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Literature summary extracted from

  • Kiuchi, K.; Nishikimi, M.; Yagi, K.
    Purification and characterization of L-gulonolactone oxidase from chicken kidney microsomes (1982), Biochemistry, 21, 5076-5082.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.3.8 0.007
-
 L-gulono-1,4-lactone
-
 Gallus gallus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.3.8 microsome
-
 Gallus gallus
-
-

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.3.8 50000
-
 x * 50000, SDS-PAGE Gallus gallus
1.1.3.8 400000
-
 gel filtraton Gallus gallus

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 Gallus gallus the enzyme has a configurational specificity for the hydroxyl group at C(2) L-xylo-hex-3-ulonolactone + H2O2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.8 Gallus gallus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.3.8
-
 Gallus gallus

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 Gallus gallus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.3.8 kidney
-
 Gallus gallus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.3.8 3.43
-
 L-ascorbate synthesis Gallus gallus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.8 D-altrono-1,4-lactone + O2 16% as active as L-gulono-1,4-lactone Gallus gallus ?
-
 ?
1.1.3.8 D-mannono-1,4-lactone + O2 64% as active as L-gulono-1,4-lactone Gallus gallus ?
-
 ?
1.1.3.8 L-galactono-1,4-lactone + O2 90% as active as L-gulono-1,4-lactone Gallus gallus 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 Gallus gallus L-xylo-hex-3-ulonolactone + H2O2 product isomerizes spontaneously to L-ascorbate ?
1.1.3.8 L-gulono-1,4-lactone + O2 the enzyme has a configurational specificity for the hydroxyl group at C(2) Gallus gallus L-xylo-hex-3-ulonolactone + H2O2
-
 ?

Subunits

EC Number Subunits Comment Organism
1.1.3.8 oligomer x * 50000, SDS-PAGE Gallus gallus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.3.8 37
-
-
 Gallus gallus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.3.8 7.5
-
 in phosphate-citrate buffer Gallus gallus
1.1.3.8 8
-
 in Tris-citrate buffer Gallus gallus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.3.8 FAD 1 mol FAD per protein monomer Gallus gallus
1.1.3.8 FAD 8alpha-(N1-histidyl)riboflavin is the cofactor structure determined by high-voltage paper electrophoresis Gallus gallus