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Literature summary extracted from

  • Kester, M.V.; Norton, S.J.
    The isolation and characterization of mouse liver glyoxalase I (1975), Biochim. Biophys. Acta, 391, 212-221.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.4.1.5 S-(omega-aminodecyl)glutathione
-
 Mus musculus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.4.1.5 43000
-
 gel filtration Mus musculus

Organism

EC Number Organism UniProt Comment Textmining
4.4.1.5 Mus musculus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.4.1.5
-
 Mus musculus

Reaction

EC Number Reaction Comment Organism Reaction ID
4.4.1.5 (R)-S-lactoylglutathione = glutathione + 2-oxopropanal there is a single site for the binding of the hemimercaptal of methylglyoxal and glutathione, for the binding of glutathione, and for the binding of S-substituted derivatives of glutathione. One-substrate reaction mechanism with hemimercaptal being the substrate, but does not rule out the possibility of the alternate branches Mus musculus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.4.1.5 liver
-
 Mus musculus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.4.1.5 2200
-
-
 Mus musculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.4.1.5 glutathione + methylglyoxal
-
 Mus musculus S-lactoylglutathione
-
 ?