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Information on EC 1.3.3.12 - L-galactonolactone oxidase
for references in articles please use BRENDA:EC1.3.3.12
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EC Tree 1 Oxidoreductases
1.3 Acting on the CH-CH group of donors
1.3.3 With oxygen as acceptor
1.3.3.12 L-galactonolactone oxidase
IUBMB Comments
A flavoprotein. Acts on the 1,4-lactones of L-galactonic, D-altronic, L-fuconic, D-arabinic and D-threonic acids; not identical with EC 1.1.3.8 L-gulonolactone oxidase. (cf. EC 1.3.2.3 galactonolactone dehydrogenase).
The enzyme appears in viruses and cellular organisms
- 1.3.3.12
- flavin
-
non-covalently
- cruzi
- l-gulonolactone
-
chagas
- l-ascorbate
- n-ethylmaleimide
- iodoacetamide
-
trypanosomal
- pharmacology
showSynonyms
l-galactonolactone oxidase, galactonolactone oxidase, galactonolactone oxidoreductase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
EC 1.1.3.24
-
-
formerly
-
GAL
galactone-gamma-lactone oxidase
-
-
-
-
galactonolactone oxidoreductase
GL oxidase
-
-
-
-
L-galactono-1,4-lactone oxidase
-
-
-
-
L-galactono-gamma-lactone oxidase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-galactono-1,4-lactone + O2 = L-ascorbate + H2O2
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
L-galactono-1,4-lactone:oxygen 3-oxidoreductase
A flavoprotein. Acts on the 1,4-lactones of L-galactonic, D-altronic, L-fuconic, D-arabinic and D-threonic acids; not identical with EC 1.1.3.8 L-gulonolactone oxidase. (cf. EC 1.3.2.3 galactonolactone dehydrogenase).
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CAS REGISTRY NUMBER
COMMENTARY
69403-13-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
D-altronolactone + O2
?
-
Substrates: 68% of the activity with L-galactono-1,4-lactone
Products: -
Products: -
?
L-gulonolactone + O2
?
-
Substrates: 32% of the activity with L-galactono-1,4-lactone
Products: -
Products: -
?
D-arabinono-1,4-lactone + 1,4-benzoquinone
? + 1,4-benzoquinol
-
Substrates: artificial electron acceptor
Products: -
Products: -
?
D-arabinono-1,4-lactone + 1,4-benzoquinone
? + 1,4-benzoquinol
-
Substrates: artificial electron acceptor
Products: -
Products: -
?
L-galactono-1,4-lactone + 1,4-benzoquinone
L-ascorbate + 1,4-benzoquinol
-
Substrates: artificial electron acceptor
Products: -
Products: -
?
L-galactono-1,4-lactone + 1,4-benzoquinone
L-ascorbate + 1,4-benzoquinol
-
Substrates: artificial electron acceptor
Products: -
Products: -
?
L-galactono-1,4-lactone + O2
L-ascorbate + H2O2
-
Substrates: enzyme catalyzes the last step of L-ascorbic acid biosynthesis
Products: -
Products: -
?
L-galactono-1,4-lactone + O2
L-ascorbate + H2O2
-
Substrates: -
Products: -
Products: -
?
L-galactono-1,4-lactone + O2
L-ascorbate + H2O2
-
Substrates: enzyme catalyzes the last step of L-ascorbic acid biosynthesis
Products: -
Products: -
?
L-galactono-1,4-lactone + O2
L-ascorbate + H2O2
-
Substrates: -
Products: -
Products: -
?
L-galactono-1,4-lactone + O2
L-ascorbate + H2O2
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: the refolded enzyme is active with both L-galactono-1,4-lactone and D-arabinono-1,4-lactone
Products: -
Products: -
?
additional information
?
-
-
Substrates: the refolded enzyme is active with both L-galactono-1,4-lactone and D-arabinono-1,4-lactone
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-galactono-1,4-lactone + O2
L-ascorbate + H2O2
-
Substrates: enzyme catalyzes the last step of L-ascorbic acid biosynthesis
Products: -
Products: -
?
L-galactono-1,4-lactone + O2
L-ascorbate + H2O2
-
Substrates: -
Products: -
Products: -
?
L-galactono-1,4-lactone + O2
L-ascorbate + H2O2
-
Substrates: enzyme catalyzes the last step of L-ascorbic acid biosynthesis
Products: -
Products: -
?
L-galactono-1,4-lactone + O2
L-ascorbate + H2O2
-
Substrates: -
Products: -
Products: -
?
L-galactono-1,4-lactone + O2
L-ascorbate + H2O2
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
FAD
-
enzyme contains a covalently bound flavin
FAD
-
non-covalently bound FAD as redox-active cofactor, FAD-binding domain sequence of TcGAL and comparison to related aldonolactone oxidoreductases, overview
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
the synthesis of the enzyme is sensitive to both mitochondrial and cytoplasmic translation inhibitors
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
10.82
D-arabinono-1,4-lactone
-
in 50 mM potassium phosphate buffer, pH 8.0, with 1 mM EDTA
11.22
L-galactono-1,4-lactone
-
in 50 mM potassium phosphate buffer, pH 8.0, with 1 mM EDTA
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.285
D-arabinono-1,4-lactone
-
in 50 mM potassium phosphate buffer, pH 8.0, with 1 mM EDTA
0.161
L-galactono-1,4-lactone
-
in 50 mM potassium phosphate buffer, pH 8.0, with 1 mM EDTA
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.19
-
purified recombinant refolded enzyme, substrate D-arabinono-1,4-lactone. pH 8.8, temperature not specified in the publication
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
might be a multimeric enzyme, in which some polypeptide chains could be synthesized in the cytosol and others in the mitochondria
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
evolution
-
the terminal step in ascorbate biosynthesis is catalyzed by flavin-dependent aldonolactone oxidoreductases belonging to the vanillyl-alcohol oxidase (VAO) protein family
evolution
-
the terminal step in ascorbate biosynthesis is catalyzed by flavin-dependent aldonolactone oxidoreductases belonging to the vanillyl-alcohol oxidase (VAO) protein family
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). ALO1_CANAL
Candida albicans (strain SC5314 / ATCC MYA-2876)
557
0
63447
Swiss-Prot
other Location (Reliability: 2)
A0A422NB30_TRYRA
509
0
57346
TrEMBL
other Location (Reliability: 2)
A0A422PRC5_9TRYP
505
0
56785
TrEMBL
other Location (Reliability: 2)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer or dimer
tetramer
additional information
-
might be a multimeric enzyme, in which some polypeptide chains could be synthesized in the cytosol and others in the mitochondria
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A113G
-
site-directed mutagenesis, in the reaction with 1,4-benzoquinone as electron acceptor, the activity of the dimeric formof A113G is about 1.5fold higher compared to the monomer, the specific activity of the A113G variant in the reaction with molecular oxygen is about 2.5-3times lower than with 1,4-benzoquinone
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
K55G
-
the mutation has only a minor inhibitory effect on both FMN binding and biochemical activity
K55H
-
the mutation causes dramatically reduced FMN binding and enzyme activity (above 90%)
A113G
-
site-directed mutagenesis, in the reaction with 1,4-benzoquinone as electron acceptor, the activity of the dimeric formof A113G is about 1.5fold higher compared to the monomer, the specific activity of the A113G variant in the reaction with molecular oxygen is about 2.5-3times lower than with 1,4-benzoquinone
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
refolded recombinant N-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by anion exchange, hydroxyapatite, and hydrophobic interaction chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed as a fusion protein with glutathione S-transferase in Escherichia coli cells with the expression vector pGEX-5X-3
-
recombinant expression of the N-terminally His6-tagged enzyme in inclusion bodies in Escherichia coli strain BL21(DE3)
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant terminally His6-tagged enzyme refolded from Escherichia coli strain BL21(DE3) inclusion bodies using a reverse micelles system. The refolded enzyme shows native-like secondary structure and is active with both L-galactono-1,4-lactone and D-arabinono-1,4-lactone
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pharmacology
pharmacology
-
because humans lack the capacity to synthesize ascorbate, the trypanosomal enzymes involved in ascorbate biosynthesis are interesting targets for drug therapy
pharmacology
-
because humans lack the capacity to synthesize ascorbate, the trypanosomal enzymes involved in ascorbate biosynthesis are interesting targets for drug therapy
-
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Eur. J. Biochem.
127
391-396
1982
Saccharomyces cerevisiae
brenda
Noguchi, E.; Nishikimi, M.; Yagi, K.
Studies on the sulfhydryl group of L-galactonolactone oxidase
J. Biochem.
90
33-38
1981
Saccharomyces cerevisiae
brenda
Kenney, W.C.; Edmondson, D.E.; Singer, T.P.; Nishikimi, M.; Noguchi, E.; Yagi, K.
Identification of the covalently-bound flavin of L-galactonolactone oxidase from yeast
FEBS Lett.
97
40-42
1979
Saccharomyces cerevisiae
brenda
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
Arch. Biochem. Biophys.
191
479-486
1978
Saccharomyces cerevisiae
brenda
Nishikimi, M.; Ohta, Y.; Ishikawa, T.
Identification by bacterial expression of the yeast genomic sequence encoding L-galactono-gamma-lactone oxidase, the homolog of L-ascorbic acid-synthesizing enzyme of higher animals
Biochem. Mol. Biol. Int.
44
907-913
1998
Saccharomyces cerevisiae
-
brenda
De Gara, L.; Tommasi, F.; Liso, R.; Arrigoni, O.
The biogenesis of galactone-gamma-lactone oxidase in Avena sativa embryos
Phytochemistry
31
755-756
1992
Avena sativa
-
brenda
Logan, F.J.; Taylor, M.C.; Wilkinson, S.R.; Kaur, H.; Kelly, J.M.
The terminal step in vitamin C biosynthesis in Trypanosoma cruzi is mediated by a FMN-dependent galactonolactone oxidase
Biochem. J.
407
419-426
2007
Trypanosoma cruzi
brenda
Kudryashova, E.V.; Leferink, N.G.; Slot, I.G.; van Berkel, W.J.
Galactonolactone oxidoreductase from Trypanosoma cruzi employs a FAD cofactor for the synthesis of vitamin C
Biochim. Biophys. Acta
1814
545-552
2011
Trypanosoma cruzi, Trypanosoma cruzi X10/6
brenda
EXTERNAL LINKS (specific for EC-Number 1.3.3.12)
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