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Literature summary 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

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.3.12 PCMB
-
 Saccharomyces cerevisiae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.3.8 mitochondrion
-
 Saccharomyces cerevisiae 5739
-
1.3.3.12 mitochondrion
-
 Saccharomyces cerevisiae 5739
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.3.3.12 56000
-
 4 * 56000, SDS-PAGE Saccharomyces cerevisiae
1.3.3.12 290000
-
 gel filtration Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.3.8 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
-
 ?
1.3.3.12 L-galactono-1,4-lactone + O2 Saccharomyces cerevisiae enzyme catalyzes the last step of L-ascorbic acid biosynthesis L-ascorbate + H2O2
-
 ?

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.3.12
-
 Saccharomyces cerevisiae

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.3.8 L-gulono-1,4-lactone + O2 = L-xylo-hex-2-ulono-1,4-lactone + H2O2 product isomerizes spontaneously to L-ascorbate Saccharomyces cerevisiae
a

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.3.3.12 0.76
-
-
 Saccharomyces cerevisiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.8 L-galactono-1,4-lactone + O2
-
 Saccharomyces cerevisiae L-ascorbic acid + H2O2
-
 ?
1.1.3.8 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
-
 ?
1.1.3.8 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
-
 ?
1.3.3.12 D-altronolactone + O2 68% of the activity with L-galactono-1,4-lactone Saccharomyces cerevisiae ?
-
 ?
1.3.3.12 L-galactono-1,4-lactone + O2
-
 Saccharomyces cerevisiae L-ascorbate + H2O2
-
 ?
1.3.3.12 L-galactono-1,4-lactone + O2 enzyme catalyzes the last step of L-ascorbic acid biosynthesis Saccharomyces cerevisiae L-ascorbate + H2O2
-
 ?
1.3.3.12 L-gulonolactone + O2 32% of the activity with L-galactono-1,4-lactone Saccharomyces cerevisiae ?
-
 ?

Subunits

EC Number Subunits Comment Organism
1.3.3.12 tetramer 4 * 56000, SDS-PAGE Saccharomyces cerevisiae

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.8 flavin covalently bound, flavoenzyme Saccharomyces cerevisiae
1.3.3.12 FAD enzyme contains a covalently bound flavin Saccharomyces cerevisiae