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Information on EC 1.11.1.11 - L-ascorbate peroxidase and Organism(s) Oryza sativa and UniProt Accession Q7XJ02
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1.11.1.11 L-ascorbate peroxidaseIUBMB Comments
A heme protein. Oxidizes ascorbate and low molecular weight aromatic substrates. The monodehydroascorbate radical produced is either directly reduced back to ascorbate by EC 1.6.5.4 [monodehydroascorbate reductase (NADH)] or undergoes non-enzymic disproportionation to ascorbate and dehydroascorbate.
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Word Map
- 1.11.1.11
- catalase
- dismutase
- sod
- malondialdehyde
- seedling
-
chlorophyl
- dehydroascorbate
- guaiacol
- shoot
- drought
- biomass
- phenol
- chloroplast
- cultivar
- monodehydroascorbate
-
electrolyte
-
carotenoid
-
non-enzymatic
- cadmium
- peroxidases
- asa
- lipoxygenase
- thylakoidal
-
foliar
-
abscisic
- photosystem
-
stomatal
-
hydroponic
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postharvest
- mdhar
- aestivum
- triticum
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ascorbate-glutathione
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photochemical
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phytotoxicity
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1.6.4.2
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chilling
- phytochelatins
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irrigation
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non-photochemical
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cd-induced
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phytoextraction
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transpiration
-
salt-stressed
-
hoagland
-
photoinhibition
- fe-sod
- juncea
- synthesis
- analysis
- agriculture
-
phytoremediation
-
ros-scavenging
The taxonomic range for the selected organisms is: Oryza sativa
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
ascorbate peroxidase, apex2, cytosolic ascorbate peroxidase, lmapx, ascorbate peroxidase 2, l-ascorbate peroxidase, ascorbate peroxidase 1, ascorbic acid peroxidase, osapx8, osapx2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ascorbate peroxidase
ascorbate peroxidase 8
ascorbic acid peroxidase
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L-ascorbic acid peroxidase
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-
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L-ascorbic acid-specific peroxidase
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OsAPx8
peroxidase, ascorbate
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-
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ascorbate peroxidase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
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-
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oxidation
reduction
peroxidation
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-
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oxidation
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reduction
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PATHWAY SOURCE
PATHWAYS
BRENDA
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-, -
SYSTEMATIC NAME
IUBMB Comments
L-ascorbate:hydrogen-peroxide oxidoreductase
A heme protein. Oxidizes ascorbate and low molecular weight aromatic substrates. The monodehydroascorbate radical produced is either directly reduced back to ascorbate by EC 1.6.5.4 [monodehydroascorbate reductase (NADH)] or undergoes non-enzymic disproportionation to ascorbate and dehydroascorbate.
CAS REGISTRY NUMBER
COMMENTARY
72906-87-7
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
glutathione + H2O2
? + H2O
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30% of the activity with ascorbate, APX 1, 13% of the activity with ascorbate, APX 2
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-
?
guaiacol + H2O2
? + H2O
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45% of the activity with ascorbate, APX 1, 15% of the activity with ascorbate, APX 2
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-
?
NADH + H+ + H2O2
NAD+ + H2O
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10% of the activity with ascorbate, APX 1, 1% of the activity with ascorbate, APX 2
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?
NADPH + H+ + H2O2
NADP+ + H2O
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27% of the activity with ascorbate, APX 1, 21% of the activity with ascorbate, APX 2
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3,3'-dithiobis(6-nitrobenzoic acid)
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5 mM, 80% residual activity, APX 1, 24% residual activity, APX 2
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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enzyme activity of ascorbate peroxidase (APX), for 2 varieties, Suakoko8 and IR31785, in samples of the leaf blade, the sheath of the youngest fully developed leaf of the main culm, the blade and sheath of the third youngest fully developed leaf of the main culm, and the root, samples are fresh or stored for 1-12 weeks frozen, or freeze-dried, overview
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
of seedlings. The expression of OsAPx7 is not affected by 150 mM and 200 mM NaCl, but is 40% decreased by 300 mM NaCl
root. The expression of OsAPx7 is not affected by 150 mM and 200 mM NaCl, but is 40% decreased by 300 mM NaCl
additional information
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APX activity is highest in the leaf blades and tends to be higher in older than in younger plant parts
of seedlings. NaCl-enhanced expression of OsAPx8 in rice roots is mediated through an accumulation of abscisic acid. Na+ but not Cl- is required for enhancing OsAPx8 expression. H2O2 is not involved in the regulation of NaCl-induced OsAPx8 expression in rice roots
of seedlings. No significant increase due to NaCl can be detected in the expression of OsAPx1
of seedlings. No significant increase due to NaCl can be detected in the expression of OsAPx2
of seedlings. No significant increase due to NaCl can be detected in the expression of OsAPx3
of seedlings. No significant increase due to NaCl can be detected in the expression of OsAPx4
of seedlings. No significant increase due to NaCl can be detected in the expression of OsAPx5
of seedlings. No significant increase due to NaCl can be detected in the expression of OsAPx6
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root of seedling, increase in enzyme activity after treatment with NaCl or H2O2, inhibition of enzyme accumulation by diphenyleneiodinium chloride or imidazole, but not by dimethylthiourea
root. NaCl-enhanced expression of OsAPx8 in rice roots is mediated through an accumulation of abscisic acid. Na+ but not Cl- is required for enhancing OsAPx8 expression. H2O2 is not involved in the regulation of NaCl-induced OsAPx8 expression in rice roots
root. No significant increase due to NaCl can be detected in the expression of OsAPx1
root. No significant increase due to NaCl can be detected in the expression of OsAPx2
root. No significant increase due to NaCl can be detected in the expression of OsAPx3
root. No significant increase due to NaCl can be detected in the expression of OsAPx4
root. No significant increase due to NaCl can be detected in the expression of OsAPx5
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ethylene glycol
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PEG 6000, 40% in assay medium, 50% inhibition of aPX 1, 65% inhibition of APX 2 with increase in enzyme Km values, incorporation of 1 M proline, glycine betaine or sucrose in presence of PEG in the assay medium restores
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
effect of dfferent storage methods such as freeze-drying, freezing at -20°C, and freezing at -80°C on the activity of enzyme ascorbate peroxidase from two rice varieties, overview. When subjected to different storage methods, there are no differences between varieties, but strong effects of the different storage methods on enzyme activities are found strongly differing between extracts from stored tissue samples or extracts stored from freshly sampled material. Enzyme-specific storage methods and durations allow for expanding the window for analyses in large experimental studies involving destructive samplings for enzyme kinetics
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Arabidopsis. Transgenic lines over-expressing OsAPXb show higher salt tolerance than OsAPXa transgenic lines. Overproduction of OsAPXb enhances and maintains APX activity to a much higher degree than OsAPXa in transgenic Arabidopsis during treatment with different concentrations of NaCl, enhances the active oxygen scavenging system, and protects plants from salt stress by equilibrating H2O2 metabolism
overexpression in Arabidopsis. Transgenic lines over-expressing OsAPXb showed higher salt tolerance than OsAPXa transgenic lines. Overproduction of OsAPXb enhances and maintains APX activity to a much higher degree than OsAPXa in transgenic Arabidopsis during treatment with different concentrations of NaCl, enhances the active oxygen scavenging system, and protects plants from salt stress by equilibrating H2O2 metabolism
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
salt stress, Na+ induces expression of OsAPx8, , NaCl-enhanced expression of OsAPx8 in rice roots is mediated through an accumulation of the plant hormone ABA
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Tsai, Y.C.; Hong, C.Y.; Liu, L.F.; Kao, C.H.
Expression of ascorbate peroxidase and glutathione reductase in roots of rice seedlings in response to NaCl and H2O2
J. Plant Physiol.
162
291-299
2005
Oryza sativa
Sharma, P.; Dubey, R.S.
Ascorbate peroxidase from rice seedlings: properties of enzyme isoforms, effects of stresses and protective roles of osmolytes
Plant Sci.
167
541-550
2004
Oryza sativa
Hong, C.Y.; Hsu, Y.T.; Tsai, Y.C.; Kao, C.H.
Expression of ascorbate peroxidase 8 in roots of rice (Oryza sativa L.) seedlings in response to NaCl
J. Exp. Bot.
58
3273-3283
2007
Oryza sativa (P0C0L0), Oryza sativa (P0C0L1), Oryza sativa (Q0JEQ2), Oryza sativa (Q10N21), Oryza sativa (Q69SV0), Oryza sativa (Q6ZJJ1), Oryza sativa (Q7XJ02), Oryza sativa (Q9FE01), Oryza sativa
Lu, Z.; Liu, D.; Liu, S.
Two rice cytosolic ascorbate peroxidases differentially improve salt tolerance in transgenic Arabidopsis
Plant Cell Rep.
26
1909-1917
2007
Oryza sativa (Q10N21), Oryza sativa (Q9FE01), Oryza sativa
Hong, C.Y.; Kao, C.H.
NaCl-induced expression of ascorbate peroxidase 8 in roots of rice (Oryza sativa L.) seedlings is not associated with osmotic component
Plant Signal. Behav.
3
199-201
2008
Oryza sativa
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