BRENDA - Enzyme Database
show all sequences of 1.3.3.12

The terminal step in vitamin C biosynthesis in Trypanosoma cruzi is mediated by a FMN-dependent galactonolactone oxidase

Logan, F.J.; Taylor, M.C.; Wilkinson, S.R.; Kaur, H.; Kelly, J.M.; Biochem. J. 407, 419-426 (2007)

Data extracted from this reference:

Cloned(Commentary)
Cloned (Commentary)
Organism
expressed in Escherichia coli BL-21+ cells
Trypanosoma cruzi
Engineering
Protein Variants
Commentary
Organism
H447G
the mutant is inactive and shows undetectable FMN binding
Trypanosoma cruzi
K450G
the substitution results in an enzyme that retains an ability to bind FMN (around 50%of the wild type enzyme), but which exhibits no activity
Trypanosoma cruzi
K55G
the mutation has only a minor inhibitory effect on both FMN binding and biochemical activity
Trypanosoma cruzi
K55H
the mutation causes dramatically reduced FMN binding and enzyme activity (above 90%)
Trypanosoma cruzi
K55L
the mutant is inactive and shows undetectable FMN binding
Trypanosoma cruzi
W448G
the mutant is inactive and shows undetectable FMN binding
Trypanosoma cruzi
Inhibitors
Inhibitors
Commentary
Organism
Structure
Hg2+
complete inhibition at 1 mM
Trypanosoma cruzi
N-ethylmaleimide
77% inhibition at 1 mM
Trypanosoma cruzi
p-chloromercuribenzoate
complete inhibition at 1 mM
Trypanosoma cruzi
Zn2+
63% inhibition at 1 mM
Trypanosoma cruzi
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
10.82
-
D-arabinono-1,4-lactone
in 50 mM potassium phosphate buffer, pH 8.0, with 1 mM EDTA
Trypanosoma cruzi
11.22
-
L-galactono-1,4-lactone
in 50 mM potassium phosphate buffer, pH 8.0, with 1 mM EDTA
Trypanosoma cruzi
Molecular Weight [Da]
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
57000
-
SDS-PAGE
Trypanosoma cruzi
Organism
Organism
UniProt
Commentary
Textmining
Trypanosoma cruzi
-
-
-
Purification (Commentary)
Purification (Commentary)
Organism
Ni-NTA column chromatography
Trypanosoma cruzi
Source Tissue
Source Tissue
Commentary
Organism
Textmining
amastigote
-
Trypanosoma cruzi
-
epimastigote
-
Trypanosoma cruzi
-
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
Substrate Product ID
D-arabinono-1,4-lactone + O2
-
684985
Trypanosoma cruzi
?
-
-
-
?
L-galactono-1,4-lactone + O2
-
684985
Trypanosoma cruzi
L-ascorbate + H2O2
-
-
-
?
Synonyms
Synonyms
Commentary
Organism
GAL
-
Trypanosoma cruzi
galactonolactone oxidase
-
Trypanosoma cruzi
Temperature Stability [°C]
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
50
-
heat-inactivated above 50°C
Trypanosoma cruzi
Turnover Number [1/s]
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.161
-
L-galactono-1,4-lactone
in 50 mM potassium phosphate buffer, pH 8.0, with 1 mM EDTA
Trypanosoma cruzi
0.285
-
D-arabinono-1,4-lactone
in 50 mM potassium phosphate buffer, pH 8.0, with 1 mM EDTA
Trypanosoma cruzi
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
8
-
Trypanosoma cruzi
Cofactor
Cofactor
Commentary
Organism
Structure
FMN
dependent on non-covalently-bound FMN
Trypanosoma cruzi
Cloned(Commentary) (protein specific)
Commentary
Organism
expressed in Escherichia coli BL-21+ cells
Trypanosoma cruzi
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
FMN
dependent on non-covalently-bound FMN
Trypanosoma cruzi
Engineering (protein specific)
Protein Variants
Commentary
Organism
H447G
the mutant is inactive and shows undetectable FMN binding
Trypanosoma cruzi
K450G
the substitution results in an enzyme that retains an ability to bind FMN (around 50%of the wild type enzyme), but which exhibits no activity
Trypanosoma cruzi
K55G
the mutation has only a minor inhibitory effect on both FMN binding and biochemical activity
Trypanosoma cruzi
K55H
the mutation causes dramatically reduced FMN binding and enzyme activity (above 90%)
Trypanosoma cruzi
K55L
the mutant is inactive and shows undetectable FMN binding
Trypanosoma cruzi
W448G
the mutant is inactive and shows undetectable FMN binding
Trypanosoma cruzi
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
Hg2+
complete inhibition at 1 mM
Trypanosoma cruzi
N-ethylmaleimide
77% inhibition at 1 mM
Trypanosoma cruzi
p-chloromercuribenzoate
complete inhibition at 1 mM
Trypanosoma cruzi
Zn2+
63% inhibition at 1 mM
Trypanosoma cruzi
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
10.82
-
D-arabinono-1,4-lactone
in 50 mM potassium phosphate buffer, pH 8.0, with 1 mM EDTA
Trypanosoma cruzi
11.22
-
L-galactono-1,4-lactone
in 50 mM potassium phosphate buffer, pH 8.0, with 1 mM EDTA
Trypanosoma cruzi
Molecular Weight [Da] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
57000
-
SDS-PAGE
Trypanosoma cruzi
Purification (Commentary) (protein specific)
Commentary
Organism
Ni-NTA column chromatography
Trypanosoma cruzi
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
amastigote
-
Trypanosoma cruzi
-
epimastigote
-
Trypanosoma cruzi
-
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
ID
D-arabinono-1,4-lactone + O2
-
684985
Trypanosoma cruzi
?
-
-
-
?
L-galactono-1,4-lactone + O2
-
684985
Trypanosoma cruzi
L-ascorbate + H2O2
-
-
-
?
Temperature Stability [°C] (protein specific)
Temperature Stability Minimum [°C]
Temperature Stability Maximum [°C]
Commentary
Organism
50
-
heat-inactivated above 50°C
Trypanosoma cruzi
Turnover Number [1/s] (protein specific)
Turnover Number Minimum [1/s]
Turnover Number Maximum [1/s]
Substrate
Commentary
Organism
Structure
0.161
-
L-galactono-1,4-lactone
in 50 mM potassium phosphate buffer, pH 8.0, with 1 mM EDTA
Trypanosoma cruzi
0.285
-
D-arabinono-1,4-lactone
in 50 mM potassium phosphate buffer, pH 8.0, with 1 mM EDTA
Trypanosoma cruzi
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
7.5
8
-
Trypanosoma cruzi
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
Synonyms
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
-
8
-
-
1
-
1
-
1
-
10
1
2
-
-
-
-
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
-
-
7
-
-
1
-
-
2
-
-
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
-
3
-
-
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
-
3
-
-
1
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
1
-
-
-
1
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
389747
Nishikimi
Occurrence in yeast of L-galac ...
Saccharomyces cerevisiae
Arch. Biochem. Biophys.
191
479-486
1978
-
-
-
-
-
-
1
-
1
-
2
1
-
5
-
-
1
-
-
-
1
-
4
1
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
1
-
-
-
-
1
-
-
1
-
2
1
-
-
-
1
-
-
1
-
4
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-