Information on EC 1.1.3.8 - L-gulonolactone oxidase

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

EC NUMBER
COMMENTARY hide
1.1.3.8
-
RECOMMENDED NAME
GeneOntology No.
L-gulonolactone oxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-gulono-1,4-lactone + O2 = L-xylo-hex-2-ulono-1,4-lactone + H2O2
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
PATHWAY
BRENDA Link
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].
CAS REGISTRY NUMBER
COMMENTARY hide
9028-78-8
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Siberian sturgeon
-
-
Manually annotated by BRENDA team
lake 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
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
strain DSM 4025
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
brindled bandicoot
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
no activity in Cavia porcellus
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
rabbit
-
-
Manually annotated by BRENDA team
long-nosed bandicoot
-
-
Manually annotated by BRENDA team
similar enzyme: L-galactono-1,4-lactone oxidase
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
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
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
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-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
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-glucono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
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 + O2
L-ascorbate + 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 + phenazine methosulfate + O2
L-ascorbic acid + ?
show the reaction diagram
L-idono-1,4-lactone + O2
?
show the reaction diagram
-
3% as active as L-gulono-1,4-lactone
-
-
?
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
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-ascorbate + H2O2
show the reaction diagram
L-gulono-1,4-lactone + O2
L-xylo-hex-3-ulonolactone + H2O2
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
flavin
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
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
MnSO4 * 4-6H2O
-
0.38 mM and 0.89 mM concentration 100% inhibition
N-ethylmaleimide
-
-
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
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
COMMENTARY hide
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]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.28 - 12.8
creatol
0.005 - 24
L-gulono-1,4-lactone
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6
assay at; assay at; assay at
8
-
in Tris-citrate buffer
9
-
synthesis of methylguanidine
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.3
-
activity stable
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
assay at; assay at; assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 55
-
no detectable optimum
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.41
-
calculated from sequence
6.54
-
sequence calculation
7.62
-
calculated from sequence
8.01
-
calculated from sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
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
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oligomer
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
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 9.2
-
-
636308
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 55
-
53% activity at 55 C
49
-
10 min 10% activity
100
-
after 5 min no activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
highly resistant to proteolytic treatment both in native and in disrupted microsomes
-
sodium deoxycholate diminishes the stability of L-gulonolactone oxidase at 37°C
-
STORAGE STABILITY
ORGANISM
UNIPROT
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
-
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
-
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
-
expressen in endothelial cell
-
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
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
-
quantitative real-time PCR expression analysis
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
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
mRNA expression of GULO gene is evaluated during the early development of Persian sturgeon
-
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
COMMENTARY hide
LITERATURE
medicine
a gene therapy approach can be successfully employed in the treatment and further study of vitamin C deficiency in scurvy-prone mammals
molecular biology
-
short-term vitamin A deficiency in broiler chicks reduces GULO activity without concomittant changes in tissue ascorbic acid
nutrition
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