BRENDA - Enzyme Database
show all sequences of 1.3.3.12

Biosynthesis of ascorbate in yeast. Purification of L-galactono-1,4-lactone oxidase with properties different from mammalian L-gulonolactone oxidase

Bleeg, H.S.; Christensen, F.; Eur. J. Biochem. 127, 391-396 (1982)

Data extracted from this reference:

Inhibitors
Inhibitors
Commentary
Organism
Structure
D-galactono-1,4-lactone
competitive inhibition
Saccharomyces cerevisiae
iodoacetamide
-
Saccharomyces cerevisiae
L-gulono-1,4-lactone
competitive inhibition
Saccharomyces cerevisiae
N-ethylmaleimide
-
Saccharomyces cerevisiae
p-chloromercuriphenyl sulfonate
-
Saccharomyces cerevisiae
Sulfide
-
Saccharomyces cerevisiae
sulfite
-
Saccharomyces cerevisiae
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.16
-
D-arabino-1,4-lactone
-
Saccharomyces cerevisiae
0.18
-
oxygen
-
Saccharomyces cerevisiae
0.3
-
L-galactono-1,4-lactone
-
Saccharomyces cerevisiae
0.36
-
L-Fucono-1,4-lactone
-
Saccharomyces cerevisiae
2
-
D-Altrono-1,4-lactone
-
Saccharomyces cerevisiae
15
-
D-threono-1,4-lactone
-
Saccharomyces cerevisiae
Localization
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrion
-
Saccharomyces cerevisiae
5739
-
Metals/Ions
Metals/Ions
Commentary
Organism
Structure
Iron
enzyme contains an iron-sulfur cluster
Saccharomyces cerevisiae
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
18000
-
4 * 18000, SDS-PAGE
Saccharomyces cerevisiae
70000
-
gel filtration in presence of deoxycholate
Saccharomyces cerevisiae
74000
-
non-denaturing gradient PAGE in presence of deoxycholate
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-galactono-1,4-lactone + O2
Saccharomyces cerevisiae
-
L-ascorbate + H2O2
-
-
-
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Saccharomyces cerevisiae
-
-
-
Purification (Commentary)
Commentary
Organism
-
Saccharomyces cerevisiae
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
3.448
-
-
Saccharomyces cerevisiae
Storage Stability
Storage Stability
Organism
5°C, 6 months, 50% loss of activity
Saccharomyces cerevisiae
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-altrono-1,4-lactone + O2
-
389744
Saccharomyces cerevisiae
?
-
-
-
?
D-arabinono-1,4-lactone + O2
-
389744
Saccharomyces cerevisiae
?
-
-
-
?
D-threono-1,4-lactone + O2
-
389744
Saccharomyces cerevisiae
?
-
-
-
?
L-fucono-1,4-lactone + O2
-
389744
Saccharomyces cerevisiae
?
-
-
-
?
L-galactono-1,4-lactone + O2
-
389744
Saccharomyces cerevisiae
L-ascorbate + H2O2
-
-
-
-
L-galactono-1,4-lactone + O2
-
389744
Saccharomyces cerevisiae
L-ascorbate + H2O2
-
389744
Saccharomyces cerevisiae
?
Subunits
Subunits
Commentary
Organism
tetramer
4 * 18000, SDS-PAGE
Saccharomyces cerevisiae
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.9
-
-
Saccharomyces cerevisiae
Cofactor
Cofactor
Commentary
Organism
Structure
FAD
enzyme contains a covalently bound flavin
Saccharomyces cerevisiae
Ki Value [mM]
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
3.3
-
D-galactono-1,4-lactone
-
Saccharomyces cerevisiae
6.52
-
L-gulono-1,4-lactone
-
Saccharomyces cerevisiae
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FAD
enzyme contains a covalently bound flavin
Saccharomyces cerevisiae
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
D-galactono-1,4-lactone
competitive inhibition
Saccharomyces cerevisiae
iodoacetamide
-
Saccharomyces cerevisiae
L-gulono-1,4-lactone
competitive inhibition
Saccharomyces cerevisiae
N-ethylmaleimide
-
Saccharomyces cerevisiae
p-chloromercuriphenyl sulfonate
-
Saccharomyces cerevisiae
Sulfide
-
Saccharomyces cerevisiae
sulfite
-
Saccharomyces cerevisiae
Ki Value [mM] (protein specific)
Ki Value [mM]
Ki Value maximum [mM]
Inhibitor
Commentary
Organism
Structure
3.3
-
D-galactono-1,4-lactone
-
Saccharomyces cerevisiae
6.52
-
L-gulono-1,4-lactone
-
Saccharomyces cerevisiae
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
0.16
-
D-arabino-1,4-lactone
-
Saccharomyces cerevisiae
0.18
-
oxygen
-
Saccharomyces cerevisiae
0.3
-
L-galactono-1,4-lactone
-
Saccharomyces cerevisiae
0.36
-
L-Fucono-1,4-lactone
-
Saccharomyces cerevisiae
2
-
D-Altrono-1,4-lactone
-
Saccharomyces cerevisiae
15
-
D-threono-1,4-lactone
-
Saccharomyces cerevisiae
Localization (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrion
-
Saccharomyces cerevisiae
5739
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
Organism
Structure
Iron
enzyme contains an iron-sulfur cluster
Saccharomyces cerevisiae
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
18000
-
4 * 18000, SDS-PAGE
Saccharomyces cerevisiae
70000
-
gel filtration in presence of deoxycholate
Saccharomyces cerevisiae
74000
-
non-denaturing gradient PAGE in presence of deoxycholate
Saccharomyces cerevisiae
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-galactono-1,4-lactone + O2
Saccharomyces cerevisiae
-
L-ascorbate + H2O2
-
-
-
Purification (Commentary) (protein specific)
Commentary
Organism
-
Saccharomyces cerevisiae
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
3.448
-
-
Saccharomyces cerevisiae
Storage Stability (protein specific)
Storage Stability
Organism
5°C, 6 months, 50% loss of activity
Saccharomyces cerevisiae
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
D-altrono-1,4-lactone + O2
-
389744
Saccharomyces cerevisiae
?
-
-
-
?
D-arabinono-1,4-lactone + O2
-
389744
Saccharomyces cerevisiae
?
-
-
-
?
D-threono-1,4-lactone + O2
-
389744
Saccharomyces cerevisiae
?
-
-
-
?
L-fucono-1,4-lactone + O2
-
389744
Saccharomyces cerevisiae
?
-
-
-
?
L-galactono-1,4-lactone + O2
-
389744
Saccharomyces cerevisiae
L-ascorbate + H2O2
-
-
-
-
L-galactono-1,4-lactone + O2
-
389744
Saccharomyces cerevisiae
L-ascorbate + H2O2
-
389744
Saccharomyces cerevisiae
?
Subunits (protein specific)
Subunits
Commentary
Organism
tetramer
4 * 18000, SDS-PAGE
Saccharomyces cerevisiae
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
8.9
-
-
Saccharomyces cerevisiae
Other publictions for EC 1.3.3.12
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
724431
Kudryashova
Galactonolactone oxidoreductas ...
Trypanosoma cruzi, Trypanosoma cruzi X10/6
Biochim. Biophys. Acta
1814
545-552
2011
-
1
1
-
1
-
-
-
-
-
-
2
-
6
-
-
1
-
1
-
1
-
10
1
-
-
-
-
2
-
-
1
-
-
-
-
1
1
1
-
1
-
-
-
-
-
-
-
-
2
-
-
-
1
1
-
1
-
10
1
-
-
-
-
2
-
-
-
-
2
2
-
-
-
684985
Logan
The terminal step in vitamin C ...
Trypanosoma cruzi
Biochem. J.
407
419-426
2007
-
-
1
-
6
-
4
2
-
-
1
-
-
5
-
-
1
-
-
2
-
-
2
-
-
-
1
2
1
-
-
1
-
-
-
-
-
1
1
-
6
-
-
4
-
2
-
-
1
-
-
-
-
1
-
2
-
-
2
-
-
-
1
2
1
-
-
-
-
-
-
-
-
-
389748
Nishikimi
-
Identification by bacterial ex ...
Saccharomyces cerevisiae
Biochem. Mol. Biol. Int.
44
907-913
1998
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
1
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
389749
De Gara
-
The biogenesis of galactone-ga ...
Avena sativa
Phytochemistry
31
755-756
1992
-
-
-
-
-
-
1
-
1
-
-
1
-
1
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
1
-
-
1
-
-
-
-
-
-
-
-
2
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
389744
Bleeg
Biosynthesis of ascorbate in y ...
Saccharomyces cerevisiae
Eur. J. Biochem.
127
391-396
1982
-
-
-
-
-
-
7
6
1
1
3
1
-
2
-
-
1
-
-
-
1
1
6
1
-
-
-
-
1
-
-
1
2
-
-
-
-
-
1
-
-
-
-
7
2
6
1
1
3
1
-
-
-
1
-
-
1
1
6
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
389745
Noguchi
Studies on the sulfhydryl grou ...
Saccharomyces cerevisiae
J. Biochem.
90
33-38
1981
-
-
-
-
-
-
7
-
-
-
-
1
-
1
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
7
-
-
-
-
-
1
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
389746
Kenney
Identification of the covalent ...
Saccharomyces cerevisiae
FEBS Lett.
97
40-42
1979
-
-
-
-
-
-
-
-
-
-
-
1
-
2
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
389747
Nishikimi
Occurrence in yeast of L-galac ...
Saccharomyces cerevisiae
Arch. Biochem. Biophys.
191
479-486
1978
-
-
-
-
-
-
1
-
1
-
2
1
-
3
-
-
1
-
-
-
1
-
4
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
1
-
-
1
-
2
1
-
-
-
1
-
-
1
-
4
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-