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Information on EC 1.1.3.8 - L-gulonolactone oxidase and Organism(s) Mus musculus and UniProt Accession P58710
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1.1.3.8 L-gulonolactone oxidaseIUBMB Comments
A microsomal flavoprotein (FAD). The product spontaneously isomerizes to L-ascorbate. While most higher animals can synthesize asborbic acid, primates and guinea pigs cannot .
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Word Map
- 1.1.3.8
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l-ascorbic
- scurvy
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scurvy-prone
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levoglucosenone
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scorbutic
- dibenzothiophene
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shionogi
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lemongrass
- l-galactono-1,4-lactone
- nutrition
- medicine
- molecular biology
The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
lgo, l-gulonolactone oxidase, l-gulono-gamma-lactone oxidase, gulonolactone oxidase, l-gulono-1,4-lactone oxidase, gullo, gloase, atgullo5, l-gulono-1,4-lactone dehydrogenase, atgullo2, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L-gulono-gamma-lactone oxidase
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L-gulono-gamma-lactone: O2 oxidoreductase
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L-gulono-gamma-lactone:oxidoreductase
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LGO
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-gulono-1,4-lactone + O2 = L-xylo-hex-2-ulono-1,4-lactone + H2O2
product isomerizes spontaneously to L-ascorbate
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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oxidation
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reduction
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SYSTEMATIC NAME
IUBMB Comments
L-gulono-1,4-lactone:oxygen 3-oxidoreductase
A microsomal flavoprotein (FAD). The product spontaneously isomerizes to L-ascorbate. While most higher animals can synthesize asborbic acid, primates and guinea pigs cannot [3].
CAS REGISTRY NUMBER
COMMENTARY
9028-78-8
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
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product isomerizes spontaneously to L-ascorbate
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additional information
?
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examination of metabolic role of vitamin C synthesis in cells or animals that, during evolution, have lost the ability to make ascorbic acid
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?
additional information
?
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examination of metabolic role of vitamin C synthesis in cells or animals that, during evolution, have lost the ability to make ascorbic acid
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?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
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examination of metabolic role of vitamin C synthesis in cells or animals that, during evolution, have lost the ability to make ascorbic acid
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?
additional information
?
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examination of metabolic role of vitamin C synthesis in cells or animals that, during evolution, have lost the ability to make ascorbic acid
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?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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clofibrate-treated mouse enzyme is 8.5fold as active as non-treated mouse enzyme in the microsome and 500fold as active in the peroxisome
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
a deficiency in GULO expression results in the inability to produce vitamin C. Using a previously derived Gulo-expressing vector, which produces murine GULO under the control of the murine cytomegalovirus (mCMV) promoter, a recombinant helper-dependent adenovirus (HDAd-mCMV-Gulo) is constructed that can be used to correct this genetic defect. A human liver cell line (Hep G2) infected with the HDAd-mCMV-Gulo vector expresses GULO in a time- and gene dose-dependent manner. These cells also produce ascorbic acid when exogenous gulonolactone is supplemented in the medium. Likewise, Gulo(-/-) mice treated with HDAd-mCMV-Gulo express GULO in the liver and produce ascorbic acid
malfunction
physiological function
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L-gulonolactone oxidase plays an important role in vitamin C biosynthesis
malfunction
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gulonolactone oxidase knockout mice that are unable to synthesize their own ascorbic acid during development
malfunction
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L-gulono-gamma-lactone dehydrogenase knockout mice are unable to synthesize ascorbic acid (vitamin C) and are not protected from malaria infection
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). GGLO_MOUSE
440
0
50478
Swiss-Prot
other Location (Reliability: 2)
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
there is a dramatic decrease in L-gulonolactone oxidase expression in beta-catenin-deficient livers as compared with the wild type livers
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
a gene therapy approach can be successfully employed in the treatment and further study of vitamin C deficiency in scurvy-prone mammals
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Braun, L.; Mile, V.; Schaff, Z.; Csala, M.; Kardon, T.; Mandl, J.; Banhegyi, G.
Induction and peroxisomal appearance of gulonolactone oxidase upon clofibrate treatment in mouse liver
FEBS Lett.
458
359-362
1999
Mus musculus, no activity in Cavia porcellus, no activity in Homo sapiens, no activity in primates
Ha, M.N.; Graham, F.L.; D'Souza, C.K.; Muller, W.J.; Igdoura, S.A.; Schellhorn, H.E.
Functional rescue of vitamin C synthesis deficiency in human cells using adenoviral-based expression of murine l-gulono-gamma-lactone oxidase
Genomics
83
482-492
2004
Mus musculus (P58710), Mus musculus
Kim, H.J.; Lee, S.I.; Lee, D.H.; Smith, D.; Jo, H.; Schellhorn, H.E.; Boo, Y.C.
Ascorbic acid synthesis due to L-gulono-1,4-lactone oxidase expression enhances NO production in endothelial cells
Biochem. Biophys. Res. Commun.
345
1657-1662
2006
Mus musculus
Li, Y.; Shi, C.; Mossman, K.; Rosenfeld, J.; Boo, Y.; Schellhorn, H.
Restoration of vitamin C synthesis in transgenic Gulo-/- mice by helper-dependent adenovirus-based expression of gulonolactone oxidase
Hum. Gene Ther.
19
1349-1357
2008
Mus musculus (P58710), Mus musculus
Harrison, F.E.; Meredith, M.E.; Dawes, S.M.; Saskowski, J.L.; May, J.M.
Low ascorbic acid and increased oxidative stress in gulo(-/-) mice during development
Brain Res.
1349
143-152
2010
Mus musculus
Herbas, M.S.; Suzuki, H.
Vitamin C deficiency fails to protect mice from malaria
Exp. Anim.
59
239-243
2010
Mus musculus
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