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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 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
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
evolution
APX belongs to the class I heme-peroxidases, isozyme CreAPX1 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
evolution
APX belongs to the class I heme-peroxidases, isozyme CreAPX2 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 CreAPX4 belongs to group VI. 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 CreAPXheme belongs to group III. 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 OsAPX1 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 OsAPX2 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 OsAPX3 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 OsAPX4 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 OsAPX5 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
evolution
APX belongs to the class I heme-peroxidases, isozyme OsAPX6 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
evolution
APX belongs to the class I heme-peroxidases, isozyme OsAPX7 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
evolution
APX belongs to the class I heme-peroxidases, isozyme OsAPX8 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
evolution
APX belongs to the class I heme-peroxidases, isozyme PpAPX-S 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
evolution
APX belongs to the class I heme-peroxidases, isozyme PpAPX2.1 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 PpAPX2.2 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 PpAPX3 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 PpAPX6-related 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 PtAPX-S.1 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
evolution
APX belongs to the class I heme-peroxidases, isozyme PtAPX-S.2 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
evolution
APX belongs to the class I heme-peroxidases, isozyme PtAPX-TL29 belongs to group VII. 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 PtAPX.3 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 PtAPX1.1 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 PtAPX1.2 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 PtAPX2 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 PtAPX3 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 PtAPX5 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 PtAPX5-like 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 PtAPX6 related 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
ascorbate peroxidase (APX) is a class I heme peroxidase. Heme peroxidases catalyse the H2O2-dependent oxidation of a wide variety of substrates. The family of heme peroxidases share a common mechanism of oxidation which involves the formation of high-valent Compound I and Compound II intermediates. Ascorbate peroxidase and manganese peroxidase bind some substrates at the gamma-heme edge, others at the delta-heme edge
evolution
Euglena gracilis contains a photosynthesis-specific APX shared with other phototrophic euglenophytes, along with a putative plastidial APX acquired from and limited to Chloroplastida. Moreover, both diplonemids and euglenids encode a novel clade of peroxidases with a yet unknown function, while most kinetoplastids share a unique hAPX-CCP enzyme exhibiting both the APX and cytochrome c peroxidases (CCP) activities
evolution
gene MaAPX1 has a high homology (83.9%) with Arabidopsis thaliana gene APX1
evolution
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sequence comparison, phylogenetic analysis and tree
evolution
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the complex phylogenetic pattern, diversity, and distribution of catalase and APX in euglenozoans testify to their importance for these protists. The distribution of APX and catalase (CAT) in diplonemids is best explained by a scenario, in which the predecessor of these marine protists lacked both enzymes, which were reacquired by horizontal gene transfer from either prokaryotic or eukaryotic sources. Moreover, both diplonemids and euglenids encode a novel clade of peroxidases with a yet unknown function, while most kinetoplastids share a unique hAPX-CCP enzyme exhibiting both the APX and cytochrome c peroxidases (CCP) activities
evolution
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the complex phylogenetic pattern, diversity, and distribution of catalase and APX in euglenozoans testify to their importance for these protists. The distribution of APX and catalase (CAT) in diplonemids is best explained by a scenario, in which the predecessor of these marine protists lacked both enzymes, which were reacquired by horizontal gene transfer from either prokaryotic or eukaryotic sources. Moreover, both diplonemids and euglenids encode a novel clade of peroxidases with a yet unknown function, while most kinetoplastids share a unique hAPX-CCP enzyme exhibiting both the APX and cytochrome c peroxidases (CCP) activities
evolution
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the complex phylogenetic pattern, diversity, and distribution of catalase and APX in euglenozoans testify to their importance for these protists. The distribution of APX and catalase (CAT) in diplonemids is best explained by a scenario, in which the predecessor of these marine protists lacked both enzymes, which were reacquired by horizontal gene transfer from either prokaryotic or eukaryotic sources. Moreover, both diplonemids and euglenids encode a novel clade of peroxidases with a yet unknown function, while most kinetoplastids share a unique hAPX-CCP enzyme exhibiting both the APX and cytochrome c peroxidases (CCP) activities
malfunction
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CrAPX4 knockdown amiRNA lines show low APX activity and CrAPX4 transcript level without a change in CrAPX1 and CrAPX2 transcript levels, and monodehydroascorbate reductase (MDAR), dehydroascorbate reductase (DHAR), and glutathione reductase (GR) activities and transcript levels. Upon exposure to high-light (HL), CrAPX4 knockdown amiRNA lines show a modification in the expression of genes encoding the enzymes in the ascorbate-glutathione cycle, including an increase in transcript level of CrVTC2, a key enzyme for ascorbate (AsA) biosynthesis but a decrease in MDAR and DHAR transcription and activity after 1 h, followed by increases in reactive oxygen species production and lipid peroxidation after 6 h, and exhibit cell death after 9 h. Besides, AsA content and AsA/DHA (dehydroascorbate) ratio decrease in CrAPX4 knockdown amiRNA lines after prolonged HL treatment
malfunction
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downregulation of cytosolic ascorbate peroxidases inhibits the development of sink organs in cotton. Downregulated expression of cAPXs inhibits the development of cotton bolls, fibers, and seeds and reduces the storage capacity of the sink organs. The photosynthetic rate is suppressed in the knockout mutant plants, and the reactive oxygen species level is increased in guard cells. Overexpression of GhAPX1 has little effect on the photosynthetic characteristics of the plants. The decrease of cAPX expression in leaves increases ROS level in stomatal guard cells, leading to the decrease of stomatal aperture, which might decrease the supply of carbon dioxide and water used for photosynthesis. The downregulation of cytosolic ascorbate peroxidases (APXs) decreases the water content and increases the water loss rate in cotton leaf. There is a close relationship between the stomatal opening and the inhibition of plant growth caused by the deficiency of antioxidant enzyme in cells
malfunction
ectopic recombinant overexpression of MaAPX1 delays the detached leaf senescence induced by darkness in Arabidopsis thaliana
malfunction
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light-induced chloroplast development is enhanced in PtotAPX-overexpressing transgenic Populus tomentosa callus with lower levels of hydrogen peroxide, but is suppressed in PtotAPX antisense transgenic callus with higher levels of hydrogen peroxide
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
metabolism
cytosolic ascorbate peroxidase is S-nitrosylated at the onset of programmed cell death, induced by both heat shock or hydrogen peroxide. S-nitrosylation of Apx is responsible for the rapid decrease in its activity, and the decrease in activity is a precocious event in the programmed cell death signaling pathway, occurring when no cellular death hallmarks are evident
metabolism
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chloroplasts with elaborate thylakoids can develop from proplastids in the cells of calli derived from leaf tissues of Populus tomentosa upon exposure to light. Chloroplast development is confirmed at the molecular and cellular levels and transcriptome analysis reveals that genes related to photoreceptors and photosynthesis are significantly upregulated during chloroplast development in a time-dependent manner. In light-induced chloroplast development, a key process is the removal of hydrogen peroxide, in which thylakoid-localized PtotAPX plays a major role
metabolism
enzyme ascorbate peroxidase 1 (CsAPX1) is involved in ascorbic acid (AsA) metabolism
metabolism
methionine sulfoxide reductase B regulates the activity of ascorbate peroxidase of banana fruit, proposed model of the involvement of MaMsrB2-mediated redox modification of methionine in MaAPX1 in regulating ripening and senescence, overview
metabolism
Simulated acid rain (SAR)stress (pH 3.5/2.5) destroys the redox state in rice cells and induces H2O2 excessive accumulation, and inhibits growth of rice. Exogenous Ca2+ alleviates SAR-induced inhibition on activities of APX and GR by regulating the concentration, activation, and transcription of their isozymes, and then maintains the redox level of cells and protects cells from oxidative damage, being beneficial to the growth of rice, effect of Ca2+ on contents of AsA and DHA in leaves and roots of rice under the simulated acid rain stress, overview
physiological function
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APX is physiologically important to the metabolism of H2O2
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
constitutive overexpression of APx in an amphotericin B-resistant strain prevents cells from the deleterious effect of oxidative stress, i.e., mitochondrial dysfunction and cellular death induced by amphotericin B
physiological function
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heterologous overexpression of Apx6 increases the survival rate and reduces leaf water loss rate in Arabidopsis thaliana under drought treatment. Compared to the wild type plants, high salinity treatment reduces the concentrations of malondialdehyde, H2O2 and proline but elevates the activities of Apx, glutathione peroxidase, catalase and superoxide dismutases in the Apx6-overexpressing plants. Germination rate, cotyledon greening, and root length are improved in the transgenic under salt and water deficit conditions
physiological function
isoform Apx1-overexpressing Arabidopsis thaliana lines show increased germination rate and root length compared with wild-type under 200 mM NaCl stress treatment. Transgeneic lines display higher chlorophyll content, relative water content, total Apx activity, proline content, and lower H2O2 accumulation
physiological function
loss of Apx2 function affects the growth and development of rice seedlings, resulting in semi-dwarf seedlings, yellow-green leaves, leaf lesion mimic and seed sterility. Apx2 mutants have lower Apx activity and are sensitive to abiotic stresses. Overexpression of Apx2 increases activity and enhances stress tolerance. H2O2 and malondialdehyde levels are high in Apx2 mutants but low in overexpressing transgenic lines relative to wild-type plants after stress treatments
physiological function
overexpressing strains are significantly more infective to macrophages and cardiomyocytes, as well as in the mouse model of Chagas disease than wild-type
physiological function
transgenic tobacco plants overexpressing Apx show no significant difference in morphology under normal conditions. The transgenic plants are more resistant to drought, salt and oxidative stress conditions and show decreased H2O2 levels, increased ascorbate consumption, an increase in the NADP to NADPH ratio, and higher Apx activity
physiological function
under 150-mM NaCl stress, compared with wild-type, the overexpression of Apx in Arabidopsis increases the germination rate, the number of leaves and the rosette area. The transgenic plants have longer roots, higher total chlorophyll content, higher total Apx activity, and lower H2O2 content
physiological function
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ascorbate peroxidase (APS) is an important antoxidant enzyme responsible for the conversion of H2O2 to H2O and O2. Role of APX in the tolerance of the boreal cushion moss Dicranum scoparium to abiotic stress
physiological function
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ascorbate peroxidase (APX) is the key enzyme in hydrogen peroxide degradation, and may have a critical function in plant-aphid interactions. The enzyme has an essential function in the scavenging of H2O2 produced in normal metabolic conditions or under environmental stress due to drought
physiological function
ascorbate peroxidase 1 regulates ascorbic acid metabolism in fresh-cut leaves of tea plant during postharvest storage under light/dark conditions. CsAPX1 is involved in regulating AsA metabolism through effecting on the changes of AsA accumulation and APX activity in the leaves
physiological function
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chloroplast development is a complex process that is critical to the growth and development of plants, overview. Chloroplast thylakoid ascorbate peroxidase PtotAPX plays a key role in chloroplast development from proplastids upon exposure to light in Populus tomentosa and in thylakoid development by decreasing hydrogen peroxide
physiological function
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cytosolic ascorbate peroxidases (APXs) are hydrogen peroxide (H2O2) scavenging enzymes in plants. H2O2 is a signaling molecule involved in regulating photosynthesis in plants. Cytosolic ascorbate peroxidase members provide an important guarantee to maintain photosynthetic rate
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
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Euglenozoa recruit APXs as detoxifying enzymes for specific molecular tasks, such as photosynthesis in euglenids and membrane-bound peroxidase activity in kinetoplastids and some diplonemids
physiological function
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Euglenozoa recruit APXs as detoxifying enzymes for specific molecular tasks, such as photosynthesis in euglenids and membrane-bound peroxidase activity in kinetoplastids and some diplonemids. The diplonemid Rhynchopus humris shows very low APX activity despite the fact that the species apparently lacks the corresponding gene. The kinetic parameters of catalase (CAT) suggest yet another explanation for the lack of measurable activity in Rhynchopus humris. The low affinity of CAT to H2O2 implies that it is responsible for the removal of excessive ROS when their concentration is high, while high-affinity APX modulates low concentration of ROS, necessary for cell signaling
physiological function
Blastochritidia sp. P57
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Euglenozoa recruit APXs as detoxifying enzymes for specific molecular tasks, such as photosynthesis in euglenids and membrane-bound peroxidase activity in kinetoplastids and some diplonemids. The kinetoplastid Blastochritidia sp. P57 shows very low APX activity despite the fact that the species apparently lacks the corresponding gene. The kinetic parameters of catalase (CAT) suggest yet another explanation for the lack of measurable activity in Blastocrithidia sp. P57. The low affinity of CAT to H2O2 implies that it is responsible for the removal of excessive ROS when their concentration is high, while high-affinity APX modulates low concentration of ROS, necessary for cell signaling
physiological function
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Euglenozoa recruit APXs as detoxifying enzymes for specific molecular tasks, such as photosynthesis in euglenids and membrane-bound peroxidase activity in kinetoplastids and some diplonemids. The respiration rate does not correlate with APX activity
physiological function
Euglenozoa recruit APXs as detoxifying enzymes for specific molecular tasks, such as photosynthesis in euglenids and membrane-bound peroxidase activity in kinetoplastids and some diplonemids. The respiration rate does not correlate with APX activity
physiological function
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Euglenozoa recruit APXs as detoxifying enzymes for specific molecular tasks, such as photosynthesis in euglenids and membrane-bound peroxidase activity in kinetoplastids and some diplonemids. The respiration rate does not correlate with APX activity
physiological function
exogenous calcium enhances rice tolerance to acid rain stress by regulating isozymes composition and transcriptional expression of ascorbate peroxidase and glutathione reductase
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
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
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
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
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
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isozyme CrAPX4 induction together with its association with the modulation of MDAR and DHAR expression for AsA regeneration is critical for Chlamydomonas to cope with photooxidative stress. APX is a central enzyme for ROS scavenging in plants can be induced under abiotic and biotic stresses
physiological function
MaAPX1 interacts with methionine sulfoxide reductase B2 (MsrB2) in bananas. Enzyme MaAPX1 might be a target of MaMsrB2 by Co-IP and mass spectrum techniques in banana fruit. The redox state of methionine in MaAPX1 is critical to its activity, and MaMsrB2 can regulate the redox state and activity of MaAPX1. Among the antioxidant enzymes, APX plays a crucial role in scavenging H2O2 by catalyzing the conversion of H2O2 to H2O and O2, using ascorbic acid as the electron donor. APX has a higher affinity than does catalase for H2O2 and contributes maximally to H2O2 detoxification in chloroplasts, cytosol, mitochondria, and peroxisomes, as well as in the apoplastic space. APX is involved in the physiological and developmental response, such as seed germination, leaf senescence, and programmed cell death. APX also participates in environmental stresses in plants, including drought, salt, chilling, photo-oxidative stress, and high temperature. MaAPX 1 might be involved in ripening and senescence in relation to oxidative stress
physiological function
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recombinant overexpression of celery enzyme AgAPX1 in Arabidopsis thaliana positively regulates drought tolerance by regulating the stomata aperture, physiological changes in Arabidopsis leaves exposed to drought stress, phenotype, overview. The AgAPX1 gene seems to be involved in the response of celery to drought stress. The response of the AgAPX1 gene to adversity may be attributed to the conservation of APX sequences among different species
physiological function
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role of Musa paradisiaca ascorbate peroxidase in the transformation of methyl phenyl sulfide to its sulfoxide
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 peroxidase (APX) derived from Cyanidioschyzon merolae, a primitive red alga living in high temperature and acidic environments (42°C, pH 2.5), has greater anti-oxidative capacity than similar peroxidases occurring in other plants. Cyanidioschyzon merolae-derived APX (cAPX) expressed in mammalian cells increases cellular antioxidative capacity. Heat and H2O2 stimulation results in ROS production. cAPX-expressing cells are more tolerant to oxidative stress induced by heat, H2O2, and acid stimulations than control cells lacking cAPX
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
physiological function
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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
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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
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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, and three-dimensional modeling using the enzyme structure (PDB ID 1apx), 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, and three-dimensional modeling using the enzyme structure (PDB ID 1apx), 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, and three-dimensional modeling using the enzyme structure (PDB ID 1apx), 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, and three-dimensional modeling using the enzyme structure (PDB ID 1apx), 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, and three-dimensional modeling using the enzyme structure (PDB ID 1apx), 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, and three-dimensional modeling using the enzyme structure (PDB ID 1apx), 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, and three-dimensional modeling using the enzyme structure (PDB ID 1apx), 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, and three-dimensional modeling using the enzyme structure (PDB ID 1apx), 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, and three-dimensional modeling using the enzyme structure (PDB ID 1iyn), 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, and three-dimensional modeling using the enzyme structure (PDB ID 1iyn), 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, and three-dimensional modeling using the enzyme structure (PDB ID 1iyn), 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, and three-dimensional modeling using the enzyme structure (PDB ID 1iyn), 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, and three-dimensional modeling using the enzyme structure (PDB ID 1iyn), 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, and three-dimensional modeling using the enzyme structure (PDB ID 1iyn), 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, and three-dimensional modeling using the enzyme structure (PDB ID 1iyn), 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, and three-dimensional modeling using the enzyme structure (PDB ID 1iyn), 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, and three-dimensional modeling using the enzyme structure (PDB ID 5jqr), 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, and three-dimensional modeling using the enzyme structure (PDB ID 5jqr), 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, and three-dimensional modeling using the enzyme structure (PDB ID 5jqr), 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, and three-dimensional modeling using the enzyme structure (PDB ID 5jqr), 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, and three-dimensional modeling using the enzyme structure (PDB ID 5jqr), 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, and three-dimensional modeling using the enzyme structure (PDB ID 5jqr), 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, and three-dimensional modeling using the enzyme structure (PDB ID 5jqr), 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, and three-dimensional modeling using the enzyme structure (PDB ID 5jqr), overview
additional information
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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
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
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
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
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possible substrate binding sites include His42, His162 and Asp20, substrate docking study
additional information
the coding sequence of APX6 is a potential target of miR398, which is a key regulator of copper redistribution
additional information
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the enzyme contains a H2O2 binding domain, the critical residues that coordinate binding of H2O2 by APX are R158,W161, and H162(numbering according to the chloroplastic ascorbate peroxidase from tobacco plants)
additional information
the enzyme contains a H2O2 binding domain, the critical residues that coordinate binding of H2O2 by APX are R158,W161, and H162(numbering according to the chloroplastic ascorbate peroxidase from tobacco plants)
additional information
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the enzyme contains a H2O2 binding domain, the critical residues that coordinate binding of H2O2 by APX are R158,W161, and H162(numbering according to the chloroplastic ascorbate peroxidase from tobacco plants)
additional information
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the enzyme contains a H2O2 binding domain, the critical residues that coordinate binding of H2O2 by APX are R158,W161, and H162(numbering according to the chloroplastic ascorbate peroxidase from tobacco plants). Enzyme domain structure, overview
additional information
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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
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