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Literature summary extracted from

  • Bleeg, H.S.; Christensen, F.
    Biosynthesis of ascorbate in yeast. Purification of L-galactono-1,4-lactone oxidase with properties different from mammalian L-gulonolactone oxidase (1982), Eur. J. Biochem., 127, 391-396.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.3.12 D-galactono-1,4-lactone competitive inhibition Saccharomyces cerevisiae
1.3.3.12 iodoacetamide
-
Saccharomyces cerevisiae
1.3.3.12 L-gulono-1,4-lactone competitive inhibition Saccharomyces cerevisiae
1.3.3.12 N-ethylmaleimide
-
Saccharomyces cerevisiae
1.3.3.12 p-chloromercuriphenyl sulfonate
-
Saccharomyces cerevisiae
1.3.3.12 Sulfide
-
Saccharomyces cerevisiae
1.3.3.12 sulfite
-
Saccharomyces cerevisiae

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.3.12 0.16
-
D-arabino-1,4-lactone
-
Saccharomyces cerevisiae
1.3.3.12 0.18
-
oxygen
-
Saccharomyces cerevisiae
1.3.3.12 0.3
-
L-galactono-1,4-lactone
-
Saccharomyces cerevisiae
1.3.3.12 0.36
-
L-Fucono-1,4-lactone
-
Saccharomyces cerevisiae
1.3.3.12 2
-
D-Altrono-1,4-lactone
-
Saccharomyces cerevisiae
1.3.3.12 15
-
D-threono-1,4-lactone
-
Saccharomyces cerevisiae

Localization

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

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.3.3.12 Iron enzyme contains an iron-sulfur cluster Saccharomyces cerevisiae

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.3.3.12 18000
-
4 * 18000, SDS-PAGE Saccharomyces cerevisiae
1.3.3.12 70000
-
gel filtration in presence of deoxycholate Saccharomyces cerevisiae
1.3.3.12 74000
-
non-denaturing gradient PAGE in presence of deoxycholate Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.3.12 L-galactono-1,4-lactone + O2 Saccharomyces cerevisiae
-
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

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 3.448
-
-
Saccharomyces cerevisiae

Storage Stability

EC Number Storage Stability Organism
1.3.3.12 5°C, 6 months, 50% loss of activity Saccharomyces cerevisiae

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
-
Saccharomyces cerevisiae ?
-
?
1.1.3.8 L-galactono-1,4-lactone + O2
-
Saccharomyces cerevisiae L-ascorbic acid + H2O2
-
?
1.3.3.12 D-altrono-1,4-lactone + O2
-
Saccharomyces cerevisiae ?
-
?
1.3.3.12 D-arabinono-1,4-lactone + O2
-
Saccharomyces cerevisiae ?
-
?
1.3.3.12 D-threono-1,4-lactone + O2
-
Saccharomyces cerevisiae ?
-
?
1.3.3.12 L-fucono-1,4-lactone + O2
-
Saccharomyces cerevisiae ?
-
?
1.3.3.12 L-galactono-1,4-lactone + O2
-
Saccharomyces cerevisiae L-ascorbate + H2O2
-
?

Subunits

EC Number Subunits Comment Organism
1.3.3.12 tetramer 4 * 18000, SDS-PAGE Saccharomyces cerevisiae

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.3.12 8.9
-
-
Saccharomyces cerevisiae

Cofactor

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

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.3.3.12 3.3
-
D-galactono-1,4-lactone
-
Saccharomyces cerevisiae
1.3.3.12 6.52
-
L-gulono-1,4-lactone
-
Saccharomyces cerevisiae