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Information on EC 1.1.3.37 - D-arabinono-1,4-lactone oxidase and Organism(s) Arabidopsis thaliana and UniProt Accession Q6NQ66
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1.1.3.37 D-arabinono-1,4-lactone oxidaseIUBMB Comments
A flavoprotein (FAD). L-Galactono-1,4-lactone, L-gulono-1,4-lactone and L-xylono-1,4-lactone can also act as substrates but D-glucono-1,5-lactone, L-arabinono-1,4-lactone, D-galactono-1,4-lactone and D-gulono-1,4-lactone cannot . With L-galactono-1,4-lactone as substrate, the product is L-ascorbate . The product dehydro-D-arabinono-1,4-lactone had previously been referred to erroneously as D-erythroascorbate (CAS no.: 5776-48-7; formula: C6H8O6), although it was referred to as a five-carbon compound .
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Word Map
- 1.1.3.37
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l-ascorbic
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d-erythroascorbic
- l-galactose
- albicans
- l-gulono-1,4-lactone
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gel-filtration
- cauliflower
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multicopy
- p-chloromercuribenzoate
- flavin
- l-xylose
- nadp+
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sephacryl
- n-ethylmaleimide
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five-carbon
- l-fucose
The taxonomic range for the selected organisms is: Arabidopsis thaliana
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
d-arabinono-1,4-lactone oxidase, ara2p, arabinonolactone oxidase, l-galactono-gamma-lactone oxidase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ALO
L-galactono-gamma-lactone oxidase
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Oxidase, D-arabinono-gamma-lactone
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ALO
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oxidation
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SYSTEMATIC NAME
IUBMB Comments
D-arabinono-1,4-lactone:oxygen oxidoreductase
A flavoprotein (FAD). L-Galactono-1,4-lactone, L-gulono-1,4-lactone and L-xylono-1,4-lactone can also act as substrates but D-glucono-1,5-lactone, L-arabinono-1,4-lactone, D-galactono-1,4-lactone and D-gulono-1,4-lactone cannot [1]. With L-galactono-1,4-lactone as substrate, the product is L-ascorbate [3]. The product dehydro-D-arabinono-1,4-lactone had previously been referred to erroneously as D-erythroascorbate (CAS no.: 5776-48-7; formula: C6H8O6), although it was referred to as a five-carbon compound [1].
CAS REGISTRY NUMBER
COMMENTARY
182372-12-9
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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
additional information
?
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the enzyme catalyzes the reaction of L-gulonolactone oxidase, EC 1.1.3.8, producing 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, producing 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, producing 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, producing 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, producing L-ascorbate, but has sequence similarities to D-arabinono-1,4-lactone oxidase, EC 1.1.3.37
-
-
?
additional information
?
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the enzyme catalyzes the reaction of L-gulonolactone oxidase, EC 1.1.3.8, producing L-ascorbate, but has sequence similarities to D-arabinono-1,4-lactone oxidase, EC 1.1.3.37
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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
?
-
the enzyme catalyzes the reaction of L-gulonolactone oxidase, EC 1.1.3.8, producing 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, producing 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, producing 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, producing 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, producing 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, producing L-ascorbate, but has sequence similarities to D-arabinono-1,4-lactone oxidase, EC 1.1.3.37
-
-
?
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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). 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)
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