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Literature summary for 3.1.2.6 extracted from

  • Norton, S.J.; Principato, G.B.; Talesa, V.; Lupattelli, M.; Rosi, G.
    Glyoxalase II from Zea mays: properties and inhibition study of the enzyme purified by use of a new affinity ligand (1989), Enzyme, 42, 189-196.
    View publication on PubMed
Search for more literature for 3.1.2.6

Inhibitors

Inhibitors Comment Organism Structure
hexyl-S-glutathione
-
 Zea mays
additional information benzyloxycarbonyl-S-derivatives are stronger inhibitors than the p-chlorophenacyl S-derivative Zea mays
p-nitrobenzyl-S-glutathione very weak Zea mays
propyl-S-glutathione
-
 Zea mays
S-benzyloxycarbonylglutathione
-
 Zea mays
S-p-nitrobenzyloxycarbonylglutathione
-
 Zea mays

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.034
-
 S-acetylglutathione
-
 Zea mays
0.054
-
 S-Acetoacetylglutathione
-
 Zea mays
0.134
-
 S-succinylglutathione
-
 Zea mays
0.137
-
 S-D-lactoylglutathione
-
 Zea mays

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
26000
-
 x * 26000, SDS-PAGE Zea mays

Organism

Organism UniProt Comment Textmining
Zea mays
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Zea mays

Source Tissue

Source Tissue Comment Organism Textmining
seed
-
 Zea mays
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
65
-
-
 Zea mays

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
lactoylglutathione + H2O
-
 Zea mays D-lactate + glutathione
-
 ?
S-acetoacetylglutathione + H2O
-
 Zea mays acetoacetate + glutathione
-
 ?
S-acetylglutathione + H2O
-
 Zea mays acetate + glutathione
-
 ?
S-D-lactoylglutathione + H2O
-
 Zea mays D-lactate + glutathione
-
 ?
S-succinylglutathione + H2O
-
 Zea mays succinate + glutathione
-
 ?

Subunits

Subunits Comment Organism
? x * 26000, SDS-PAGE Zea mays