Information on EC 1.10.3.3 - L-ascorbate oxidase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY hide
1.10.3.3
-
RECOMMENDED NAME
GeneOntology No.
L-ascorbate oxidase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
4 L-ascorbate + O2 = 4 monodehydroascorbate + 2 H2O
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-ascorbate:oxygen oxidoreductase
A multicopper protein.
CAS REGISTRY NUMBER
COMMENTARY hide
9029-44-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Acremonium HI-25
sp. HI-25
-
-
Manually annotated by BRENDA team
mutant, T-DNA inserted into enzyme gene
-
-
Manually annotated by BRENDA team
cabbage
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
wild watermelon No. 1011171, and domesticated watermelon cv. Sanki
-
-
Manually annotated by BRENDA team
satsuma mandarin
-
-
Manually annotated by BRENDA team
Cucumis sp.
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
Cucurbita sp.
cv. Jubilant, two anionic isozymes A1 and A2, two cationic isozymes C2 and C3, one Cd-actiated cationic isozyme C1
-
-
Manually annotated by BRENDA team
bottle gourd
-
-
Manually annotated by BRENDA team
cv. Keitt
-
-
Manually annotated by BRENDA team
strain NFFA2
-
-
Manually annotated by BRENDA team
strain NFFA2
-
-
Manually annotated by BRENDA team
cv. Paloma
-
-
Manually annotated by BRENDA team
white mustard
-
-
Manually annotated by BRENDA team
Solanum lycopersicum West Virginia 106
-
UniProt
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
evolution
malfunction
metabolism
-
stability of total vitamin C in situ was strongly dependent on the plant maturity stage and the processing conditions applied
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 hydroquinone + O2
2 quinone + 2 H2O
show the reaction diagram
Cucurbita pepo condensa
-
at pH 7.2
-
?
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
2,5-dichlorohydroquinone + O2
2,5-dichloroquinone + H2O
show the reaction diagram
2,6-dichlorohydroquinone + O2
2,6-dichloroquinone + H2O
show the reaction diagram
2,6-dichloroindophenol + O2
oxidized 2,6-dichloroindophenol + H2O
show the reaction diagram
4 L-ascorbate + O2
4 monodehydroascorbate + 2 H2O
show the reaction diagram
5,6-ene-L-ascorbate + O2
5,6-ene-L-dehydroascorbate
show the reaction diagram
Cucurbita pepo medullosa
-
-
-
?
5,6-isopropylidene-L-ascorbate + O2
5,6-isopropylidene-L-dehydroascorbate
show the reaction diagram
Cucurbita pepo medullosa
-
-
-
?
5-methyl-5-O-(alpha-D-glucopyranosyl)-D-erythroascorbic acid + O2
? + H2O2
show the reaction diagram
5-methyl-5-O-(alpha-D-xylopyranosyl)-D-erythroascorbic acid + O2
? + H2O2
show the reaction diagram
5-O-(alpha-D-glucopyranosyl)-D-erythroascorbic acid + O2
? + H2O2
show the reaction diagram
5-O-(alpha-D-xylopyranosyl)-D-erythroascorbic acid + O2
? + H2O2
show the reaction diagram
6-amino-L-ascorbate + O2
6-amino-L-dehydroascorbate
show the reaction diagram
Cucurbita pepo medullosa
-
-
-
?
6-bromo-L-ascorbate + O2
6-bromo-L-dehydroascorbate
show the reaction diagram
Cucurbita pepo medullosa
-
-
-
?
6-deoxy-L-ascorbate + O2
6-deoxy-L-dehydroascorbate
show the reaction diagram
Cucurbita pepo medullosa
-
-
-
?
6-O-phenyl-L-ascorbate + O2
6-O-phenyl-L-dehydroascorbate
show the reaction diagram
Cucurbita pepo medullosa
-
-
-
?
6-S-phenyl-L-ascorbate + O2
6-S-phenyl-L-dehydroascorbate
show the reaction diagram
Cucurbita pepo medullosa
-
-
-
?
chlorohydroquinone + O2
chloroquinone + H2O
show the reaction diagram
Cucurbita sp.
-
6% of activity with L-ascorbic acid
-
?
D-erythroascorbic acid + O2
? + H2O2
show the reaction diagram
D-glucoascorbic acid + O2
D-glucodehydroascorbate + H2O
show the reaction diagram
Cucurbita pepo condensa
-
-
-
?
D-isoascorbic acid + O2
2-dehydroisoascorbate + H2O
show the reaction diagram
hydroxyhydroquinone + O2
hydroxyquinone + H2O
show the reaction diagram
Cucurbita pepo condensa
-
oxidation rate approx. 1/12 that of ascorbic acid, pH 5.7
-
?
L-ascorbic acid + O2
L-dehydroascorbic acid + H2O
show the reaction diagram
L-ascorbic acid + O2
L-dehydroascorbic acid + H2O2
show the reaction diagram
-
-
-
-
?
L-ascorbyl-6-palmitate + O2
L-dehydroascorbyl-6-palmitate
show the reaction diagram
-
36% of activity with L-ascorbate
-
?
L-ascorbyl-6-stearate + O2
L-dehydroascorbyl-6-stearate
show the reaction diagram
-
29% of activity with L-ascorbate
-
?
leuco 2,6-dichloroindophenol + O2
oxidized leuco 2,6-dichloroindophenol + H2O
show the reaction diagram
Cucurbita pepo condensa
-
oxidation to the blue quinoid dye at pH 5.7
-
?
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
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
-
formation of free radicals during the oxidation reaction by ascorbate oxidase
-
-
?
4 L-ascorbate + O2
4 monodehydroascorbate + 2 H2O
show the reaction diagram
L-ascorbic acid + O2
L-dehydroascorbic acid + H2O
show the reaction diagram
additional information
?
-
-
cell wall-localized enzyme that catalyses the oxidation of ascorbate to the unstable radical monodehydroascorbate, which rapidly disproportionates to yield dehydroascorbate and ascorbate, and thus contributes to the regulation of the ascorbic acid redox state regulating the cell redox status
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
NaCl
-
induces the ascorbate oxidase activity
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3,4,5-hydroxybenzoic acid propyl ester
Cucurbita pepo condensa
-
-
3,4-Dichlorophenylserine
Cucurbita pepo condensa
-
-
8-hydroxyquinoline
Ag+
Cucurbita pepo medullosa
-
inhibition of intramolecular electron transfer, mechnanism
alpha-tocopherol
Cucurbita pepo condensa
-
-
Anthocyanin pigments
Cucurbita pepo condensa
-
-
-
Auxin analogs
Cucurbita pepo condensa
-
-
-
Carotenes
Cucurbita pepo condensa
-
-
-
Cd2+
-
cadmium-induced inhibition of apoplastic isozyme in barley roots, 50% inhibition of root growth at 1.0 mM 72 h after the treatment, root growth inhibition due to excess Cd is accompanied by a corresponding loss of plasma membrane integrity in root cells, cationic isozyme C1 is activated by Cd2+
citrate
Cucurbita pepo condensa
-
univalent anion, competitive vs. ascorbate
Cu2+
Cucurbita pepo condensa
-
-
Cupferron
Cucurbita pepo condensa
-
-
cyanide
deoxycorticosterone
Cucurbita pepo condensa
-
-
diethyldithiocarbamate
ethyl xanthate
Fe3+
-
1 mM, 91% inhibition
Fenton's reagent
-
Fe2+ + H2O2 + 2 H+
Hg2+
Cucurbita pepo condensa
-
0.01 mM, appreciable inhibition
iodoacetate
Cucurbita pepo condensa
-
-
Lauryl sulfate
-
-
leucocyanidol
Cucurbita pepo condensa
-
-
Metabisulfite
-
complete inhibition
Ni2+
Cucurbita pepo condensa
-
some authors found inhibition, others not
Nitrofurantoin
-
slight
nordihydroguaiaretic acid
Cucurbita pepo condensa
-
-
o-fluorophenol
-
-
Organic mercurials
Cucurbita pepo condensa
-
-
-
p-chlorophenol
Cucurbita pepo medullosa
-
-
p-Cresol
Cucurbita pepo medullosa
-
-
p-cyanophenol
Cucurbita pepo medullosa
-
-
p-fluorophenol
-
-
p-mercuribenzoate
Cucurbita pepo condensa
-
some authors report inhibition, others do not
p-nitrophenol
Cucurbita pepo medullosa
-
-
Phenol
Cucurbita pepo medullosa
-
-
Piperazine N,N'-bis(2-ethanesulfonic acid)
Cucurbita pepo condensa
-
anions
Pyridine-KNCS
Cucurbita pepo condensa
-
-
-
Salicylaldoxime
Cucurbita pepo condensa
-
-
SO2
Cucurbita pepo condensa
-
-
Tetraethylthiuramidisulfide
Cucurbita pepo condensa
-
-
thiamine
Cucurbita pepo condensa
-
-
Thiocyanate
Cucurbita pepo medullosa
-
weak inhibition, mixed-type inhibition
Thiourea
Zn2+
Cucurbita pepo condensa
-
some authors found inhibition, others not
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2,2'-bipyridyl
-
stimulation
ascorbate
Cucurbita pepo condensa
-
treatment with excess ascorbate at pH 4.85 to pH 5.5 in the presence of citrate and chloride and in the absence of O2, 9fold increase in maximal velocity
Cd2+
-
cadmium-induced inhibition of apoplastic isozyme in barley roots, cationic isozyme C1 is activated by Cd2+
CuCl2
-
1 mM, 2fold activation
ethanol
-
stimulation
far red light
-
7fold increase in activity after exposure to far red light for 36 h, suggesting post-translational control of activity by phytochrome
-
H2O2
-
stimulation at low concentration, 0.056 mM
iodoacetate
-
stimulation
o-phenanthroline
-
stimulation
p-chloromercuribenzoate
-
stimulation
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
1.12
5,6-ene-L-ascorbate
Cucurbita pepo medullosa
-
commercial enzyme preparation from Sigma
0.554
5,6-isopropylidene-L-ascorbate
Cucurbita pepo medullosa
-
commercial enzyme preparation from Sigma
0.433
5-methyl-5-O-(alpha-D-glucopyranosyl)-D-erythroascorbic acid
-
-
0.162
5-methyl-5-O-(alpha-D-xylopyranosyl)-D-erythroascorbic acid
-
-
0.402
5-O-(alpha-D-glucopyranosyl)-D-erythroascorbic acid
-
-
0.642
5-O-(alpha-D-xylopyranosyl)-D-erythroascorbic acid
-
-
0.887
6-amino-L-ascorbate
Cucurbita pepo medullosa
-
commercial enzyme preparation from Sigma
0.124
6-bromo-L-ascorbate
Cucurbita pepo medullosa
-
commercial enzyme preparation from Sigma
0.187
6-deoxy-L-ascorbate
Cucurbita pepo medullosa
-
commercial enzyme preparation from Sigma
0.026
6-O-phenyl-L-ascorbate
Cucurbita pepo medullosa
-
commercial enzyme preparation from Sigma
0.032
6-S-phenyl-L-ascorbate
Cucurbita pepo medullosa
-
commercial enzyme preparation from Sigma
0.37
chlorohydroquinone
Cucurbita sp.
-
-
0.304
D-erythroascorbic acid
-
-
0.53
D-iso-ascorbate
-
-
1.307
D-isoascorbate
Cucurbita pepo medullosa
-
commercial enzyme preparation from Sigma
0.039 - 10
L-ascorbate
0.126 - 1.5
L-ascorbic acid
0.47
O2
-
-
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
639
5,6-ene-L-ascorbate
Cucurbita pepo medullosa
-
commercial enzyme preparation from Sigma
623
5,6-isopropylidene-L-ascorbate
Cucurbita pepo medullosa
-
commercial enzyme preparation from Sigma
0.55
5-methyl-5-O-(alpha-D-glucopyranosyl)-D-erythroascorbic acid
Pleurotus ostreatus
-
-
0.24
5-methyl-5-O-(alpha-D-xylopyranosyl)-D-erythroascorbic acid
Pleurotus ostreatus
-
-
0.6
5-O-(alpha-D-glucopyranosyl)-D-erythroascorbic acid
Pleurotus ostreatus
-
-
1.29
5-O-(alpha-D-xylopyranosyl)-D-erythroascorbic acid
Pleurotus ostreatus
-
-
546
6-amino-L-ascorbate
Cucurbita pepo medullosa
-
commercial enzyme preparation from Sigma
702
6-bromo-L-ascorbate
Cucurbita pepo medullosa
-
commercial enzyme preparation from Sigma
969
6-deoxy-L-ascorbate
Cucurbita pepo medullosa
-
commercial enzyme preparation from Sigma
473
6-O-phenyl-L-ascorbate
Cucurbita pepo medullosa
-
commercial enzyme preparation from Sigma
526
6-S-phenyl-L-ascorbate
Cucurbita pepo medullosa
-
commercial enzyme preparation from Sigma
1.12
D-erythroascorbic acid
Pleurotus ostreatus
-
-
804
D-isoascorbate
Cucurbita pepo medullosa
-
commercial enzyme preparation from Sigma
7.6 - 10800
L-ascorbate
0.66
L-ascorbic acid
Pleurotus ostreatus
-
-
1130
O2
Acremonium
-
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.06 - 0.21
azide
1
p-chlorophenol
Cucurbita pepo medullosa
-
at pH 7.0
18
p-Cresol
Cucurbita pepo medullosa
-
at pH 7.0
2
p-cyanophenol
Cucurbita pepo medullosa
-
at pH 7.0
2.5 - 4.6
p-nitrophenol
6
Phenol
Cucurbita pepo medullosa
-
at pH 7.0
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
133.5 - 310
Cucurbita sp.
-
different purified commercial preparations
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.8
-
assay at
5.3
-
assay at
5.5 - 7
5.5
-
optimal pH of free ascorbate oxidase
5.8 - 7
-
assay at
6.2
-
basic enzyme
6.5
Cucurbita sp.
-
-
7.5
-
optimum for the electrochemical catalytic reaction
7.8
-
spectrophotometric assay at
7.9
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.5 - 8.3
-
at pH 4.5 and 8.3: approx. 50% activity
5 - 9
-
free enzyme: approx. 60% activity at pH 5.0, less than 10% activity at pH 9.0, immobilized enzyme: approx. 80% activity at pH 5.0, approx. 45% activity at pH 9.0
additional information
-
pH profile, overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
28
-
assay at
30
-
assay at
40
-
optimal pH of freee and biosensor/immobilized ascorbate oxidase
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
10 - 70
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
Cucurbita pepo medullosa
-
-
Manually annotated by BRENDA team
Cucurbita sp.
-
different batches of commercially available crude enzyme from different suppliers, batch compositions, overview
Manually annotated by BRENDA team
-
broccoli florets show higher AAO activity compared to stalks
Manually annotated by BRENDA team
-
homogenates of the mouth area
Manually annotated by BRENDA team
arbuscular, enzyme localization in the highly specialized structures at the host-symbiont interface
Manually annotated by BRENDA team
high expression level of isozyme AO4
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
Cucurbita pepo medullosa
-
-
Manually annotated by BRENDA team
additional information
-
no activity in chloroplast
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
132000
139000
-
basic enzyme, gel filtration
140000
141000
-
gel filtration
150000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dodecamer
Cucurbita pepo condensa
-
12 * 35000, enzyme exists as monomer, tetramer, octamer, dodecamer and polymer, SDS-PAGE
homodimer
-
ascorbate oxidase is a large, multidomain, dimeric protein
monomer
octamer
Cucurbita pepo condensa
-
8 * 35000, enzyme exists as monomer, tetramer, octamer, dodecamer and polymer, SDS-PAGE
polymer
Cucurbita pepo condensa
-
x * 35000, between 670000 Da and 2000000 Da, enzyme exists as monomer, tetramer, octamer, dodecamer and polymer, SDS-PAGE
tetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
fully oxidized form of ascorbate oxidase, X-ray diffraction structure determination and analysis at 1.90 A resolution
15 mg/ml enzyme solution, dialysis with 10% 2-methyl-2,4-pentanediol in 50 mM phosphate buffer, pH 5.4 at 4C, crystals suitable for X-ray studies, 2.5 A resolution
Cucurbita pepo medullosa
-
vapour diffusion method, 1.9 M sodium-potassium phosphate buffer pH 7.0 as reservoir solution at 4C, final protein concentration 5-6 mg/ml
Cucurbita pepo medullosa
-
X-ray crystal structure at 2.5 A resolution
Cucurbita pepo medullosa
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.6
Cucurbita pepo medullosa
-
loss of 80% activity after 30 min at 0C
439924
4
Cucurbita pepo condensa
-
irreversible loss of activity below
439889
5 - 8
-
-
439930
5 - 10
Cucurbita sp.
-
rapid loss of activity below pH 4 and above pH 12
439928
5 - 9
-
-
439938
6 - 10
-
at 30C
439932
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 40
-
30 min, stable
10
-
half-life: 1047 min
12
Cucurbita pepo medullosa
-
stable for at least 30 days
15
-
immobilized enzyme retains full activity for 3 months at pH 5.0-7.0, free enzyme looses 40-70% activity within one day at pH 5.0-7.0
40 - 50
40
-
stable for 30 min
50 - 80
-
during thermal treatments for 10 min, AAO in broccoli florets and stalks is stable until around 50C. A 10 min thermal treatment at 80C almost completely inactivates AAO. AAO inactivation is irreversible since no increase in activity is observed when extracts of thermal treated broccoli are stored at 4C for 24 h
50
-
stable for 5 min
55
Cucurbita sp.
-
no loss in activity after 30 min, approx. 55% activity after 30 min at 60C, approx. 30% activity after 30 min at 65C
70
-
half-life: 21.2 min
90
-
thermal inactivation of AAO follows first-order reaction kinetics. Heating at temperatures above 90C for short times results in a complete AAO inactivation, resulting in a protective effect of L-ascorbic acid toward enzyme-catalyzed oxidation
additional information
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
20-25% retention of activity after immobilization, at 12C, stable for at least 30 days
Cucurbita pepo medullosa
-
a long acting enzyme derivative is synthesized by covalently linking poly(ethylene glycol) to the enzyme
Cucurbita sp.
-
ascorbate oxidase is alternately deposited with Au nanoparticles and forms a layer-by-layer membrane on a Pt electrode. The enzyme activities remain even after the deposition. The oxidation current of ascorbic acid (0.1 mM) decreases to 36% for the (ascorbate oxidase/Au)1 modified electrode, and to 19% for the (ascorbate oxidase/Au)10 modified electrode
Cucumis sp.
-
gelatin, catalase, peroxidase and methemoglobin protect against inactivation
Cucurbita pepo condensa
-
immobilization within 6% Ca-alginate gel beads improves stability
-
no change in total activity in the presence of 5 M urea, conversion of tetrameric form into monomer with 75% activity in 8 M urea
Cucurbita pepo medullosa
-
partially unfolding of the enzyme by 1.4 M guanidinium hydrochloride or 2.8 M urea
role of copper in stability
Cucurbita pepo medullosa
-
stable to dialysis against EDTA or cyanide
-
OXIDATION STABILITY
ORGANISM
UNIPROT
LITERATURE
comparison of tolerance of wild-type and transgenic tobacco plants to oxidative stress, overview
-
675145
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, purified commercial enzymes, 10 mM HEPES-NaOH, pH 8.0, and 60% sucrose, comparison of the stability of the different enzyme batches, overview
Cucurbita sp.
-
12C, at least 30 d, no loss of activity
Cucurbita pepo medullosa
-
4C, 10 months, no loss in activity
Cucurbita pepo medullosa
-
4C, 2 months, 20% loss of activity
Cucurbita pepo medullosa
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4C, ascorbate oxidase immobilized onto egg shell membrane through glutaraldehyde coupling in 0.1 M sodium phosphate EDTA buffer pH 5.6, 120 days, 50% loss of activity
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4C, concentrated solution, 3 months, 20% loss of activity
Cucurbita pepo medullosa
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate fractionation
ammonium sulfate precipitation, DEAE-Sephacel column chromatography, and Sephadex G-100 gel filtration
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ammonium sulfate, DEAE-dextran-silochrome
Cucurbita sp.
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ammonium sulfate, DEAE-Toyopearl, CM-Sephadex, Sephadex G-100
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ammonium sulfate, phenyl Sepharose, Sephacryl S-300, Q-Sepharose, preparative isoelectric focusing, basic and acidic enzyme purified from flour, ammonium sulfate, phenyl Sepharose, Q-Sepharose, Mono S, Superdex 200, basic and acidic enzyme purified from immature kernels
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further purification of different commercial preparations, overview
Cucurbita sp.
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liquid-liquid extraction in aqueous two-phase systems in continuous process using perforated rotating disc contactor with 10% (w/v) PEG 20000 and 25% (w/v) citrate; pre-purification using a aqueous two-phase system (PEG/citrate)
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native enzyme from cucumber cortex, too homogeneity as blue oxidase
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recombinant wild-type enzyme and various mutants
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloning of cDNA
co-expression of cytochrome b561 and ascorbate oxidase
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expressed in Populus tremula x Populus alba
expression of cDNA in Nicotiana tabacum cell culture
Cucurbita sp.
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expression of RNAi constructs in tomato plants using transfection of WVa106 tomato cotyledons via Agrobacterium strain GV3101, real-time quantitative PCR expression analysis
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expression of wild-type, Q183R, T527A, E177K, V185K, V188R, P190I, V193P, R194Q, Q382G, H383Y, V385K, R387A, A389N, L539E, H540L, M542L, V543H, W189H, W386H, V193G, V193F, V193H, V193K, V193E, V185K/V188R, V188R/P190I and P190I/V193P mutant enzyme in Aspergillus nidulans
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gene-specific expression studies of the AO gene family in melon reveal that only CmAO1 and CmAO4 are transcriptionally active and differentially regulated dependent on tissue, developmental stage and external stimuli, overview; gene-specific expression studies of the AO gene family in melon reveal that only CmAO1 and CmAO4 are transcriptionally active and differentially regulated dependent on tissue, developmental stage and external stimuli, overview
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
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overexpression of the enzyme in transgenic tobacco lines
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phylogenetic analysis
quantitative expression analysis
symbiosis-induced AO gene overexpressed in Lotus japonicus during its interaction with either N2-fixing Mesorhizobium loti or the AM fungus Gigaspora margarita, overview
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
enzyme expression of Lotus japonicus is induced in the symbiotic interaction with both nitrogen-fixing bacteria and arbuscular mycorrhizal fungi, symbiosis-induced ascorbate oxidase gene overexpressed in Lotus japonicus during its interaction with either N2-fixing Mesorhizobium loti or the AM fungus Gigaspora margarita, overview
NaCl-induced ascorbate oxidase activity
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A389N
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slightly reduced thermostability
E177K
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slightly reduced thermostability
E540L
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slightly reduced thermostability
H383Y
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slightly reduced thermostability
L539E
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slightly increased thermostability
M542L
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strongly reduced thermostability
P190I
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reduced thermostability
P190I/V193P
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pH optimum shifted to pH 4.5, slightly reduced thermostability
Q183R
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similar properties as wild-type
Q382G
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slightly higher thermostability
R194Q
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similar properties as wild-type
R387A
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slightly reduced thermostability
T527A
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similar properties as wild-type
V185K
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slightly reduced thermostability
V185K/V188R
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similar properties as wild-type
V188R/P190I
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no detectable activity
V193E
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pH optimum shifted to pH 4.5, very thermolabile
V193F
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slightly reduced thermostability
V193G
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very thermolabile
V193H
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slightly reduced thermostability
V193K
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slightly reduced thermostability
V193P
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pH optimum shifted to pH 5.0
V193T
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similar properties as wild-type
V385K
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reduced thermostability
V543H
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very thermolabile
W189H
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no detectable activity
W386H
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reduced thermostability
additional information
Renatured/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
reconstitution of copper-free apoascorbate oxidase with cuprous copper solution
Cucurbita pepo medullosa
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refolding after denaturation in urea or guanidinium hydrochloride, enzymatic activity is achieved after a further incubation in anaerobiosis of the refolded enzyme in the presence of cupric ions
Cucurbita pepo medullosa
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
analysis
medicine
Cucurbita sp.
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reagent for clinical analysis of L-ascorbic acid
Show AA Sequence (155 entries)
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