Information on EC 1.1.3.8 - L-gulonolactone oxidase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
1.1.3.8
-
RECOMMENDED NAME
GeneOntology No.
L-gulonolactone oxidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
L-gulono-1,4-lactone + O2 = L-xylo-hex-2-ulono-1,4-lactone + H2O2
show the reaction diagram
product isomerizes spontaneously to L-ascorbate
-
L-gulono-1,4-lactone + O2 = L-xylo-hex-2-ulono-1,4-lactone + H2O2
show the reaction diagram
product isomerizes spontaneously to L-ascorbate
-
L-gulono-1,4-lactone + O2 = L-xylo-hex-2-ulono-1,4-lactone + H2O2
show the reaction diagram
product isomerizes spontaneously to L-ascorbate
-
L-gulono-1,4-lactone + O2 = L-xylo-hex-2-ulono-1,4-lactone + H2O2
show the reaction diagram
product isomerizes spontaneously to L-ascorbate
-
L-gulono-1,4-lactone + O2 = L-xylo-hex-2-ulono-1,4-lactone + H2O2
show the reaction diagram
product isomerizes spontaneously to L-ascorbate
-
L-gulono-1,4-lactone + O2 = L-xylo-hex-2-ulono-1,4-lactone + H2O2
show the reaction diagram
product isomerizes spontaneously to L-ascorbate
-
L-gulono-1,4-lactone + O2 = L-xylo-hex-2-ulono-1,4-lactone + H2O2
show the reaction diagram
product isomerizes spontaneously to L-ascorbate
-
L-gulono-1,4-lactone + O2 = L-xylo-hex-2-ulono-1,4-lactone + H2O2
show the reaction diagram
product isomerizes spontaneously to L-ascorbate
-
L-gulono-1,4-lactone + O2 = L-xylo-hex-2-ulono-1,4-lactone + H2O2
show the reaction diagram
product isomerizes spontaneously to L-ascorbate
-
L-gulono-1,4-lactone + O2 = L-xylo-hex-2-ulono-1,4-lactone + H2O2
show the reaction diagram
product isomerizes spontaneously to L-ascorbate
-
L-gulono-1,4-lactone + O2 = L-xylo-hex-2-ulono-1,4-lactone + H2O2
show the reaction diagram
product isomerizes spontaneously to L-ascorbate
-
L-gulono-1,4-lactone + O2 = L-xylo-hex-2-ulono-1,4-lactone + H2O2
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Ascorbate and aldarate metabolism
-
Metabolic pathways
-
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].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
AtGulLO2
Q6NQ66
-
AtGulLO3
Q9LYD8
-
AtGulLO5
O81030
-
GLO
-
-
GULO
P58710
-
gulonolactone oxidase
-
-
gulonolactone oxidase
P58710
-
L-gluconon-1,4-lactone
-
-
L-GulL oxidase
O81030, Q6NQ66, Q9LYD8
-
L-gulono-1,4-lactone dehydrogenase
-
-
L-gulono-1,4-lactone oxidase
O81030, Q6NQ66, Q9LYD8
-
L-gulono-gamma-lactone dehydrogenase
-
-
L-gulono-gamma-lactone oxidase
-
-
-
-
L-gulono-gamma-lactone oxidase
-
-
L-gulono-gamma-lactone oxidase
-
-
L-gulono-gamma-lactone oxidase
-
-
L-gulono-gamma-lactone oxidase
-
-
L-gulono-gamma-lactone oxidase
-
-
L-gulono-gamma-lactone oxidase
Q90YK3
-
L-gulono-gamma-lactone oxidase
-
-
L-gulono-gamma-lactone oxidase
-
-
L-gulono-gamma-lactone: O2 oxidoreductase
-
-
-
-
L-gulono-gamma-lactone:oxidoreductase
-
-
-
-
L-gulonolactone oxidase
-
-
LGO
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9028-78-8
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
Siberian sturgeon
-
-
Manually annotated by BRENDA team
lake sturgeon
-
-
Manually annotated by BRENDA team
white sturgeon
-
-
Manually annotated by BRENDA team
transgenic plants of Lattuca sativa inoculated with Agrobacterium tumefaciens harboring a plasmid with enzyme gene
-
-
Manually annotated by BRENDA team
bowfin
-
-
Manually annotated by BRENDA team
AtGulLO2; isozyme AtGulLO2
UniProt
Manually annotated by BRENDA team
AtGulLO3; isozyme AtGulLO3
UniProt
Manually annotated by BRENDA team
AtGulLO5; isozyme AtGulLO5
UniProt
Manually annotated by BRENDA team
embryo
-
-
Manually annotated by BRENDA team
strain DSM 4025
-
-
Manually annotated by BRENDA team
brindled bandicoot
-
-
Manually annotated by BRENDA team
commentary
-
-
Manually annotated by BRENDA team
expression in HEK cells
Q8K152
Swissprot
Manually annotated by BRENDA team
mouse treated with clofibrate, a peroxisome proliferator
-
-
Manually annotated by BRENDA team
no activity in Cavia porcellus
-
-
-
Manually annotated by BRENDA team
no activity in Cavia porcellus
guinea pig
-
-
Manually annotated by BRENDA team
no activity in Homo sapiens
-
-
-
Manually annotated by BRENDA team
no activity in Mus musculus
-
-
-
Manually annotated by BRENDA team
no activity in Oncorhynchus mykiss
teleost fish rainbow trout
-
-
Manually annotated by BRENDA team
no activity in primates
-
-
-
Manually annotated by BRENDA team
long-nosed bandicoot
-
-
Manually annotated by BRENDA team
expression in wild type and in vitamin-C-deficient Arabidopsis thaliana
-
-
Manually annotated by BRENDA team
similar enzyme: L-galactono-1,4-lactone oxidase
-
-
Manually annotated by BRENDA team
cloudy catshark
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
P58710
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
-
gulonolactone oxidase knockout mice that are unable to synthesize their own ascorbic acid during development
malfunction
-
L-gulono-gamma-lactone dehydrogenase knockout mice are unable to synthesize ascorbic acid (vitamin C) and are not protected from malaria infection
metabolism
-
L-gulono-gamma-lactone oxidase is a key enzyme for the biosynthesis of ascorbate, it catalyzes the final step of ascorbate biosynthesis in which L-gulonolactone is oxidized to ascorbate
physiological function
-
the effect of vitamin A deficiency in chicks on tissue ascorbic acid, plasma oxidant status and antioxidant capacity, and renal GULO oxidase activity in broiler chickens is investigated. Chicks are fed a practical diet with vitamin A (control) or the same diet without supplemental vitamin A from day-old to 23 or 30 days of age. Growth, feed intake, relative weights of bursa of Fabricius, liver, spleen and testis are significantly reduced in vitamin A-deficient chicks. Vitamin A deficiency depresses renal GULO activity between 20% to 30%
physiological function
-
L-gulono-gamma-lactone oxidase is a key enzyme required during the synthesis of L-ascorbic acid
physiological function
Q90YK3, -
L-gulono-gamma-lactone oxidase is a key enzyme required during the synthesis of L-ascorbic acid
physiological function
-
L-gulonolactone oxidase plays an important role in vitamin C biosynthesis
physiological function
-
L-gulono-gamma-lactone oxidase is a key enzyme for the biosynthesis of ascorbate, which is essential for several cellular functions. The fish vitamin C requirements are highest during early life stages
metabolism
-
L-gulono-gamma-lactone oxidase is a key enzyme for the biosynthesis of ascorbate, it catalyzes the final step of ascorbate biosynthesis in which L-gulonolactone is oxidized to ascorbate
additional information
-
transgenic plants with increased vitamin C content in the fruit show enhanced tolerance to abiotic stresses induced by methyl viologen, NaCl, and mannitol as compared with wild-type plants. The leaf disc senescence assay show better tolerance in transgenic plants by retaining higher chlorophyll content compared with wild-type plants, phenotypes, overview
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
creatol + O2
methylguanidine + ?
show the reaction diagram
-
creatone A and creatone B are intermediates
-
-
?
D-altrono-1,4-lactone + O2
?
show the reaction diagram
-
-
-
-
?
D-altrono-1,4-lactone + O2
?
show the reaction diagram
-
16% as active as L-gulono-1,4-lactone
-
-
?
D-glucono-1,4-lactone + O2
?
show the reaction diagram
-
4% as active as L-gulono-1,4-lactone
-
-
?
D-glucose + phenazine methosulfate + O2
D-glucosone + ?
show the reaction diagram
-
23.4% as active as L-gulono-1,4-lactone
-
-
?
D-mannono-1,4-lactone + O2
?
show the reaction diagram
-
64% as active as L-gulono-1,4-lactone
-
-
-
D-mannono-1,4-lactone + O2
?
show the reaction diagram
-
25% as active as L-gulono-1,4-lactone
-
-
?
D-mannose + phenazine methosulfate + O2
?
show the reaction diagram
-
6.4% as active as L-gulono-1,4-lactone
-
-
?
D-xylose + phenazine methosulfate + O2
D-xylosone + ?
show the reaction diagram
-
6.4% as active as L-gulono-1,4-lactone
-
-
?
L-galactono-1,4-lactone + O2
L-ascorbic acid + H2O2
show the reaction diagram
-
-
-
-
?
L-galactono-1,4-lactone + O2
L-ascorbic acid + H2O2
show the reaction diagram
-
90% as active as L-gulono-1,4-lactone
-
-
?
L-galactono-1,4-lactone + O2
L-ascorbic acid + H2O2
show the reaction diagram
-
2% as active as L-gulono-1,4-lactone
-
-
?
L-glucono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
-
-
r
L-glucono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
-
-
r
L-glucurono-1,4-lactone + phenazine methosulfate + O2
?
show the reaction diagram
-
6.4% as active as L-gulono-1,4-lactone
-
-
?
L-gulono-1,4-lactone + 2,6-dichlorophenolindophenol + O2
L-ascorbic acid + ?
show the reaction diagram
-
-
-
-
?
L-gulono-1,4-lactone + 2,6-dichlorophenolindophenol + O2
L-ascorbic acid + ?
show the reaction diagram
-
enzyme is a dehydrogenase, not an oxidase
-
-
?
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
-
-
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
-
-
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
-
-
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
-
-
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
-
-
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
-
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
-
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
-
-
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
-
-
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
-
-
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
-
-
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
Q8K152
-
-
-
?
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
product isomerizes spontaneously to L-ascorbate
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
product isomerizes spontaneously to L-ascorbate
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
product isomerizes spontaneously to L-ascorbate
?
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
product isomerizes spontaneously to L-ascorbate
?
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
product isomerizes spontaneously to L-ascorbate
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
product isomerizes spontaneously to L-ascorbate
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
product isomerizes spontaneously to L-ascorbate
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
product isomerizes spontaneously to L-ascorbate
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
product isomerizes spontaneously to L-ascorbate
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
product isomerizes spontaneously to L-ascorbate
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
product isomerizes spontaneously to L-ascorbate
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
product isomerizes spontaneously to L-ascorbate
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
product isomerizes spontaneously to L-ascorbate
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
product isomerizes spontaneously to L-ascorbate
?
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
product isomerizes spontaneously to L-ascorbate
?
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
product isomerizes spontaneously to L-ascorbate
?
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
product isomerizes spontaneously to L-ascorbate
?
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
product isomerizes spontaneously to L-ascorbate
?
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
product isomerizes spontaneously to L-ascorbate
?
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
product isomerizes spontaneously to L-ascorbate
?
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
product isomerizes spontaneously to L-ascorbate
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
product isomerizes spontaneously to L-ascorbate
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
product isomerizes spontaneously to L-ascorbate
?
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
product isomerizes spontaneously to L-ascorbate
?
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
product isomerizes spontaneously to L-ascorbate
?
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
product isomerizes spontaneously to L-ascorbate
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
the enzyme has a configurational specificity for the hydroxyl group at C-2
-
-
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
the enzyme has a configurational specificity for the hydroxyl group at C-2
product isomerizes spontaneously to L-ascorbate
?
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
key enzyme for L-ascorbic acid biosynthesis
-
-
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
the enzyme has a configurational specificity for the hydroxyl group at C(2)
-
-
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
the enzyme has a configurational specificity for the hydroxyl group at C(2)
-
-
-
L-gulono-1,4-lactone + O2
L-ascorbate + H2O2
show the reaction diagram
-
-
-
-
?
L-gulono-1,4-lactone + O2
L-ascorbate + H2O2
show the reaction diagram
-
-
-
-
?
L-gulono-1,4-lactone + O2
L-ascorbate + H2O2
show the reaction diagram
O81030, Q6NQ66, Q9LYD8
-
-
-
?
L-gulono-1,4-lactone + O2
L-ascorbate + H2O2
show the reaction diagram
-
-
-
-
?
L-gulono-1,4-lactone + phenazine methosulfate + O2
L-ascorbic acid + ?
show the reaction diagram
-
-
-
-
?
L-gulono-1,4-lactone + phenazine methosulfate + O2
L-ascorbic acid + ?
show the reaction diagram
-
enzyme is a dehydrogenase, not an oxidase
-
-
?
L-gulono-1,4-lactone + phenazine methosulfate + O2
L-ascorbic acid + ?
show the reaction diagram
-
reaction also takes place under anaerobic conditions
-
-
?
L-idono-1,4-lactone + O2
?
show the reaction diagram
-
3% as active as L-gulono-1,4-lactone
-
-
?
additional information
?
-
Q8K152
examination of metabolic role of vitamin C synthesis in cells or animals that, during evolution, have lost the ability to make ascorbic acid
-
-
-
additional information
?
-
-
presence of a alternative pathway for vitamin C production in plants which can circumvent steps of the D-mannose pathway
-
-
-
additional information
?
-
O81030, Q6NQ66, Q9LYD8
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
-
-
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
-
-
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
-
-
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
-
-
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
-
-
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
-
-
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
-
-
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
-
-
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
-
-
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
-
-
-
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
key enzyme for L-ascorbic acid biosynthesis
-
-
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
the enzyme has a configurational specificity for the hydroxyl group at C(2)
-
-
-
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
-
the enzyme has a configurational specificity for the hydroxyl group at C(2)
-
-
-
L-gulono-1,4-lactone + O2
L-ascorbate + H2O2
show the reaction diagram
-
-
-
-
?
L-gulono-1,4-lactone + O2
L-ascorbate + H2O2
show the reaction diagram
-
-
-
-
?
L-gulono-1,4-lactone + O2
L-ascorbate + H2O2
show the reaction diagram
O81030, Q6NQ66, Q9LYD8
-
-
-
?
L-gulono-1,4-lactone + O2
L-ascorbate + H2O2
show the reaction diagram
-
-
-
-
?
additional information
?
-
Q8K152
examination of metabolic role of vitamin C synthesis in cells or animals that, during evolution, have lost the ability to make ascorbic acid
-
-
-
additional information
?
-
-
presence of a alternative pathway for vitamin C production in plants which can circumvent steps of the D-mannose pathway
-
-
-
additional information
?
-
O81030, Q6NQ66, Q9LYD8
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 ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
FAD
-
covalently-bound
FAD
-
1 mol FAD per protein monomer; 8alpha-(N1-histidyl)riboflavin is the cofactor structure determined by high-voltage paper electrophoresis
FAD
-
8alpha-(N1-histidyl)riboflavin is the cofactor structure determined by high-voltage paper electrophoresis
FAD
-
8alpha-(N1-histidyl)riboflavin is the cofactor structure determined by high-voltage paper electrophoresis; covalently-bound
flavin
-
covalently bound, flavoenzyme
flavin
-
covalently bound, flavoenzyme
flavin
-
covalently bound, flavoenzyme
flavin
-
covalently bound, flavoenzyme
flavin
-
covalently bound, flavoenzyme
flavin
-
covalently bound, flavoenzyme
flavin
-
covalently bound, flavoenzyme
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
Cd2+
-
0.1 mM concentration 13% inhibition
Cu(NO3)2
-
0.19 mM concentration 12% inhibition, 0.38 mM concentration 76% inhibition and 0.89 mM concentration 100% inhibition
CuCl2 * 2H2O
-
0.19 mM concentration 16% inhibition, 0.38 mM concentration 92% inhibition and 0.89 mM concentration 100% inhibition
-
CuSO4
-
0.19 mM concentration 20% inhibition, 0.38 mM concentration 80% inhibition and 0.89 mM concentration 100% inhibition
Fe2(SO4)3
-
sub mM concentration slight inhibition
Hg2+
-
0.1 mM concentration 98% inhibition
L-ascorbic acid
-
high concentration supresses liver enzyme activity
MgCl2 * 6H2O
-
sub mM concentration slight inhibition
MgSO4 * 7H2O
-
sub mM concentration slight inhibition
MnCl2 * 4H2O
-
0.38 mM and 0.89 mM concentration 100% inhibition
Na2S
-
2 mM concentration 76% inhibition, 20 mM concentration 94% concentration
Na2SO3
-
5 mM concentration, 33% inhibition, 20 mM concentration 61% inhibition
NiSO4
-
sub mM concentration slight inhibition
p-Nitrothiophenol
-
0.5 mM concentration 72% inhibition
TiCl2
-
sub mM concentration slight inhibition
ZnCl2
-
sub mM concentration slight inhibition
ZnSO4
-
sub mM concentration slight inhibition
MnSO4 * 4-6H2O
-
0.38 mM and 0.89 mM concentration 100% inhibition
additional information
-
not inhibitory are: EDTA, sodium azide, monoiodoacetate, p-chloromercuribenzoate, NaHAsO4, sodium fluoride, KCN, hydroxyl ammonium sulfate, hydroxylamine, hydrazine monohydrate, hydrazinium dichloride, and 1,4-benzoquinone
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
alamethicin
-
0.1 mg per mg protein 7.5% activation
phenazine methosulfate
-
under aerobic conditions activity enhancement, under anaerobic conditions electron acceptor
potassium ferricyanide
-
under aerobic conditions activity enhancement, under anaerobic conditions electron acceptor
Triton X-100
-
addition to intact microsomes results in a concentration dependent increase in gulonolactone oxidase activity, 38% activation with 5 mg Triton X-100 per mg protein
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4.28
-
creatol
-
at pH 9.0
12.8
-
creatol
-
at pH 7.4
0.005
-
L-gulono-1,4-lactone
-
at pH 7.4
0.007
-
L-gulono-1,4-lactone
-
-
0.066
-
L-gulono-1,4-lactone
-
-
0.15
-
L-gulono-1,4-lactone
-
-
5.5
-
L-gulono-1,4-lactone
-
the FAD-binding motif Rv1771 protein is a metalloenzyme that oxidizes L-gulono-1,4-lactone
24
-
L-gulono-1,4-lactone
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.016
0.02
-
enzyme expressed in silkworm cells
0.078
-
-
methylguanidine synthesis
1.11
-
-
L-ascorbate synthesis
3.43
-
-
L-ascorbate synthesis
100
-
-
after transfection in guinea pig cells
additional information
-
-
clofibrate-treated mouse enzyme is 8.5fold as active as non-treated mouse enzyme in the microsome and 500fold as active in the peroxisome
additional information
-
-
maximum activity in mesonephros at the 14th day of incubation, in metanephros increasing activity from the 6th to the 18th day of incubation, respectively, decreasing activity in liver and increasing activity in the yolk sac membrane
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6
-
O81030, Q6NQ66, Q9LYD8
assay at; assay at; assay at
7
-
-
assay at
7.5
-
-
L-ascorbate synthesis
7.5
-
-
in phosphate-citrate buffer
8
-
-
in Tris-citrate buffer
9
-
-
synthesis of methylguanidine
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.5
8.3
-
activity stable
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
-
O81030, Q6NQ66, Q9LYD8
assay at; assay at; assay at
37
-
-
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
25
55
-
no detectable optimum
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.41
-
-
calculated from sequence
6.54
-
-
sequence calculation
7.62
-
-
calculated from sequence
8.01
-
-
calculated from sequence
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
embryo, mesonephros and metanephros
Manually annotated by BRENDA team
-
relatively high levels of gulonolactone oxidase in kidney and liver
Manually annotated by BRENDA team
-
primary locus of ascorbate is in liver
Manually annotated by BRENDA team
-
relatively high levels of gulonolactone oxidase in kidney and liver
Manually annotated by BRENDA team
-
primary locus of ascorbate is in liver
Manually annotated by BRENDA team
-
no activity in any other tissue tested
Manually annotated by BRENDA team
-
increase of dietary levels of alpha-tocopherol and/or ascorbic acid lower kidneys enzymic activity
Manually annotated by BRENDA team
-
relatively high levels of gulonolactone oxidase in kidney and liver
Manually annotated by BRENDA team
-
primary locus of ascorbate is in liver
Manually annotated by BRENDA team
-
relatively high levels of gulonolactone oxidase in kidney and liver
Manually annotated by BRENDA team
-
primary locus of ascorbate is in liver
Manually annotated by BRENDA team
Q8K152
high expression of enzyme
Manually annotated by BRENDA team
additional information
-
mRNA expression of GULO gene is evaluated during the early development of Persian sturgeon, quantitative real-time PCR expression analysis, overview. Expression is highest at the embryonic stage, 2 days before hatching, and starts to decline from hatching of larvae to the rest of the developmental time-points
Manually annotated by BRENDA team
additional information
-
no expression in brain, spleen, liver, gut, and muscle
Manually annotated by BRENDA team
additional information
-
GULO expression occurs throughout the early fish development, during hatching in the embryonic stage, but also in late larval stage and before hatching, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
integral membrane protein in the endoplasmic reticulum
-
Manually annotated by BRENDA team
-
integral membrane protein in the endoplasmic reticulum
-
Manually annotated by BRENDA team
Q8K152
recombinant enzyme
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
50000
-
-
SDS-PAGE
50610
-
-
amino acid composition
51000
-
-
expressed in silkworm cells, SDS-PAGE
100000
-
-
gel filtration
110000
-
-
gel filtration
250000
-
-
gel filtration
400000
-
-
gel filtraton
450000
-
-
gel filtration
500000
-
-
gel filtration
500000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 50976, calculation from nucleotide sequence
?
-
x * 50529, calculated from sequence
?
-
x * 51405, calculated from sequence
?
-
x * 51217, calculated from sequence
?
-
x * 50600, about, sequence calculation
oligomer
-
x * 50000, SDS-PAGE
oligomer
-
-
oligomer
-
x * 51000, SDS-PAGE
trimer
-
alpha,beta,gamma, 1 * 61000 + 1 * 32500 + 1 * 16500, the largest is a flavoprotein, gel filtration with 0.1% SDS in buffer and SDS-PAGE
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0
55
-
53% activity at 55 C
49
-
-
10 min 10% activity
100
-
-
after 5 min no activity
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
sodium deoxycholate diminishes the stability of L-gulonolactone oxidase at 37°C
-
highly resistant to proteolytic treatment both in native and in disrupted microsomes
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20 C, 1 month, 100% activity
-
-20 C, 2 days, frozen homogenate, activity declines rapidly
-
-80 C, overnight, frozen liver, 100% activity
-
4°C, 2 weeks, 90% activity loss
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
quantitative real-time PCR expression analysis
-
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
O81030, Q6NQ66, Q9LYD8
expressen in endothelial cell
-
DNA and amino acid sequence determination and analysis, phylogenetic tree
-
expressed in COS1-cells; expressed in silkworm cell line BmN4 with baculovirus vector
-
expressed in Escherichia coli JM109, transfected into guinea pig cell line 104C1
-
biologically functional GLO activity is obtained by direct delivery of an expression vector containing the GLO cDNA into kidney of Silurus asotus, which lacks endogenous GLO
-
overexpression in transgenic tomato fruits using the Agrobacterium tumefaciens strain EHA 105 and CaMV35S constitutive promoter in transfection, semi-quantitative RT-PCR expression analysis. Compared with wild-type, ascorbic acid is 1.5fold higher in red fruits from transgenic plants. Overexpression of GLOase improves tolerance to salt stress of tomato plant
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
mRNA expression of GULO gene is evaluated during the early development of Persian sturgeon
-
L-gulono-1,4-lactone induces the enzyme, overview; L-gulono-1,4-lactone induces the enzyme, overview; L-gulono-1,4-lactone induces the enzyme, overview
O81030, Q6NQ66, Q9LYD8
there is a dramatic decrease in L-gulonolactone oxidase expression in beta-catenin-deficient livers as compared with the wild type livers
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
nutrition
-
increase of dietary levels of alpha-tocopherol and/or ascorbic acid lower kidneys enzymic activity
nutrition
-
up to 4fold increased vitamin C levels in lettuce by overexpression of enzyme
molecular biology
-
short-term vitamin A deficiency in broiler chicks reduces GULO activity without concomittant changes in tissue ascorbic acid
medicine
P58710
a gene therapy approach can be successfully employed in the treatment and further study of vitamin C deficiency in scurvy-prone mammals
nutrition
-
2fold increase in vitamin C content in wild type Arabidopsis thaliana leaf upon expression of enzyme, in vitamin-C-deficient plants, rescued vitamin C content upon enzyme expression is equal or higher than in wild type leaf