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Literature summary extracted from

  • Mitsumoto, A.; Kim, K.R.; Oshima, G.; Kunimoto, M.; Okawa, K.; Iwamatsu, A.; Nakagawa, Y.
    Glyoxalase I is a novel nitric-oxide-responsive protein (1999), Biochem. J., 344, 837-844.
    View publication on PubMedView publication on EuropePMC

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.4.1.5 S-nitroso-N-acetyl-D,L-penicillamine released NO inhibits glyoxalase I by reversible modification at a critical thiol residue, inactivation is reversed by reducing agents Homo sapiens
4.4.1.5 S-nitrosocysteine released NO inhibits glyoxalase I by reversible modification at a critical thiol residue, inactivation is reversed by reducing agents Homo sapiens
4.4.1.5 S-nitrosoglutathione glyoxal I activity in cells decreases rapidly within 30 min and reaches 10% of the control level within 2 h, activity returns to approx. 80% and 70% after removal of S-nitrosoglutathione or incubation with dithiothreitol, respectively, released NO inhibits glyoxalase I by reversible modification at a critical thiol residue, inactivation is reversed by reducing agents Homo sapiens

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.4.1.5 glutathione-methylglyoxal hemithioacetal Homo sapiens glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione (R)-S-lactoylglutathione
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.4.1.5 Homo sapiens
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.4.1.5 glutathione-methylglyoxal hemithioacetal glutathione-methylglyoxal hemithioacetal is formed non-enzymatically from methylglyoxal and glutathione Homo sapiens (R)-S-lactoylglutathione
-
 ?

Synonyms

EC Number Synonyms Comment Organism
4.4.1.5 glyoxalase I
-
 Homo sapiens