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Information on EC 1.1.3.8 - L-gulonolactone oxidase and Organism(s) Scyliorhinus torazame and UniProt Accession Q90YK3

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EC Tree
     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.3 With oxygen as acceptor
                1.1.3.8 L-gulonolactone oxidase
IUBMB 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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This record set is specific for:
Scyliorhinus torazame
UNIPROT: Q90YK3
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Word Map
The taxonomic range for the selected organisms is: Scyliorhinus torazame
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, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
L-gulono-gamma-lactone oxidase
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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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-
-
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LGO
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
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-
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oxidation
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-
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reduction
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-
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PATHWAY SOURCE
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].
CAS REGISTRY NUMBER
COMMENTARY hide
9028-78-8
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
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key enzyme for L-ascorbic acid biosynthesis
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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
-
key enzyme for L-ascorbic acid biosynthesis
-
-
?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
cloudy catshark
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
no activity in any other tissue tested
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
L-gulono-gamma-lactone oxidase is a key enzyme required during the synthesis of L-ascorbic acid
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GGLO_SCYTO
440
1
50958
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50976
-
x * 50976, calculation from nucleotide sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 50976, calculation from nucleotide sequence
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nam, Y.K.; Cho, Y.S.; Douglas, S.E.; Gallant, J.W.; Reith, M.E.; Kim, D.S.
Isolation and transient expression of a cDNA encoding L-gulono-gamma-lactone oxidase, a key enzyme for L-ascorbic acid biosynthesis, from the tiger shark Scyliorhinus torazame.
Aquaculture
209
271-284
2002
Silurus asotus, Scyliorhinus torazame
Manually annotated by BRENDA team
Ocalewicz, K.; Dabrowski, K.; Mambrini, M.
Evidence for the possible existence of a remnant L-gulono-gamma-lactone oxidase (GULO) gene in a teleost genome
Folia Biol. (Krakow)
58
51-54
2010
Acipenser baerii, Cyprinus carpio, Acipenser fulvescens, Amia calva, Scyliorhinus torazame (Q90YK3), Scyliorhinus torazame
Manually annotated by BRENDA team