Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 1.10.3.3 - L-ascorbate oxidase and Organism(s) Cucumis sativus and UniProt Accession P14133

for references in articles please use BRENDA:EC1.10.3.3
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments
A multicopper protein.
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Cucumis sativus
UNIPROT: P14133
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
Word Map
hide
The taxonomic range for the selected organisms is: Cucumis sativus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
hide
4
L-ascorbate
+
O2
=
4
monodehydroascorbate
+
2
H2O
4
+
=
4
+
2
Synonyms
ascorbate oxidase, ascorbic acid oxidase, l-ascorbate oxidase, aa-ox, af_ao1, aa oxidase, ascorbic oxidase, asc oxidase, l-ascorbic acid oxidase, l-ascorbate:oxygen oxidoreductase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ascorbate oxidase
-
AA oxidase
-
-
-
-
AAO
-
-
-
-
AO4
-
isoform
ascorbase
-
-
-
-
ascorbate dehydrogenase
-
-
-
-
ascorbate oxidase
-
-
-
-
ascorbic acid oxidase
ascorbic oxidase
-
-
-
-
L-ascorbate:O2 oxidoreductase
-
-
-
-
L-ascorbic acid oxidase
-
-
-
-
oxidase, ascorbate
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
redox reaction
-
-
-
-
oxidation
-
-
-
-
reduction
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
L-ascorbate:oxygen oxidoreductase
A multicopper protein.
CAS REGISTRY NUMBER
COMMENTARY hide
9029-44-1
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 L-ascorbate + O2
2 L-dehydroascorbate + 2 H2O
show the reaction diagram
-
-
-
?
2 L-ascorbate + O2
2 L-dehydroascorbate + 2 H2O
show the reaction diagram
2 L-ascorbate + O2 + 4 H+
2 monodehydroascorbate + 2 H2O
show the reaction diagram
L-ascorbate + O2
monodehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
the enzyme might perform two types of free radical decay reaction, dismutation and oxidation
-
-
?
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
2 L-ascorbate + O2 + 4 H+
2 monodehydroascorbate + 2 H2O
show the reaction diagram
-
formation of free radicals during the oxidation reaction by ascorbate oxidase
-
-
?
L-ascorbate + O2
monodehydroascorbate + H2O
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
copper
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Urea
-
effect on various molecular forms
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.181 - 1.125
L-ascorbate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06 - 0.21
azide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8
-
assay at
5.5 - 7
-
-
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 8.3
-
at pH 4.5 and 8.3: approx. 50% activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
up to 380fold increase in enzyme activity of transgenic plant
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
ascorbate oxidase and viral movement protein interaction helps in early viral movement of Cucumber mosaic virus
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ASO_CUCSA
587
1
65876
Swiss-Prot
Secretory Pathway (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
132000
-
sedimentation equilibrium
140000
30000
62258
-
x * 62258, deduced from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 62258, deduced from amino acid sequence
dimer
monomer
-
1 * 30000, enzyme also exists as dimer and tetramer, SDS-PAGE
tetramer
-
4 * 30000, enzyme exists as monomer, dimer and tetramer, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
100
-
1 min, all forms of enzyme inactivated
40 - 50
-
conversion of octamer and heavier forms to a dimer
additional information
-
different molecular forms vary in resistance to heat inactivation: tetramer of squash and dimer of cucumber being most resistant
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
native enzyme from cucumber cortex, too homogeneity as blue oxidase
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Populus tremula x Populus alba
cloning of cDNA
-
expressed in Nicotiana benthamiana and Arabidopsis thaliana
-
Nicotiana tabacum L., cv. xanthi over-expressing cucumber ascorbate oxidase. In comparison to wild-type plants, leaves of ascorbate oxidase over-expressing plants exhibit reduced stomatal conductance (due to partial stomatal closure), higher water content, and reduced rates of water loss on detachment. Transgenic plants also exhibit elevated levels of hydrogen peroxide and a decline in hydrogen peroxide-scavenging enzyme activity. Leaf abscisic acid content is also higher in ascorbate oxidase over-expressing plants
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the expression of isoform AO4 is induced during the initial infection period (up to 72 h) in Cucumber mosaic virus-infected Nicotiana benthamiana
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
up to 380fold increase in enzyme activity of leaf of transgenic plants, no change in total ascorbate content of apoplast, but redox state of ascorbate is reduced to below the threshold while that of glutathione is increased. Overexpressing plants show substantial increase in foliar injury and greater decline in CO2 assimilation upon exposure to ozone
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tanaka, N.; Murao, S.
Difference between various copper-containing enzymes (Polyporus laccase, mushroom tyrosinase and cucumber ascorbate oxidase) and bilirubin oxidase
Agric. Biol. Chem.
47
1627-1628
1983
Cucumis sativus
-
Manually annotated by BRENDA team
Lee, M.H.; Dawson, C.R.
Ascorbate oxidase
Methods Enzymol.
62
30-39
1979
Cucumis sativus, Cucurbita pepo condensa, Cucurbita pepo medullosa
Manually annotated by BRENDA team
Nakamura, T.; Makino, N.; Ogura, Y.
Purification and properties of ascorbate oxidase from cucumber
J. Biochem.
64
189-195
1968
Cucumis sativus
Manually annotated by BRENDA team
Messerschmidt, A.; Huber, R.
The blue oxidases, ascorbate oxidase, laccase and ceruloplasmin. Modelling and structural relationships
Eur. J. Biochem.
187
341-352
1990
Cucumis sativus, Cucurbita pepo medullosa
Manually annotated by BRENDA team
Esaka, M.; Hattori, T.; Fujisawa, K.; Sakajo, S.; Asahi, T.
Molecular cloning and nucleotide sequence of full-length cDNA for ascorbate oxidase from cultured pumpkin cells
Eur. J. Biochem.
191
537-541
1990
Cucumis sativus, Cucurbita sp.
Manually annotated by BRENDA team
Cho, H.J.; Aimi, T.; Paik, S.Y.; Murooka, Y.
Secretory production of ascorbate oxidase by cultured cells of cucumber
J. Ferment. Bioeng.
68
193-199
1989
Cucumis sativus
-
Manually annotated by BRENDA team
Sakurai, T.; Sawada, S.; Suzuki, S.; Nakahara, A.
Oxidation of reduced cucumber ascorbate oxidase
Biochem. Biophys. Res. Commun.
131
647-652
1985
Cucumis sativus
Manually annotated by BRENDA team
Aikazyan, V.T.; Nalbandyan, R.M.
Copper-containing proteins from Cucumis sativus
FEBS Lett.
104
127-130
1979
Cucumis sativus
-
Manually annotated by BRENDA team
Amon, A.; Markakis, P.
Properties of ascorbate oxidase isozymes
Phytochemistry
12
2127-2132
1973
Cucumis sativus, Cucurbita pepo condensa, Cucurbita pepo medullosa
-
Manually annotated by BRENDA team
Sanmartin, M.; Drogoudi, P.A.; Lyons, T.; Pateraki, I.; Barnes, J.; Kanellis, A.K.
Over-expression of ascorbate oxidase in the apoplast of transgenic tobacco results in altered ascorbate and glutathione redox states and increased sensitivity to ozone
Planta
216
918-928
2003
Cucumis sativus (P14133), Cucumis sativus
Manually annotated by BRENDA team
Fotopoulos, V.; De Tullio, M.C.; Barnes, J.; Kanellis, A.K.
Altered stomatal dynamics in ascorbate oxidase over-expressing tobacco plants suggest a role for dehydroascorbate signalling
J. Exp. Bot.
59
729-737
2008
Cucumis sativus
Manually annotated by BRENDA team
Barbehenn, R.V.; Jaros, A.; Yip, L.; Tran, L.; Kanellis, A.K.; Constabel, C.P.
Evaluating ascorbate oxidase as a plant defense against leaf-chewing insects using transgenic poplar
J. Chem. Ecol.
34
1331-1340
2008
Cucumis sativus (P14133)
Manually annotated by BRENDA team
Yamazaki, I.; Piette, L.H.
Mechanism of free radical formation and disappearance during the ascorbic acid oxidase and peroxidase reactions
Biochim. Biophys. Acta
50
62-69
1961
Cucumis sativus
Manually annotated by BRENDA team
Kumari, R.; Kumar, S.; Singh, L.; Hallan, V.
Movement protein of cucumber mosaic virus associates with apoplastic ascorbate oxidase
PLoS ONE
11
e0163320
2016
Cucumis sativus
Manually annotated by BRENDA team