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2 hydroquinone + O2
2 quinone + 2 H2O
-
at pH 7.2
-
?
2 L-ascorbate + O2
2 L-dehydroascorbate + 2 H2O
2 L-ascorbate + O2 + 4 H+
2 monodehydroascorbate + 2 H2O
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
2,5-dichlorohydroquinone + O2
2,5-dichloroquinone + H2O
2,6-dichlorohydroquinone + O2
2,6-dichloroquinone + H2O
2,6-dichloroindophenol + O2
oxidized 2,6-dichloroindophenol + H2O
4 L-ascorbate + O2
4 monodehydroascorbate + 2 H2O
5,6-ene-L-ascorbate + O2
5,6-ene-L-dehydroascorbate
-
-
-
?
5,6-isopropylidene-L-ascorbate + O2
5,6-isopropylidene-L-dehydroascorbate
-
-
-
?
5-methyl-5-O-(alpha-D-glucopyranosyl)-D-erythroascorbic acid + O2
? + H2O2
5-methyl-5-O-(alpha-D-xylopyranosyl)-D-erythroascorbic acid + O2
? + H2O2
5-O-(alpha-D-glucopyranosyl)-D-erythroascorbic acid + O2
? + H2O2
5-O-(alpha-D-xylopyranosyl)-D-erythroascorbic acid + O2
? + H2O2
6-amino-L-ascorbate + O2
6-amino-L-dehydroascorbate
-
-
-
?
6-bromo-L-ascorbate + O2
6-bromo-L-dehydroascorbate
-
-
-
?
6-deoxy-L-ascorbate + O2
6-deoxy-L-dehydroascorbate
-
-
-
?
6-O-phenyl-L-ascorbate + O2
6-O-phenyl-L-dehydroascorbate
-
-
-
?
6-S-phenyl-L-ascorbate + O2
6-S-phenyl-L-dehydroascorbate
-
-
-
?
chlorohydroquinone + O2
chloroquinone + H2O
Cucurbita sp.
-
6% of activity with L-ascorbic acid
-
?
D-erythroascorbic acid + O2
? + H2O2
-
-
-
-
?
D-glucoascorbic acid + O2
D-glucodehydroascorbate + H2O
-
-
-
?
D-isoascorbate + O2
2-dehydroisoascorbate + H2O
D-isoascorbate + O2
?
-
-
-
-
?
D-isoascorbic acid + O2
2-dehydroisoascorbate + H2O
hydroxyhydroquinone + O2
hydroxyquinone + H2O
-
oxidation rate approx. 1/12 that of ascorbic acid, pH 5.7
-
?
L-ascorbate + O2
monodehydroascorbate + H2O
L-ascorbyl-6-palmitate + O2
L-dehydroascorbyl-6-palmitate
-
36% of activity with L-ascorbate
-
?
L-ascorbyl-6-stearate + O2
L-dehydroascorbyl-6-stearate
-
29% of activity with L-ascorbate
-
?
leuco 2,6-dichloroindophenol + O2
oxidized leuco 2,6-dichloroindophenol + H2O
-
oxidation to the blue quinoid dye at pH 5.7
-
?
additional information
?
-
2 L-ascorbate + O2
2 L-dehydroascorbate + 2 H2O
-
highly specific for ascorbic acid and a few of its analogs and O2
-
?
2 L-ascorbate + O2
2 L-dehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + O2
2 L-dehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + O2
2 L-dehydroascorbate + 2 H2O
-
-
-
-
?
2 L-ascorbate + O2
2 L-dehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + O2
2 L-dehydroascorbate + 2 H2O
-
low reaction rate with bilirubin
-
?
2 L-ascorbate + O2
2 L-dehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + O2
2 L-dehydroascorbate + 2 H2O
-
-
-
-
?
2 L-ascorbate + O2
2 L-dehydroascorbate + 2 H2O
-
double displacement mechanism, so called enzymatic memory
-
?
2 L-ascorbate + O2
2 L-dehydroascorbate + 2 H2O
-
substrate specificity: overview
-
?
2 L-ascorbate + O2
2 L-dehydroascorbate + 2 H2O
-
no appreciable activity with: p-phenylenediamine, Na2S2O3, glutathione and cysteine
-
?
2 L-ascorbate + O2
2 L-dehydroascorbate + 2 H2O
-
anionic form of the substrate is an important requirement of the enzyme specificity
-
?
2 L-ascorbate + O2
2 L-dehydroascorbate + 2 H2O
-
no oxidation of hydroquinone
-
?
2 L-ascorbate + O2
2 L-dehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + O2
2 L-dehydroascorbate + 2 H2O
-
-
-
-
?
2 L-ascorbate + O2
2 L-dehydroascorbate + 2 H2O
Cucurbita sp.
-
-
-
?
2 L-ascorbate + O2
2 L-dehydroascorbate + 2 H2O
Cucurbita sp.
-
enzyme may play a key role in the regulation of cell expansion
-
?
2 L-ascorbate + O2
2 L-dehydroascorbate + 2 H2O
Cucurbita sp.
-
possibly a kind of pathogenesis-related protein
-
?
2 L-ascorbate + O2
2 L-dehydroascorbate + 2 H2O
-
-
-
-
?
2 L-ascorbate + O2
2 L-dehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + O2 + 4 H+
2 monodehydroascorbate + 2 H2O
-
formation of free radicals during the oxidation reaction by ascorbate oxidase
-
-
?
2 L-ascorbate + O2 + 4 H+
2 monodehydroascorbate + 2 H2O
-
formation of free radicals during the oxidation reaction by ascorbate oxidase, determination of steady-state free radical concentration, overview
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
-
-
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
-
-
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
-
-
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
-
-
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
-
-
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
-
role of AO is regulation of cell division through controlled apoplastic Asc levels
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
-
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
the gene expression is transcriptionally regulated during fruit development and in response to hormonal cues associated with the control of cell growth and the stress response
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
-
-
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
-
metabolic regulation, overview
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
-
-
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
-
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
-
the enzyme activity is up- or down-regulated in response to oxygen availability
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
-
-
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
-
aerobic oxidation of ascorbate to the unstable ascorbate free radical
the radical plays a role as an electron acceptor in plant growth including plasma membrane electron transport, cell elongation and cell wall metabolism, overview
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
-
-
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
-
the enzyme activity is up- or down-regulated in response to oxygen availability
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
-
-
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
-
-
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
-
-
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
-
-
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
-
the enzyme activity is up- or down-regulated in response to oxygen availability
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) + O2
?
-
-
-
-
?
2,5-dichlorohydroquinone + O2
2,5-dichloroquinone + H2O
-
-
-
-
?
2,5-dichlorohydroquinone + O2
2,5-dichloroquinone + H2O
-
oxidation rate approx. 1/12 that of ascorbic acid, pH 5.7
-
?
2,6-dichlorohydroquinone + O2
2,6-dichloroquinone + H2O
-
-
-
?
2,6-dichlorohydroquinone + O2
2,6-dichloroquinone + H2O
-
oxidation rate approx. 1/12 that of ascorbic acid, pH 5.7
-
?
2,6-dichloroindophenol + O2
oxidized 2,6-dichloroindophenol + H2O
-
2,6-dichloroindophenol is an effective electron-transfer mediator for the enzyme, while ferrocyanide and cytochrome c are poor mediators
-
-
?
2,6-dichloroindophenol + O2
oxidized 2,6-dichloroindophenol + H2O
-
2,6-dichloroindophenol is an effective electron-transfer mediator for the enzyme, while ferrocyanide and cytochrome c are poor mediators
-
-
?
2,6-dichloroindophenol + O2
oxidized 2,6-dichloroindophenol + H2O
-
-
-
?
4 L-ascorbate + O2
4 monodehydroascorbate + 2 H2O
-
-
-
-
?
4 L-ascorbate + O2
4 monodehydroascorbate + 2 H2O
-
-
-
-
?
4 L-ascorbate + O2
4 monodehydroascorbate + 2 H2O
-
-
-
?
4 L-ascorbate + O2
4 monodehydroascorbate + 2 H2O
-
-
-
-
?
4 L-ascorbate + O2
4 monodehydroascorbate + 2 H2O
-
-
-
-
?
4 L-ascorbate + O2
4 monodehydroascorbate + 2 H2O
-
-
-
-
?
4 L-ascorbate + O2
4 monodehydroascorbate + 2 H2O
Cucurbita sp.
-
the enzyme is involved in catalyzing the oxidation of apoplastic ascorbic acid to dehydroascorbic acid
-
-
?
4 L-ascorbate + O2
4 monodehydroascorbate + 2 H2O
-
-
-
?
4 L-ascorbate + O2
4 monodehydroascorbate + 2 H2O
-
-
-
?
4 L-ascorbate + O2
4 monodehydroascorbate + 2 H2O
-
-
-
?
4 L-ascorbate + O2
4 monodehydroascorbate + 2 H2O
-
-
-
-
?
5-methyl-5-O-(alpha-D-glucopyranosyl)-D-erythroascorbic acid + O2
? + H2O2
-
-
-
-
?
5-methyl-5-O-(alpha-D-glucopyranosyl)-D-erythroascorbic acid + O2
? + H2O2
-
-
-
-
?
5-methyl-5-O-(alpha-D-xylopyranosyl)-D-erythroascorbic acid + O2
? + H2O2
-
-
-
-
?
5-methyl-5-O-(alpha-D-xylopyranosyl)-D-erythroascorbic acid + O2
? + H2O2
-
-
-
-
?
5-O-(alpha-D-glucopyranosyl)-D-erythroascorbic acid + O2
? + H2O2
-
-
-
-
?
5-O-(alpha-D-glucopyranosyl)-D-erythroascorbic acid + O2
? + H2O2
-
-
-
-
?
5-O-(alpha-D-xylopyranosyl)-D-erythroascorbic acid + O2
? + H2O2
-
-
-
-
?
5-O-(alpha-D-xylopyranosyl)-D-erythroascorbic acid + O2
? + H2O2
-
-
-
-
?
D-isoascorbate + O2
2-dehydroisoascorbate + H2O
-
-
-
-
r
D-isoascorbate + O2
2-dehydroisoascorbate + H2O
-
-
-
-
r
D-isoascorbic acid + O2
2-dehydroisoascorbate + H2O
-
-
-
?
D-isoascorbic acid + O2
2-dehydroisoascorbate + H2O
-
-
-
?
D-isoascorbic acid + O2
2-dehydroisoascorbate + H2O
-
-
-
?
D-isoascorbic acid + O2
2-dehydroisoascorbate + H2O
-
-
-
?
L-ascorbate + O2
monodehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + O2
monodehydroascorbate + H2O
-
-
-
-
r
L-ascorbate + O2
monodehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + O2
monodehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + O2
monodehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + O2
monodehydroascorbate + H2O
-
-
-
?
L-ascorbate + O2
monodehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + O2
monodehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + O2
monodehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + O2
monodehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + O2
monodehydroascorbate + H2O
-
-
-
-
?
additional information
?
-
-
the active site binding pocket of ascorbate oxidase is specific for ascorbate10 and the electron transfer of ascorbate oxidase is strongly dependent on the nature of the electron donor, overview
-
-
?
additional information
?
-
-
the oxidative activity of ascorbate oxidase is dominated by the highly selective substrate-binding affinity based on electrostatic interaction beyond the one-electron redox potential difference between type 1 copper site of ascorbate oxidase and substrate
-
-
?
additional information
?
-
-
the active site binding pocket of ascorbate oxidase is specific for ascorbate10 and the electron transfer of ascorbate oxidase is strongly dependent on the nature of the electron donor, overview
-
-
?
additional information
?
-
-
the oxidative activity of ascorbate oxidase is dominated by the highly selective substrate-binding affinity based on electrostatic interaction beyond the one-electron redox potential difference between type 1 copper site of ascorbate oxidase and substrate
-
-
?
additional information
?
-
-
ascorbic acid interferes with the realtime measurement of neuronal NO, an important gaseous neurotransmitter, by use of diaminofluoresceins, which act as receptors for NO, ascorbic acid reduces N2O3, the reaction intermediate of NO oxidation, while dehydroascorbic acid competes with NO for the receptors, while ascorbic acid inhibits the binding between NO and diaminofluoresceins, overview
-
-
?
additional information
?
-
-
syringaldezine and guaiacol are not oxidized
-
-
-
additional information
?
-
-
syringaldezine and guaiacol are not oxidized
-
-
-
additional information
?
-
-
the enzyme might perform two types of free radical decay reaction, dismutation and oxidation
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2 L-ascorbate + O2
2 L-dehydroascorbate + 2 H2O
2 L-ascorbate + O2 + 4 H+
2 monodehydroascorbate + 2 H2O
-
formation of free radicals during the oxidation reaction by ascorbate oxidase
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
4 L-ascorbate + O2
4 monodehydroascorbate + 2 H2O
L-ascorbate + O2
monodehydroascorbate + H2O
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
-
-
?
2 L-ascorbate + O2
2 L-dehydroascorbate + 2 H2O
Cucurbita sp.
-
enzyme may play a key role in the regulation of cell expansion
-
?
2 L-ascorbate + O2
2 L-dehydroascorbate + 2 H2O
Cucurbita sp.
-
possibly a kind of pathogenesis-related protein
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
-
-
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
-
-
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
-
-
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
-
role of AO is regulation of cell division through controlled apoplastic Asc levels
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
the gene expression is transcriptionally regulated during fruit development and in response to hormonal cues associated with the control of cell growth and the stress response
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
-
-
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
-
metabolic regulation, overview
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
-
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
-
the enzyme activity is up- or down-regulated in response to oxygen availability
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
-
-
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
-
the enzyme activity is up- or down-regulated in response to oxygen availability
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
-
-
-
-
?
2 L-ascorbic acid + O2
2 L-dehydroascorbic acid + 2 H2O
-
the enzyme activity is up- or down-regulated in response to oxygen availability
-
-
?
4 L-ascorbate + O2
4 monodehydroascorbate + 2 H2O
-
-
-
-
?
4 L-ascorbate + O2
4 monodehydroascorbate + 2 H2O
-
-
-
-
?
4 L-ascorbate + O2
4 monodehydroascorbate + 2 H2O
Cucurbita sp.
-
the enzyme is involved in catalyzing the oxidation of apoplastic ascorbic acid to dehydroascorbic acid
-
-
?
4 L-ascorbate + O2
4 monodehydroascorbate + 2 H2O
-
-
-
?
4 L-ascorbate + O2
4 monodehydroascorbate + 2 H2O
-
-
-
?
4 L-ascorbate + O2
4 monodehydroascorbate + 2 H2O
-
-
-
?
4 L-ascorbate + O2
4 monodehydroascorbate + 2 H2O
-
-
-
-
?
L-ascorbate + O2
monodehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + O2
monodehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + O2
monodehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + O2
monodehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + O2
monodehydroascorbate + H2O
-
-
-
?
L-ascorbate + O2
monodehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + O2
monodehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + O2
monodehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + O2
monodehydroascorbate + H2O
-
-
-
-
?
L-ascorbate + O2
monodehydroascorbate + H2O
-
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NaCl
-
induces the ascorbate oxidase activity
copper
-
-
copper
-
enzyme contains type I, type II and type III copper atoms in the ratio 1/2/2, 4 copper atoms/enzyme
copper
-
the oxidative activity of ascorbate oxidase is dominated by the highly selective substrate-binding affinity based on electrostatic interaction beyond the one-electron redox potential difference between type 1 copper site of ascorbate oxidase and substrate
copper
-
multi-copper oxidase
copper
-
10 copper atoms per enzyme molecule
copper
-
4 copper atoms per subunit, mononuclear blue copper in domain 3 and trinuclear copper between domain 1 and 3
copper
-
principal active site comprised of one type I, one type II and a pair of type III coppers
copper
-
enzyme contains a set of 1 type I, 1 type II and a pair of type III copper ions at its active site
copper
-
8 atoms of copper per enzyme molecule of 132000 Da
copper
-
8 atoms of copper per enzyme molecule of 140000 Da
copper
-
a multicopper protein, 6 atoms of copper per enzyme molecule
copper
-
each subunit has 4 copper atoms bound as mononuclear and trinuclear species, mononuclear copper representing the type I copper is located in the 3 domain
copper
-
evidence that the coordination environment and electronic structure of the type 1 copper is similar to those of plastocyanin and azurin
copper
-
native enzyme contains two type 1, two type 2 and four type 3 copper ions
copper
-
type 2 copper may be part of the ascorbate binding site
copper
-
measurement of intramolecular electron transfer between type I and type III copper centers in the multi-copper enzyme
copper
-
electronic structure of blue copper sites
copper
-
4 copper atoms per subunit, mononuclear blue copper in domain 3 and trinuclear copper between domain 1 and 3
copper
-
coordination environment of type 2 copper
copper
-
8 atoms of copper per enzyme molecule of 140000 Da
copper
-
10-12 atoms of copper per enzyme molecule of 140000 Da
copper
-
type I and trinuclear type II copper center
Cu2+
-
a multicopper oxidase, contains type 1 Cu2+, binding residues are His445, Cys507, His512, and Met517
Cu2+
-
a multicopper oxidase
Cu2+
copper-containing enzyme
Cu2+
-
a plant blue-copper protein
Cu2+
essential for activity, a tri-nuclear copper center structure, a partial loss of tertiary structure has strong effects on copper
Cu2+
9 copper atoms per enzyme molecule. Each subunit has four copper atoms bound as mononuclear and trinuclear species. The mononuclear copper has two histidine, a cysteine and a methionine ligand and represents the type-l copper. It is located in domain 3. Binding structure analysis, copper site structures, detailed overview
Cu2+
-
a blue copper-containing oxidase
Cu2+
-
a plant blue-copper protein
Cu2+
-
a plant blue-copper protein
additional information
-
no support of a metal in the enzyme
additional information
-
selective removal of copper with chelating agents, e.g. EDTA or N,N-diethyldithiocarbamate produces an inactive enzyme, CN- treatment gives fully copper-depleted apoform, indication that copper affects the enzyme stability but not the enzyme conformation
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3,4,5-hydroxybenzoic acid propyl ester
-
-
3,4-Dichlorophenylserine
-
-
Ag+
-
inhibition of intramolecular electron transfer, mechnanism
Anthocyanin pigments
-
-
-
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
-
univalent anion, competitive vs. ascorbate
Fe3+
-
1 mM, 91% inhibition
Fenton's reagent
-
Fe2+ + H2O2 + 2 H+
Hg2+
-
0.01 mM, appreciable inhibition
Metabisulfite
-
complete inhibition
Ni2+
-
some authors found inhibition, others not
nordihydroguaiaretic acid
-
-
p-mercuribenzoate
-
some authors report inhibition, others do not
Piperazine N,N'-bis(2-ethanesulfonic acid)
-
anions
Tetraethylthiuramidisulfide
-
-
thiocyanate
-
weak inhibition, mixed-type inhibition
Zn2+
-
some authors found inhibition, others not
8-hydroxyquinoline
-
1 mM, 42% inhibition of enzyme from soluble fraction
azide
-
1 mM, complete inhibition
azide
-
1 mM, 42% inhibition of enzyme from soluble fraction
azide
-
8 mM, 28% inhibition; weak inhibition
azide
-
competitive vs. ascorbate, noncompetitive vs. O2
azide
-
mixed-type inhibition above pH 6, competitive inhibition at pH 5.6; weak inhibition
cyanide
-
1 mM, 57% inhibition
cyanide
-
complete inhibition
cyanide
-
0.001 mM, 50% inhibition of ascorbic acid and 2,6-dichloroindophenol oxidation
diethyldithiocarbamate
-
1 mM, 75% inhibition of enzyme from soluble fraction, 60% inhibition of enzyme from cell-wall preparatin
diethyldithiocarbamate
-
complete inhibition
diethyldithiocarbamate
-
-
diethyldithiocarbamate
-
0.0001 mM, 50% inhibition of ascorbic acid and 2,6-dichloroindophenol oxidation
ethyl xanthate
-
-
F-
-
-
F-
-
competitive vs. ascorbate, noncompetitive vs. O2
F-
-
mixed-type inhibition above pH 5.6
H2O2
-
inhibition at 5.6 mM, stimulation at 0.56 mM
H2S
-
1 mM, 97% inhibition
Thiourea
-
300 mM, 55% inhibition
Urea
-
effect on various molecular forms
Urea
-
effect on various molecular forms
additional information
-
reaction inactivation: progressive loss of activity during oxidation of ascorbic acid, not inhibited by diethyldithiocarbamate
-
additional information
-
drought conditions suppress the enzyme
-
additional information
-
the enzyme activity decreases during germination of under hypoxic conditions
-
additional information
-
natural inhibitors: cabbage extract, tomato extract, strawberry juice, extract of lemons, oranges, parsley, hips, leeks
-
additional information
-
the enzyme activity decreases during germination of under hypoxic conditions
-
additional information
-
the enzyme activity decreases during germination of under hypoxic conditions
-
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evolution
AOase occurs only in higher plants
evolution
-
AAO belongs to the large family of multicopper oxidases. AAO labelling in the cytosol, walls and chloroplasts of Chaetomorpha linum cells, whereas in angiosperms this enzyme is almost exclusively confined to the extracellular matrix, possible function of AAO in adaptation and functional evolution of its cellular location, overview
evolution
phylogenetic tree of plant ascorbate oxidases, overview
evolution
phylogenetic tree of plant ascorbate oxidases, overview
malfunction
a diminution in ascorbate oxidase activity affects carbon allocation and improves yield in tomato under water deficit, overview. RNAi knockout plants show increased fruit yield under three conditions where assimilate became limiting for wild-type plants: when fruit trusses are left unpruned, when leaves are removed or when water supply is limited. Several alterations in the transgenic lines can contribute to the improved yield and favour transport of assimilate from leaves to fruits in the ascorbate oxidase lines. RNAi lines show altered sink strength
malfunction
-
a diminution in ascorbate oxidase activity affects carbon allocation and improves yield in tomato under water deficit, overview. RNAi knockout plants show increased fruit yield under three conditions where assimilate became limiting for wild-type plants: when fruit trusses are left unpruned, when leaves are removed or when water supply is limited. Several alterations in the transgenic lines can contribute to the improved yield and favour transport of assimilate from leaves to fruits in the ascorbate oxidase lines. RNAi lines show altered sink strength
-
metabolism
-
stability of total vitamin C in situ was strongly dependent on the plant maturity stage and the processing conditions applied
metabolism
Cucurbita sp.
-
the enzyme is involved in catalyzing the oxidation of apoplastic ascorbic acid to dehydroascorbic acid
physiological function
-
AAO plays a major role in the initial phase (oxidation of L-ascorbic acid to dehydroascorbic acid) of vitamin C degradation in broccoli
physiological function
ascorbate oxidase is a blue multicopper oxidase that catalyses the four-electron reduction of dioxygen to water with concomitant one-electron oxidation of the reducing organic substrate
physiological function
ascorbate oxidase catalyzes the oxidation of ascorbate to yield water. Enzyme overexpressing plants are prone to ozone and salt stresses, whereas lower expression apparently confers resistance to unfavorable environmental conditions. High enzme expression is viewed as a possible strategy to down-regulate oxygen diffusion in root nodules, and a component of arbuscular mycorrhizal symbiosis. Key role of this gene/enzyme in both nodule and arbuscular mycorrhizal development and functioning. The enzyme might be part of the general mechanism regulating cell wall architecture
physiological function
ascorbate oxidase is an apoplastic enzyme, which controls the redox state of the apoplastic ascorbate pool, effects of ascorbate oxidase on the apoplastic redox state, overview
physiological function
-
ascorbate/dehydroascorbate play important roles in plant growth
physiological function
the enzyme is involved in antioxidant and redox regulation, overview. The protein catalyzes a complex reaction, with the safe reduction of molecular oxygen into water, without the release of reactive oxygen species, like hydrogen peroxide, superoxide anion, which result from partial O2 reduction
physiological function
the enzyme is involved in antioxidant and redox regulation, overview. The protein catalyzes a complex reaction, with the safe reduction of molecular oxygen into water, without the release of reactive oxygen species, like hydrogen peroxide, superoxide anion, which result from partial O2 reduction. Involvement of the enzyme in plant-microbe interaction
physiological function
-
ascorbate oxidase and viral movement protein interaction helps in early viral movement of Cucumber mosaic virus
physiological function
the enzyme plays an important role in fiber cell elongation and may promote cell growth by generating the oxidation of apoplasts, via the auxin-mediated signaling pathway
physiological function
-
ascorbate oxidase is an apoplastic enzyme, which controls the redox state of the apoplastic ascorbate pool, effects of ascorbate oxidase on the apoplastic redox state, overview
-
additional information
proposed catalytic model, structure-function relationship, overview. Intramolecular electron transfer from the type-l copper centre to the trinuclear copper centre
additional information
-
partially folded monomeric species might populate the energy landscape of the enzyme. The overall AAO stability is crucially controlled by a few quaternary interactions at the subunits' interface
additional information
-
a rapid and sensitive ratiometric fluorescence sensing method for the detection of ascorbic acid and ascorbate oxidase is developed
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139000
-
basic enzyme, gel filtration
61000
-
calculated from sequence
61268
Cucurbita sp.
-
x * 61268, deduced from amino acid sequence
62000
-
1 * 74000 + 1 * 62000, SDS-PAGE
62258
-
x * 62258, deduced from amino acid sequence
64000
Cucurbita sp.
-
x * 64000, SDS-PAGE
65000
-
2 * 65000, treatment with 2-mercaptoethanol results in 2 new bands, an A chain of 38000 Da and an B chain of 28000 Da, SDS-PAGE
72000
-
2 * 72000, basic enzyme, SDS-PAGE
74000
-
1 * 74000 + 1 * 62000, SDS-PAGE
132000
-
gel filtration
132000
-
sedimentation equilibrium
140000
-
-
140000
-
acidic enzyme, gel filtration
140000
-
sedimentation equilibrium and difussion studies
30000
-
1 * 30000, enzyme also exists as dimer and tetramer, SDS-PAGE
30000
-
2 * 30000, enzyme exists as monomer, dimer and tetramer, SDS-PAGE
30000
-
4 * 30000, enzyme exists as monomer, dimer and tetramer, SDS-PAGE
35000
-
1 * 35000, enzyme also exists as tetramer, octamer, dodecamer and polymer, SDS-PAGE
35000
-
4 * 35000, enzyme exists as monomer, tetramer, octamer, dodecamer and polymer, SDS-PAGE
35000
-
4 * 35000, enzyme exists as monomer, tetramer, octamer, dodecamer and polymer, SDS-PAGE
35000
-
8 * 35000, enzyme exists as monomer, tetramer, octamer, dodecamer and polymer, SDS-PAGE
35000
-
12 * 35000, enzyme exists as monomer, tetramer, octamer, dodecamer and polymer, SDS-PAGE
35000
-
x * 35000, between 670000 Da and 2000000 Da, enzyme exists as monomer, tetramer, octamer, dodecamer and polymer, SDS-PAGE
70000
-
2 * 70000, 70000 Da subunit consists of 2 polypeptide chains of 30000 and 40000 Da respectively
70000
4 * 70000, tetramer with D2 symmetry, crystal structure and SDS-PAGE, present as dimer in solution. Each subunit is built up by three domains arranged sequentially on the polypeptide chain and tightly associated in space. The folding of all three domains is of a similar beta-barrel type, analysis of intra- and intertetramer hydrogen bond and van der Waals interactions, domains structures, detailed overview
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dodecamer
-
12 * 35000, enzyme exists as monomer, tetramer, octamer, dodecamer and polymer, SDS-PAGE
heterodimer
-
1 * 72000 + 1 * 75000
homodimer
-
ascorbate oxidase is a large, multidomain, dimeric protein
octamer
-
8 * 35000, enzyme exists as monomer, tetramer, octamer, dodecamer and polymer, SDS-PAGE
polymer
-
x * 35000, between 670000 Da and 2000000 Da, enzyme exists as monomer, tetramer, octamer, dodecamer and polymer, SDS-PAGE
?
-
x * 62258, deduced from amino acid sequence
?
Cucurbita sp.
-
x * 64000, SDS-PAGE
?
Cucurbita sp.
-
x * 61268, deduced from amino acid sequence
?
x * 62800, calculated from amino acid sequence
dimer
-
1 * 74000 + 1 * 62000, SDS-PAGE
dimer
-
2 * 30000, enzyme exists as monomer, dimer and tetramer, SDS-PAGE
dimer
unfolding studies, pressure-induced and denaturing agents-induced dissociation and unfolding, and the role of dimerization in the folding strategy of a large protein, crystal structure analysis, physico-chemical properties of a molten dimer enzyme, three distinct domains per subunit, sharing a common beta-barrel topology, overview
dimer
-
2 * 70000, 70000 Da subunit consists of 2 polypeptide chains of 30000 and 40000 Da respectively
dimer
-
2 * 65000, treatment with 2-mercaptoethanol results in 2 new bands, an A chain of 38000 Da and an B chain of 28000 Da, SDS-PAGE
dimer
-
2 * 72000, basic enzyme, SDS-PAGE
monomer
-
1 * 80000
monomer
Acremonium HI-25
-
1 * 80000
-
monomer
-
1 * 30000, enzyme also exists as dimer and tetramer, SDS-PAGE
monomer
-
1 * 35000, enzyme also exists as tetramer, octamer, dodecamer and polymer, SDS-PAGE
tetramer
-
4 * 30000, enzyme exists as monomer, dimer and tetramer, SDS-PAGE
tetramer
4 * 70000, tetramer with D2 symmetry, crystal structure and SDS-PAGE, present as dimer in solution. Each subunit is built up by three domains arranged sequentially on the polypeptide chain and tightly associated in space. The folding of all three domains is of a similar beta-barrel type, analysis of intra- and intertetramer hydrogen bond and van der Waals interactions, domains structures, detailed overview
tetramer
-
4 * 35000, enzyme exists as monomer, tetramer, octamer, dodecamer and polymer, SDS-PAGE
tetramer
-
4 * 35000, enzyme exists as monomer, tetramer, octamer, dodecamer and polymer, SDS-PAGE
additional information
-
structure analysis: the monomers keep their secondary structure, whereas subtle conformational changes in the tertiary structure become apparent, salt bridges and electrostatic interactions occurring at the dimeric interface play a crucial role in the stabilization of the monomer's tertiary structure., folding/unfolding pathway, overview. Each subunit is formed by three distinct domains and contains four copper ions, three of which are located at the interface between domains, forming a so-called trinuclear centre
additional information
-
quarternary structure
additional information
-
each subunit is devided into 3 domains
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A389N
-
slightly reduced thermostability
E177K
-
slightly reduced thermostability
E540L
-
slightly reduced thermostability
H383Y
-
slightly reduced thermostability
L539E
-
slightly increased thermostability
M542L
-
strongly reduced thermostability
P190I
-
reduced thermostability
P190I/V193P
-
pH optimum shifted to pH 4.5, slightly reduced thermostability
Q183R
-
similar properties as wild-type
Q382G
-
slightly higher thermostability
R194Q
-
similar properties as wild-type
R387A
-
slightly reduced thermostability
T527A
-
similar properties as wild-type
V185K
-
slightly reduced thermostability
V185K/V188R
-
similar properties as wild-type
V188R/P190I
-
no detectable activity
V193E
-
pH optimum shifted to pH 4.5, very thermolabile
V193F
-
slightly reduced thermostability
V193G
-
very thermolabile
V193H
-
slightly reduced thermostability
V193K
-
slightly reduced thermostability
V193P
-
pH optimum shifted to pH 5.0
V193T
-
similar properties as wild-type
V385K
-
reduced thermostability
V543H
-
very thermolabile
W189H
-
no detectable activity
W386H
-
reduced thermostability
additional information
-
mutant with T-DNA inserted into enzyme gene, delay in flowering time, at high salinity, increase in percentage of germination, photosynthetic activity and seed yield
additional information
-
construction of transgenic Nicotiana tabacum plants overexpressing the enzyme in sense orientation, lines P221 and P372, the apoplast ascorbic acid pool is only about 3% reduced in enzyme 'in sense' lines, ascorbic acid oxidase sense leaves exhibit significantly lower dehydroascorbate reductase and ascorbate peroxidase activities than wild-type and antisense leaves, phenotype and effects on enzyme regulation, overview
additional information
-
construction of three transgenic enzyme overexpressing lines R50, R60, and R68, selected on the basis of enzyme expression and single transgene copy number, the overexpression has a slight effect on chlorophyll and carotinoid contents, and on sensitivity to oxidative stress, phenotypes, overview
additional information
construction of RNAi knockout plants lacking AAO activity, phenotype, overview. RNAi tomato lines have reduced ascorbate oxidase transcript and activity in leaves. Stomatal conductance is increased in transgenic ascorbate oxidase lines
additional information
-
construction of RNAi knockout plants lacking AAO activity, phenotype, overview. RNAi tomato lines have reduced ascorbate oxidase transcript and activity in leaves. Stomatal conductance is increased in transgenic ascorbate oxidase lines
additional information
-
construction of RNAi knockout plants lacking AAO activity, phenotype, overview. RNAi tomato lines have reduced ascorbate oxidase transcript and activity in leaves. Stomatal conductance is increased in transgenic ascorbate oxidase lines
-
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