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Information on EC 1.1.3.8 - L-gulonolactone oxidase and Organism(s) Arabidopsis thaliana and UniProt Accession Q6NQ66
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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
-
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: Arabidopsis thaliana
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, atgullo2, l-gulono-1,4-lactone dehydrogenase, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
GulLO5
L-gulono-1,4-lactone oxidase
L-gulono-gamma-lactone oxidase
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-
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L-gulono-gamma-lactone: O2 oxidoreductase
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-
-
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L-gulono-gamma-lactone:oxidoreductase
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LGO
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-
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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-ascorbate + H2O2
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-
-
?
L-galactono-1,4-lactone + O2
L-ascorbic acid + H2O2
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-
-
?
L-gulono-1,4-lactone + cytochrome C
L-ascorbate + ?
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-
-
?
L-gulono-1,4-lactone + O2
L-ascorbate + H2O2
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-
-
?
additional information
?
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the enzyme catalyzes the reaction of L-gulonolactone oxidase, EC 1.1.3.8, producting L-ascorbate, but has sequence similarities to D-arabinono-1,4-lactone oxidase, EC 1.1.3.37
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-
?
additional information
?
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the enzyme catalyzes the reaction of L-gulonolactone oxidase, EC 1.1.3.8, producting L-ascorbate, but has sequence similarities to D-arabinono-1,4-lactone oxidase, EC 1.1.3.37
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-
?
additional information
?
-
the enzyme catalyzes the reaction of L-gulonolactone oxidase, EC 1.1.3.8, producting L-ascorbate, but has sequence similarities to D-arabinono-1,4-lactone oxidase, EC 1.1.3.37
-
-
?
additional information
?
-
the enzyme catalyzes the reaction of L-gulonolactone oxidase, EC 1.1.3.8, producting L-ascorbate, but has sequence similarities to D-arabinono-1,4-lactone oxidase, EC 1.1.3.37
-
-
?
additional information
?
-
the enzyme catalyzes the reaction of L-gulonolactone oxidase, EC 1.1.3.8, producting L-ascorbate, but has sequence similarities to D-arabinono-1,4-lactone oxidase, EC 1.1.3.37
-
-
?
additional information
?
-
the enzyme catalyzes the reaction of L-gulonolactone oxidase, EC 1.1.3.8, producting L-ascorbate, but has sequence similarities to D-arabinono-1,4-lactone oxidase, EC 1.1.3.37
-
-
?
additional information
?
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no dehydrogenase or oxidase activity with L-galactono-1,4-lactone, D-galactono-1,4-lactone, and D-gluconic acid-gamma-lactone. No oxidase activity with L-gulono-1,4-lactone
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-
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additional information
?
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no dehydrogenase or oxidase activity with L-galactono-1,4-lactone, D-galactono-1,4-lactone, and D-gluconic acid-gamma-lactone. No oxidase activity with L-gulono-1,4-lactone
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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
L-gulono-1,4-lactone + O2
L-ascorbate + H2O2
-
-
-
?
L-gulono-1,4-lactone + O2
L-ascorbate + H2O2
-
-
-
?
additional information
?
-
the enzyme catalyzes the reaction of L-gulonolactone oxidase, EC 1.1.3.8, producting L-ascorbate, but has sequence similarities to D-arabinono-1,4-lactone oxidase, EC 1.1.3.37
-
-
?
additional information
?
-
the enzyme catalyzes the reaction of L-gulonolactone oxidase, EC 1.1.3.8, producting L-ascorbate, but has sequence similarities to D-arabinono-1,4-lactone oxidase, EC 1.1.3.37
-
-
?
additional information
?
-
the enzyme catalyzes the reaction of L-gulonolactone oxidase, EC 1.1.3.8, producting L-ascorbate, but has sequence similarities to D-arabinono-1,4-lactone oxidase, EC 1.1.3.37
-
-
?
additional information
?
-
the enzyme catalyzes the reaction of L-gulonolactone oxidase, EC 1.1.3.8, producting L-ascorbate, but has sequence similarities to D-arabinono-1,4-lactone oxidase, EC 1.1.3.37
-
-
?
additional information
?
-
the enzyme catalyzes the reaction of L-gulonolactone oxidase, EC 1.1.3.8, producting L-ascorbate, but has sequence similarities to D-arabinono-1,4-lactone oxidase, EC 1.1.3.37
-
-
?
additional information
?
-
the enzyme catalyzes the reaction of L-gulonolactone oxidase, EC 1.1.3.8, producting L-ascorbate, but has sequence similarities to D-arabinono-1,4-lactone oxidase, EC 1.1.3.37
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
L-gulono-1,4-lactone
enzyme activity is inhibited when L-gulono-1,4-lactone concentration is increased to 400 mM
NaCl
inhibitory (20-70% residual activity) between 5 and 300 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8 - 9
the enzyme has a higher activity between pH 8.0 and 9.0 compared to lower pH
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 40
the activity of the enzyme increases by up to 3fold when the temperature is changed from 20 to 25°C and the same is true until 35°C. At 40°C, the activity increases by at least another 1fold
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.2
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
physiological function
physiological function
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The enzyme is involved in biosynthesis of L-ascorbic acid, that has a key role in protecting plant cells and tissues from oxidative stress caused by multiple forms of abiotic stress. Arabidopsis thaliana lines overexpressing a myo-inositol oxygenase or an L-gulono-1,4-lactone oxidase, contain elevated ascorbate and display enhanced growth and biomass accumulation of both aerial and root tissues, marked positive effect in plant growth in lines engineered to contain elevated vitamin C content
physiological function
Nicotiana benthamiana leaves expressing GulLO3 do not show an increase in ascorbate content, but ascorbate content is increased in all leaves fed with L-gulono-1,4-lactone compared to water fed controls. Isoform GulLO3 protein is regulated post-transcriptionally by rapid turnover
physiological function
Nicotiana benthamiana leaves expressing GulLO5 do not show an increase in ascorbate content
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). GGLO2_ARATH
591
0
64970
Swiss-Prot
Mitochondrion (Reliability: 5)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
Arabidopsis thaliana lines overexpressing a myo-inositol oxygenase or an L-gulono-1,4-lactone oxidase, contain elevated ascorbate and display enhanced growth and biomass accumulation of both aerial and root tissues, marked positive effect in plant growth in lines engineered to contain elevated vitamin C content. The transgenic lines are tolerant to a wide range of abiotic stresses including salt, cold, and heat and ascorbate content of the transgenic lines remained higher than those of controls under the abiotic stresses tested. Also the effects of exposure to pyrene, a known inducer of oxidative stress in plants (leading to stunted growth of the aerial tissue, reduction in the number of root hairs, and inhibition of leaf expansion in wild-type plants) are less severe in the overexpressers
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cation exchange cholumn chromatography and nickel affinity column chromatography
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene AtGulLO2, transgenic expression of the isozyme in Nicotiana tabacum BY-2 cells, the overexpression does not affect the cells. Expression of His-tagged isozyme in Escherichia coli strain BL21(DE3)pLysS is not successful
gene AtGulLO3, transgenic expression of the isozyme in Nicotiana tabacum BY-2 cells, the overexpression does not affect the cells. Expression of His-tagged isozyme in Escherichia coli strain BL21(DE3)pLysS is not successful
gene AtGulLO5, transgenic expression of the isozyme in Nicotiana tabacum BY-2 cells, the overexpression does not affect the cells. Expression of His-tagged isozyme in Escherichia coli strain BL21(DE3)pLysS is not successful
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Maruta, T.; Ichikawa, Y.; Mieda, T.; Takeda, T.; Tamoi, M.; Yabuta, Y.; Ishikawa, T.; Shigeoka, S.
The contribution of Arabidopsis homologs of L-gulono-1,4-lactone oxidase to the biosynthesis of ascorbic acid
Biosci. Biotechnol. Biochem.
74
1494-1497
2010
Arabidopsis thaliana (O81030), Arabidopsis thaliana (Q6NQ66), Arabidopsis thaliana (Q9LYD8)
Lisko, K.A.; Torres, R.; Harris, R.S.; Belisle, M.; Vaughan, M.M.; Jullian, B.; Chevone, B.I.; Mendes, P.; Nessler, C.L.; Lorence, A.
Elevating vitamin C content via overexpression of myo-inositol oxygenase and l-gulono-1,4-lactone oxidase in Arabidopsis leads to enhanced biomass and tolerance to abiotic stresses
In Vitro Cell. Dev. Biol. Plant
49
643-655
2013
Arabidopsis thaliana, Arabidopsis thaliana Col-0
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