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Information on EC 1.11.1.11 - L-ascorbate peroxidase and Organism(s) Arabidopsis thaliana and UniProt Accession Q42592
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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
-
postharvest
- mdhar
- aestivum
- triticum
-
ascorbate-glutathione
-
photochemical
-
phytotoxicity
-
1.6.4.2
-
chilling
- phytochelatins
-
irrigation
-
non-photochemical
-
cd-induced
-
phytoextraction
-
transpiration
-
salt-stressed
-
hoagland
-
photoinhibition
- fe-sod
- juncea
- synthesis
- analysis
- agriculture
-
phytoremediation
-
ros-scavenging
The taxonomic range for the selected organisms is: Arabidopsis thaliana
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
APXS
AT4G08390
APX
APX1
APXT
ascorbate peroxidase
ascorbate peroxidase 1
ascorbic acid peroxidase
-
-
-
-
At1g07890
AT1G77490
L-ascorbate peroxidase 6
L-ascorbic acid peroxidase
-
-
-
-
L-ascorbic acid-specific peroxidase
-
-
-
-
peroxidase, ascorbate
-
-
-
-
ascorbate peroxidase
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
redox reaction
-
-
-
-
oxidation
reduction
peroxidation
-
-
-
-
oxidation
-
-
-
-
reduction
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-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
-
-, -
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
-
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
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
?
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
AtAPX1 exhibits both peroxidase and chaperone activities
-
-
-
additional information
?
-
-
AtAPX1 exhibits both peroxidase and chaperone activities
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
APX enzymatic activity is measured by the decrease in absorbance at 290 nm due to the oxidation of ascorbate. The AtAPX1 protein shows a high chaperone activity as incubation of MDH with increasing amounts of AtAPX1 results in a concomitant decrease in the aggregation of MDH at 43°C. The aggregation of MDH is effectively suppressed at a subunit molar ratio of MDH to AtAPX1 of 1:2
-
-
-
additional information
?
-
-
APX enzymatic activity is measured by the decrease in absorbance at 290 nm due to the oxidation of ascorbate. The AtAPX1 protein shows a high chaperone activity as incubation of MDH with increasing amounts of AtAPX1 results in a concomitant decrease in the aggregation of MDH at 43°C. The aggregation of MDH is effectively suppressed at a subunit molar ratio of MDH to AtAPX1 of 1:2
-
-
-
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
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
?
2 L-ascorbate + H2O2 + 2 H+
L-ascorbate + L-dehydroascorbate + 2 H2O
-
-
-
?
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
AtAPX1 exhibits both peroxidase and chaperone activities
-
-
-
additional information
?
-
-
AtAPX1 exhibits both peroxidase and chaperone activities
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
additional information
?
-
enzyme interaction analysis, overview
-
-
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Fe2+
Fe2+
in the heme group
Fe2+
in the heme group
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
tyrosine nitration has a negative impact. No effects are observed on the chaperone function and the oligomeric status of AtAPX1
-
additional information
-
tyrosine nitration has a negative impact. No effects are observed on the chaperone function and the oligomeric status of AtAPX1
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
methyl jasmonate
knockout mutant plants lacking Apx1 show high sensitivity to wounding and methyl jasmonate treatment. In the leaves of wild-type plants, H2O2 accumulates only in the vicinity of the wound, while in the leaves of the knockout mutant plants it accumulates extensively from damaged to undamaged regions. During methyl jasmonate treatment, the levels of H2O2 are much higher in the leaves of Apx1 knockout plants
additional information
S-nitrosylation and S-sulfhydration positively regulate the peroxidase activity, whereas no effects are observed on the chaperone function and the oligomeric status of AtAPX1
-
additional information
-
S-nitrosylation and S-sulfhydration positively regulate the peroxidase activity, whereas no effects are observed on the chaperone function and the oligomeric status of AtAPX1
-
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42
fusion protein with C-end tail of human alpha-synuclein, 50% residual activity
64.5
fusion protein with C-end tail of Arabidopsis tubulin TUA2, 50% residual activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
8.31
isozyme SAPX, sequence calculation
5.72
isozyme APX1, sequence calculation
5.87
isozyme APX2, sequence calculation
6.47
isozyme APX3, sequence calculation
6.81
isozyme AtTAPX, sequence calculation
8.8
isozyme APX5, sequence calculation
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
the constitutive expression of APX6 is restricted to old and dying cells and absent in younger tissues
APX6 is nearly 4fold higher in late senescing leaves of 6.5-week-old plants compared with young green leaves of 4-week-old plants
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
stroma
stromal ascorbate peroxidase is particularly important for photoprotection during the early greening process. In mature leaves, thylakoid-bound enzyme and stromal enzyme are functionally redundant, and crucial upon sudden onset of oxidative stress. The chloroplast ascorbate peroxidases contribute to chloroplast retrograde signalling pathways upon slight fluctuations in the accumulation of H2O2 in chloroplasts
-
thylakoid-bound
stromal enzyme is particularly important for photoprotection during the early greening process. In mature leaves, thylakoid-bound enzyme and stromal enzyme are functionally redundant, and crucial upon sudden onset of oxidative stress. The chloroplast ascorbate peroxidases contribute to chloroplast retrograde signalling pathways upon slight fluctuations in the accumulation of H2O2 in chloroplasts
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
APX belongs to the class I heme-peroxidases, isozyme AtSAPX belongs to group IV. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
malfunction
stromal and thylakoid membrane-bound ascorbate peroxidases (sAPX and tAPX, respectively) knockout mutants do not exhibit a visible phenotype under high-light (HL) stress. PGR5-dependent mechanisms compensate for chloroplast APXs, and vice versa
physiological function
evolution
malfunction
physiological function
additional information
physiological function
hydrogen peroxide (H2O2) is one important component of ROS and able to modulate plant growth and development at low level and damage plant cells at high concentrations. Ascorbate peroxidase (APX) shows high affinity towards H2O2 and plays vital roles in H2O2-scavenging
physiological function
stromal and thylakoid membrane-bound ascorbate peroxidases (sAPX and tAPX, respectively) are major H2O2-scavenging enzymes in chloroplasts. PGR5-dependent mechanisms compensate for chloroplast APXs, and vice versa under high-light stress
evolution
APX belongs to the class I heme-peroxidases, isozyme AtAPX1 belongs to group I. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme AtAPX2 belongs to group I. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme AtAPX3 belongs to group II. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme AtAPX5 belongs to group II. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme AtAPX6 belongs to group V. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
evolution
APX belongs to the class I heme-peroxidases, isozyme AtTAPX belongs to group IV. APXs in the selected plant species show high evolutionary conservation and are able to divide into seven groups, group I to VII. Members in the groups contain abundant phosphorylation sites. Group I and VII have only protein kinase C site. Additionally, promoters of the APXs contain abundant stress-related cis-elements. APX is comprised of different isozymes, which are encoded by a multi-gene family and found in many compartments of cell
malfunction
reduced APX activity, increased H2O2 level, and altered redox state of the ascorbate pool in mature pre-senescing green leaves of the apx6 mutants correlated with the early onset of senescence. Mutants of squamosa promoter binding protein-like7 (SPL7), the master regulator of copper homeostasis and miR398 expression, have a higher APX6 level compared to the wild-type, which further increases under copper deficiency. APX6-deficient mutants prematurely induce senescence programs triggered by the transition to flowering, extended darkness, and ethylene. Mutants of SPL7 show increased levels of APX6 in as yet flowering or senescing plants. The earlier onset of senescence in the mutants is accompanied by higher levels of H2O2 compared with the wild-type and reduced ability to adjust the leaves' redox state
malfunction
stromal and thylakoid membrane-bound ascorbate peroxidases (sAPX and tAPX, respectively) knockout mutants do not exhibit a visible phenotype under high-light (HL) stress. PGR5-dependent mechanisms compensate for chloroplast APXs, and vice versa
physiological function
knockout mutant plants lacking Apx1 show high sensitivity to wounding and methyl jasmonate treatment. In the leaves of wild-type plants, H2O2 accumulates only in the vicinity of the wound, while in the leaves of the knockout mutant plants it accumulates extensively from damaged to undamaged regions. During methyl jasmonate treatment, the levels of H2O2 are much higher in the leaves of Apx1 knockout plants. Oxidative damage in the chloroplasts and nucleus is also enhanced in the leaves of apx1 knockout plants
physiological function
enzyme APX6 is a modulator of ROS/redox homeostasis and signaling in aging leaves that plays an important role in developmental- and stress-induced senescence programs. Senescence marks the last step in the development of annual plants, culminating in the death of tissues, and finally, the entire organism
physiological function
hydrogen peroxide (H2O2) is one important component of ROS and able to modulate plant growth and development at low level and damage plant cells at high concentrations. Ascorbate peroxidase (APX) shows high affinity towards H2O2 and plays vital roles in H2O2-scavenging
physiological function
stromal and thylakoid membrane-bound ascorbate peroxidases (sAPX and tAPX, respectively) are major H2O2-scavenging enzymes in chloroplasts. PGR5-dependent mechanisms compensate for chloroplast APXs, and vice versa under high-light stress
physiological function
the ascorbate-glutathione cycle is a pivotal antioxidant system involved in the regulation of H2O2 levels. Ascorbate peroxidase, being an important enzymatic antioxidant of this cycle, catalyzes the reduction of H2O2 to water using ascorbate as a specific electron donor. Cytosolic APX1 from Arabidopsis thaliana (AtAPX1) is crucial for tuning the regulation of H2O2, playing a key role in providing acclimation to a combination of heat and drought stress. Enzyme AtAPX1 plays a dual role behaving both as a regular peroxidase and a chaperone molecule, as the latter with the ability to inhibit the thermal aggregation of malate dehydrogenase (MDH), a heat-sensitive substrate. The dual activity of AtAPX1 is strongly related to its structural status. Abiotic stresses, such as heat and salt, regulate this dual function and structural status of AtAPX1 through the association and dissociation of APX proteins, respectively. The main dimeric form of the AtAPX1 protein shows the highest peroxidase activity, whereas the HMW form exhibits the highest chaperone activity. S-nitrosylation and S-sulfhydration positively regulate the peroxidase activity, whereas tyrosine nitration has a negative impact. No effects are observed on the chaperone function and the oligomeric status of AtAPX1
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
abiotic stress modulates structural changes in AtAPX1 protein and function in vivo. The recombinant AtAPX1 protein shows oligomeric forms besides the major dimeric form, and these different forms appear to play varying roles depending on the structural status of the protein. The protein exhibits a transition from dimeric units to HMW complexes under heat stress, whereas the HMW complexes are dissociated under salt stress
additional information
-
abiotic stress modulates structural changes in AtAPX1 protein and function in vivo. The recombinant AtAPX1 protein shows oligomeric forms besides the major dimeric form, and these different forms appear to play varying roles depending on the structural status of the protein. The protein exhibits a transition from dimeric units to HMW complexes under heat stress, whereas the HMW complexes are dissociated under salt stress
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
bioinformatics methods and public databases are used to evaluate the physicochemical properties, conserved motifs, potential modifications and cis-elements in all the APXs, and protein-protein network and expression profiles of rice APX isozymes, modeling, overview
additional information
the coding sequence of APX6 is a potential target of miR398, which is a key regulator of copper redistribution
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). APXS_ARATH
372
0
40407
Swiss-Prot
Chloroplast (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the second size exclusion chromatography (SEC) fraction (F2) shows a band of proteins between 158 and 440 kDa, whereas the F3 fraction corresponding to the dimeric form of AtAPX1 appears below 158 kDa, representing the major peak in SEC analysis
additional information
-
the second size exclusion chromatography (SEC) fraction (F2) shows a band of proteins between 158 and 440 kDa, whereas the F3 fraction corresponding to the dimeric form of AtAPX1 appears below 158 kDa, representing the major peak in SEC analysis
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
cytosol-type APX1 from Arabidopsis thaliana (AtAPX1) exists in multimeric forms ranging from dimeric to high-molecular-weight (HMW) complexes. The structure of AtAPX1 is regulated by heat and salt stresses, with both involved in the association and dissociation of complexes, respectively. No effects are observed on the chaperone function and the oligomeric status of AtAPX1
additional information
-
cytosol-type APX1 from Arabidopsis thaliana (AtAPX1) exists in multimeric forms ranging from dimeric to high-molecular-weight (HMW) complexes. The structure of AtAPX1 is regulated by heat and salt stresses, with both involved in the association and dissociation of complexes, respectively. No effects are observed on the chaperone function and the oligomeric status of AtAPX1
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
isozyme AtSAPX contains one phosphorylation site for protein kinase A and 15 sites for protein kinase C
lipoprotein
1 site of S-farnesylation
phosphoprotein
S-nitrosylation
additional information
phosphoprotein
isozyme AtAPX1 contains one phosphorylation site for protein kinase C
phosphoprotein
isozyme AtAPX2 contains two phosphorylation sites for protein kinase C
phosphoprotein
isozyme AtAPX3 contains three phosphorylation sites for protein kinase C
phosphoprotein
isozyme AtAPX5 contains 4 phosphorylation sites for protein kinase C and 2 sites for protein kinase A
phosphoprotein
isozyme AtAPX6 contains one phosphorylation site for protein kinase A, one site for protein kinase B, and 5 sites for protein kinase C
phosphoprotein
isozyme AtTAPX contains one phosphorylation site for protein kinase A and 8 sites for protein kinase C
S-nitrosylation
recombinant AtAPX1 protein is incubated with various concentrations (0-1 mM) of S-nitrosoglutathione (GSNO) at 25°C for 30 min in the dark to achieve S-nitrosylation of protein. S-nitrosylation and S-sulfhydration positively regulate the peroxidase activity, whereas no effects are observed on the chaperone function and the oligomeric status of AtAPX1. The GSNO-induced change in the activity of APX1 is not related to its oligomeric status, and NaHS-treated. In contrast to the negative regulation of the peroxidase activity of the SIN-1-treated protein, no effects on the chaperone activity are observed. Treatment with SIN-1 (peroxynitrite donor) does not cause any conformational changes eitherindicating that tyrosine nitration does not affect the structural status of AtAPX1
additional information
age-dependent post-transcriptional regulation of APX6
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
generation of stromal and thylakoid membrane-bound ascorbate peroxidases (sAPX and tAPX, respectively) knockout mutants, exhibiting no visible phenotype under high-light (HL) stress. The Arabidopsis thaliana sapx/tapx double mutant is crossed with a proton gradient regulation 5 (pgr5) single mutant, wherein both DELTApH-dependent mechanisms are impaired. The sapx/tapx/pgr5 triple mutant exhibits extreme sensitivity to HL compared with its parental lines. This phenotype is consistent with cellular redox perturbations and enhanced expression of many oxidative stress-responsive genes. These findings demonstrate that the PGR5-dependent mechanisms compensate for chloroplast APXs, and vice versa. The failure of induction of non-photochemical quenching in pgr5 (because of the limitation in DELTApH formation) is partially recovered in sapx/tapx/pgr5 mutants. This recovery is dependent on the NADH dehydrogenase-like complex-dependent pathway for cyclic electron flow around photosystem I
additional information
generation of stromal and thylakoid membrane-bound ascorbate peroxidases (sAPX and tAPX, respectively) knockout mutants, exhibiting no visible phenotype under high-light (HL) stress. The Arabidopsis thaliana sapx/tapx double mutant is crossed with a proton gradient regulation 5 (pgr5) single mutant, wherein both DELTApH-dependent mechanisms are impaired. The sapx/tapx/pgr5 triple mutant exhibits extreme sensitivity to HL compared with its parental lines. This phenotype is consistent with cellular redox perturbations and enhanced expression of many oxidative stress-responsive genes. These findings demonstrate that the PGR5-dependent mechanisms compensate for chloroplast APXs, and vice versa. The failure of induction of non-photochemical quenching in pgr5 (because of the limitation in DELTApH formation) is partially recovered in sapx/tapx/pgr5 mutants. This recovery is dependent on the NADH dehydrogenase-like complex-dependent pathway for cyclic electron flow around photosystem I
additional information
expression with hyperacidic fusion partners such as C-end tail of human alpha-synuclein, C-end tails of Arabidopsis tubulins, TUA2 and TUB3, Escherichia coli msyB and C-end tail of Escherichia coli yjgD efficiently improves the thermostability and prevents thermal inactivation of APX1 with an elevated heat tolerance of at least 2°C
additional information
expression analysis of cytosolic APX isozymes in recombinant Nicotiana benthamiana shows that only APX6 displays a gradual increase in expression along the leaf blade with about a 4 and a 30fold higher level in the mid and tip sections, respectively, compared with the base. The changes in the level of APX6 correlate with the changes in the expression of the senescence marker gene SAG12. The age-dependent activation of the APX6 promoter is proven by APX6pro::GUS expression in leaves at different ages of the plants, phenotypes, detailed overview
additional information
generation of stromal and thylakoid membrane-bound ascorbate peroxidases (sAPX and tAPX, respectively) knockout mutants, exhibiting no visible phenotype under high-light (HL) stress. The Arabidopsis thaliana sapx/tapx double mutant is crossed with a proton gradient regulation 5 (pgr5) single mutant, wherein both DELTApH-dependent mechanisms are impaired. The sapx/tapx/pgr5 triple mutant exhibits extreme sensitivity to HL compared with its parental lines. This phenotype is consistent with cellular redox perturbations and enhanced expression of many oxidative stress-responsive genes. These findings demonstrate that the PGR5-dependent mechanisms compensate for chloroplast APXs, and vice versa. The failure of induction of non-photochemical quenching in pgr5 (because of the limitation in DELTApH formation) is partially recovered in sapx/tapx/pgr5 mutants. This recovery is dependent on the NADH dehydrogenase-like complex-dependent pathway for cyclic electron flow around photosystem I
additional information
generation of stromal and thylakoid membrane-bound ascorbate peroxidases (sAPX and tAPX, respectively) knockout mutants, exhibiting no visible phenotype under high-light (HL) stress. The Arabidopsis thaliana sapx/tapx double mutant is crossed with a proton gradient regulation 5 (pgr5) single mutant, wherein both DELTApH-dependent mechanisms are impaired. The sapx/tapx/pgr5 triple mutant exhibits extreme sensitivity to HL compared with its parental lines. This phenotype is consistent with cellular redox perturbations and enhanced expression of many oxidative stress-responsive genes. These findings demonstrate that the PGR5-dependent mechanisms compensate for chloroplast APXs, and vice versa. The failure of induction of non-photochemical quenching in pgr5 (because of the limitation in DELTApH formation) is partially recovered in sapx/tapx/pgr5 mutants. This recovery is dependent on the NADH dehydrogenase-like complex-dependent pathway for cyclic electron flow around photosystem I
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Escherichia coli recombinant stromal ascorbate peroxidase is purified with a HisTrap kit, proteins are used to immunize rabbits and rats
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recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, tag cleavage by thrombin, ultrafiltration, and gel filtration, again followed by ultrafiltration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence analysis, sequence comparisons and phylogenetic analysis and tree, conserved cis-regulatory elements in the promoters of the APX isozyme, overview
DNA and amino acid sequence analysis, sequence comparisons and phylogenetic analysis and tree, conserved cis-regulatory elements in the promoters of the APX isozyme, overview
full length AtstAPX is cloned into the pPZP221 binary vector, introduced into Arabidopsis thaliana by the floral dip method using Agrobacterium tumefaciens strain GV3101, for the generation of antibodies into the vector pQE80L for expression in Escherichia coli cells
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gee APX, DNA and amino acid sequence analysis, sequence comparisons and phylogenetic analysis and tree, conserved cis-regulatory elements in the promoters of the APX isozyme, overview
gene APX1, DNA and amino acid sequence analysis, sequence comparisons and phylogenetic analysis and tree, conserved cis-regulatory elements in the promoters of the APX isozyme, overview
gene APX6, quantitative RT-PCR enzyme expression analysis, transient expression assays in Nicotiana benthamiana leaves, constitutive expression of APX6 is restricted to old and dying cells and absent in younger tissues, thus age-dependent post-transcriptional regulation of APX6. The coding sequence of APX6 is a potential target of miR398, which is a key regulator of copper redistribution
gene AtAPX1, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
APX6 is a bona fide senescence-associated gene. High osmotic conditions, dark stress, and abscisic acid (ABA) activate APX6 expression in an age-dependent manner. APX6 expression is specifically induced in aging leaves and in response to senescence-promoting stimuli such as abscisic acid (ABA), extended darkness, and osmotic stress. apx6 mutants showed early developmental senescence and increased sensitivity to dark stress. Mutants of squamosa promoter binding protein-like7 (SPL7), the master regulator of copper homeostasis and miR398 expression, have a higher APX6 level compared to the wild-type, which further increases under copper deficiency. miR398 is a potential post-transcriptional regulator of APX6
cytosolic ascorbate peroxidase 1 protein and mRNA accumulates during drought and heat stress
-
identification of potential small RNAs involved in regulating APX6 level, overview
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
overexpression of thylakoidal isozyme, increased resistance to the herbicide Paraquat but not to photoinhibitory treatments ot iron or copper overload. Sodium nitroprusside partially inhibits enzyme activity
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Lokhande, S.D.; Ogawa, K.; Tanaka, A.; Hara, T.
Effect of temperature on ascorbate peroxidase activity and flowering of Arabidopsis thaliana ecotypes under different light conditions
J. Plant Physiol.
160
57-64
2003
Arabidopsis thaliana
Murgia, I.; Tarantino, D.; Vannini, C.; Bracale, M.; Carravieri, S.; Soave, C.
Arabidopsis thaliana plants overexpressing thylakoidal ascorbate peroxidase show increased resistance to Paraquat-induced photooxidative stress and to nitric oxide-induced cell death
Plant J.
38
940-953
2004
Arabidopsis thaliana
Panchuk, II; Volkov, R.A.; Schoffl, F.
Heat stress- and heat shock transcription factor-dependent expression and activity of ascorbate peroxidase in Arabidopsis
Plant Physiol.
129
838-853
2002
Arabidopsis thaliana
Kangasjaervi, S.; Lepistoe, A.; Haennikaeinen, K.; Piippo, M.; Luomala, E.M.; Aro, E.M.; Rintamaeki, E.
Diverse roles for chloroplast stromal and thylakoid-bound ascorbate peroxidases in plant stress responses
Biochem. J.
412
275-285
2008
Arabidopsis thaliana (Q42592), Arabidopsis thaliana (Q42593)
Koussevitzky, S.; Suzuki, N.; Huntington, S.; Armijo, L.; Sha, W.; Cortes, D.; Shulaev, V.; Mittler, R.
Ascorbate peroxidase 1 plays a key role in the response of Arabidopsis thaliana to stress combination
J. Biol. Chem.
283
34197-34203
2008
Arabidopsis thaliana
Hirooka, S.; Misumi, O.; Yoshida, M.; Mori, T.; Nishida, K.; Yagisawa, F.; Yoshida, Y.; Fujiwara, T.; Kuroiwa, H.; Kuroiwa, T.
Expression of the Cyanidioschyzon merolae stromal ascorbate peroxidase in Arabidopsis thaliana enhances thermotolerance
Plant Cell Rep.
28
1881-1893
2009
Arabidopsis thaliana, Cyanidioschyzon merolae
Maruta, T.; Inoue, T.; Noshi, M.; Tamoi, M.; Yabuta, Y.; Yoshimura, K.; Ishikawa, T.; Shigeoka, S.
Cytosolic ascorbate peroxidase 1 protects organelles against oxidative stress by wounding- and jasmonate-induced H2O2 in Arabidopsis plants
Biochim. Biophys. Acta
1820
1901-1907
2012
Arabidopsis thaliana (Q05431)
Zhang, M.; Gong, M.; Yang, Y.; Li, X.; Wang, H.; Zou, Z.
Improvement on the thermal stability and activity of plant cytosolic ascorbate peroxidase 1 by tailing hyper-acidic fusion partners
Biotechnol. Lett.
37
891-898
2015
Jatropha curcas (D3GC00), Jatropha curcas, Arabidopsis thaliana (Q05431)
Kaur, S.; Prakash, P.; Bak, D.H.; Hong, S.H.; Cho, C.; Chung, M.S.; Kim, J.H.; Lee, S.; Bai, H.W.; Lee, S.Y.; Chung, B.Y.; Lee, S.S.
Regulation of dual activity of ascorbate peroxidase 1 from Arabidopsis thaliana by conformational changes and posttranslational modifications
Front. Plant Sci.
12
678111
2021
Arabidopsis thaliana (Q05431), Arabidopsis thaliana, Arabidopsis thaliana Col-0 (Q05431)
Kameoka, T.; Okayasu, T.; Kikuraku, K.; Ogawa, T.; Sawa, Y.; Yamamoto, H.; Ishikawa, T.; Maruta, T.
Cooperation of chloroplast ascorbate peroxidases and proton gradient regulation 5 is critical for protecting Arabidopsis plants from photo-oxidative stress
Plant J.
107
876-892
2021
Arabidopsis thaliana (Q42592), Arabidopsis thaliana (Q42593)
Chen, C.; Galon, Y.; Rahmati Ishka, M.; Malihi, S.; Shimanovsky, V.; Twito, S.; Rath, A.; Vatamaniuk, O.K.; Miller, G.
Ascrobate peroxidase6 delays the onset of age-dependent leaf senescence
Plant Physiol.
185
441-456
2021
Arabidopsis thaliana (Q8GY91)
Wu, B.; Wang, B.
Comparative analysis of ascorbate peroxidases (APXs) from selected plants with a special focus on Oryza sativa employing public databases
PLoS ONE
14
e0226543
2019
Chlamydomonas reinhardtii, Chlamydomonas reinhardtii (A0A2K3DF40), Chlamydomonas reinhardtii (A0A2K3DPX4), Chlamydomonas reinhardtii (O49822), Populus trichocarpa, Populus trichocarpa (A0A2K1Z156), Populus trichocarpa (A0A2K2AW57), Populus trichocarpa (A0A2K2BFE0), Populus trichocarpa (A0A3N7F4X7), Populus trichocarpa (A9P9X7), Populus trichocarpa (B9HAE4), Populus trichocarpa (B9HR68), Populus trichocarpa (B9MXE8), Populus trichocarpa (U5GAF3), no activity in Arabidopsis thaliana isozyme AtAPX4, Physcomitrium patens (A0A2K1ITN5), Physcomitrium patens (A0A2K1J327), Physcomitrium patens (A0A2K1L9S9), Physcomitrium patens (A9U1S4), Physcomitrium patens (Q8GU36), Oryza sativa Japonica Group (P0C0L0), Oryza sativa Japonica Group (P0C0L1), Oryza sativa Japonica Group (Q0JEQ2), Oryza sativa Japonica Group (Q10N21), Oryza sativa Japonica Group (Q69SV0), Oryza sativa Japonica Group (Q6ZJJ1), Oryza sativa Japonica Group (Q7XJ02), Oryza sativa Japonica Group (Q9FE01), Arabidopsis thaliana (Q05431), Arabidopsis thaliana (Q1PER6), Arabidopsis thaliana (Q42564), Arabidopsis thaliana (Q42592), Arabidopsis thaliana (Q42593), Arabidopsis thaliana (Q7XZP5), Arabidopsis thaliana (Q8GY91)
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