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Literature summary for 1.1.3.8 extracted from

  • Braun, L.; Mile, V.; Schaff, Z.; Csala, M.; Kardon, T.; Mandl, J.; Banhegyi, G.
    Induction and peroxisomal appearance of gulonolactone oxidase upon clofibrate treatment in mouse liver (1999), FEBS Lett., 458, 359-362.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome integral membrane protein in the endoplasmic reticulum Mus musculus
-
-

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-gulono-1,4-lactone + O2 Mus musculus
-
L-xylo-hex-3-ulonolactone + H2O2
-
?

Organism

Organism UniProt Comment Textmining
Mus musculus
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mouse treated with clofibrate, a peroxisome proliferator
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no activity in Cavia porcellus
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guinea pig
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no activity in Homo sapiens
-
-
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no activity in primates
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-
-

Reaction

Reaction Comment Organism Reaction ID
L-gulono-1,4-lactone + O2 = L-xylo-hex-2-ulono-1,4-lactone + H2O2 product isomerizes spontaneously to L-ascorbate Mus musculus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Mus musculus
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Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
clofibrate-treated mouse enzyme is 8.5fold as active as non-treated mouse enzyme in the microsome and 500fold as active in the peroxisome Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-gulono-1,4-lactone + O2
-
Mus musculus L-xylo-hex-3-ulonolactone + H2O2
-
?
L-gulono-1,4-lactone + O2
-
Mus musculus L-xylo-hex-3-ulonolactone + H2O2 product isomerizes spontaneously to L-ascorbate ?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
-
Mus musculus

Cofactor

Cofactor Comment Organism Structure
flavin covalently bound, flavoenzyme Mus musculus