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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Inhibitors
Inhibitors on EC 4.2.1.130 - D-lactate dehydratase
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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%
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
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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
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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
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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
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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
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additional information
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the effects of some metal ions might be due to a change in oxidation state of enzyme
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additional information
the effects of some metal ions might be due to a change in oxidation state of enzyme
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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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additional information
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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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