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Literature summary for 4.4.1.5 extracted from

  • Mannervik, B.; Lindström, L.; Bartfai, T.
    Partial purification and characterization of glyoxalase I from porcine erythrocytes (1972), Eur. J. Biochem., 29, 276-281.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
1,10-phenanthroline reactivation by Mg2+, Mn2+ or Ca2+ Sus scrofa
EDTA reactivation by Mg2+, Mn2+ or Ca2+ Sus scrofa

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information
-
Sus scrofa

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activates apoenzyme Sus scrofa
Mg2+ activates apoenzyme Sus scrofa
Mn2+ activates apoenzyme Sus scrofa

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
52000
-
gel filtration Sus scrofa

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Purification (Commentary)

Purification (Comment) Organism
partial Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
erythrocyte
-
Sus scrofa
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
159
-
-
Sus scrofa

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glutathione + methylglyoxal the substrat is the hemithioacetal of methylglyoxal and glutathione Sus scrofa S-lactoylglutathione
-
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