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Literature summary for 1.1.3.15 extracted from

  • Gunshore, S.; Brush, E.J.; Hamilton, G.A.
    Equilibrium constants for the formation of glyoxylate thiohemiacetals and kinetic constants for their oxidation by O2 catalyzed by L-hydroxy acid oxidase (1985), Bioorg. Chem., 13, 1-13.
No PubMed abstract available

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.6
-
DL-2-hydroxybutyrate
-
Rattus sp.

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
DL-2-hydroxybutyrate + O2 Rattus sp. best substrate tested 2-oxobutyrate + H2O2
-
?
glyoxylate thiohemiacetals + O2 Rattus sp. possible natural substrates, i.e. glyoxylate thiohemiacetals of coemzyme A, D-phosphopantetheine, D-pantetheine, N-acetylcysteamine, 2-mercaptoethanol, DL-dihydrolipoate, propane-1,3-dithiol ? + H2O2
-
?

Organism

Organism UniProt Comment Textmining
Rattus sp.
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
kidney
-
Rattus sp.
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
DL-2-hydroxybutyrate + O2 best substrate tested Rattus sp. 2-oxobutyrate + H2O2
-
?
glyoxylate thiohemiacetals + O2 possible natural substrates, i.e. glyoxylate thiohemiacetals of coemzyme A, D-phosphopantetheine, D-pantetheine, N-acetylcysteamine, 2-mercaptoethanol, DL-dihydrolipoate, propane-1,3-dithiol Rattus sp. ? + H2O2
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.76
-
DL-2-hydroxybutyrate
-
Rattus sp.