Information on EC 1.1.3.8 - L-gulonolactone oxidase

for references in articles please use BRENDA:EC1.1.3.8
Word Map on EC 1.1.3.8
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:


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 metabolism
-
-
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
no significant changes in mRNA expression levels and protein abundances of gulo/Gulo in the brain during estivation and arousal, overview
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16500
-
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
32500
-
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
50529
-
x * 50529, calculated from sequence
50600
-
x * 50600, about, sequence calculation
50610
-
amino acid composition
50976
-
x * 50976, calculation from nucleotide sequence
51217
-
x * 51217, calculated from sequence
51405
-
x * 51405, calculated from sequence
61000
-
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
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
additional information
the two main domains in the Gulo protein include the flavin adenine dinucleotide (FAD) binding domain, aa 21-155, and the D-arabinono-1,4-lactone oxidase (ALO) activity domain, aa 180-350
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
gene gulo, cloned from kidney, DNA and amino acid sequence determination and analysis, phylogenetic analysis, quantitative real-time PCR expression analysis
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
drastic decreases in gulo mRNA expression as well as Gulo protein abundance in the kidney after 6 months of estivation
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
-
no significant changes in mRNA expression levels and protein abundances of gulo/Gulo in the brain during estivation and arousal, overview
there is a dramatic decrease in L-gulonolactone oxidase expression in beta-catenin-deficient livers as compared with the wild type livers
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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
Show AA Sequence (165 entries)
Please use the Sequence Search for a specific query.