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Literature summary for 1.1.3.8 extracted from

  • Nishikimi, M.; Noguchi, E.; Yagi, K.
    Occurrence in yeast of L-galactonolactone oxidase which is similar to a key enzyme for ascorbic acid biosynthesis in animals, L-gulonolactone oxidase (1978), Arch. Biochem. Biophys., 191, 479-486.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
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Saccharomyces cerevisiae 5739
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
L-gulono-1,4-lactone + O2 Saccharomyces cerevisiae the enzyme has a configurational specificity for the hydroxyl group at C(2) L-xylo-hex-3-ulonolactone + H2O2
-
?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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similar enzyme: L-galactono-1,4-lactone oxidase
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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 Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-galactono-1,4-lactone + O2
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Saccharomyces cerevisiae L-ascorbic acid + H2O2
-
?
L-gulono-1,4-lactone + O2 the enzyme has a configurational specificity for the hydroxyl group at C-2 Saccharomyces cerevisiae L-xylo-hex-3-ulonolactone + H2O2
-
?
L-gulono-1,4-lactone + O2 the enzyme has a configurational specificity for the hydroxyl group at C(2) Saccharomyces cerevisiae L-xylo-hex-3-ulonolactone + H2O2
-
?

Cofactor

Cofactor Comment Organism Structure
flavin covalently bound, flavoenzyme Saccharomyces cerevisiae