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Literature summary extracted from

  • Okado-Matsumoto, A.; Fridovich, I.
    The role of alpha,beta-dicarbonyl compounds in the toxicity of short chain sugars (2000), J. Biol. Chem., 275, 34853-34857.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.2.1.130 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 Escherichia coli
4.2.1.130 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 Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.2.1.130 methylglyoxal + H2O Escherichia coli
-
(R)-lactate
-
?
4.2.1.130 methylglyoxal + H2O Escherichia coli AB1157
-
(R)-lactate
-
?

Organism

EC Number Organism UniProt Comment Textmining
4.2.1.130 Escherichia coli
-
-
-
4.2.1.130 Escherichia coli AB1157
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.2.1.130 methylglyoxal + H2O
-
Escherichia coli (R)-lactate
-
?
4.2.1.130 methylglyoxal + H2O
-
Escherichia coli AB1157 (R)-lactate
-
?

Expression

EC Number Organism Comment Expression
4.2.1.130 Escherichia coli 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 additional information

General Information

EC Number General Information Comment Organism
4.2.1.130 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 Escherichia coli