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Literature summary for 4.2.1.130 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
Search for more literature for 4.2.1.130

Inhibitors

Inhibitors Comment Organism Structure
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
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)

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Escherichia coli AB1157
-
-
-

Substrates and Products (Substrate)

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

Expression

Organism Comment Expression
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

General Information Comment Organism
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