL from Escherichia coli repair proteins from glycation by methylglyoxal and glyoxal
Biochem. Biophys. Res. Commun.
470
282-286
2016
Escherichia coli (P45470), Escherichia coli (Q46948), Escherichia coli
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