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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
enzyme activity of ascorbate peroxidase (APX), for 2 varieties, Suakoko8 and IR31785, in samples of the leaf blade, the sheath of the youngest fully developed leaf of the main culm, the blade and sheath of the third youngest fully developed leaf of the main culm, and the root, samples are fresh or stored for 1-12 weeks frozen, or freeze-dried, overview
of seedlings. NaCl-enhanced expression of OsAPx8 in rice roots is mediated through an accumulation of abscisic acid. Na+ but not Cl- is required for enhancing OsAPx8 expression. H2O2 is not involved in the regulation of NaCl-induced OsAPx8 expression in rice roots
root of seedling, increase in enzyme activity after treatment with NaCl or H2O2, inhibition of enzyme accumulation by diphenyleneiodinium chloride or imidazole, but not by dimethylthiourea
root. NaCl-enhanced expression of OsAPx8 in rice roots is mediated through an accumulation of abscisic acid. Na+ but not Cl- is required for enhancing OsAPx8 expression. H2O2 is not involved in the regulation of NaCl-induced OsAPx8 expression in rice roots
PEG 6000, 40% in assay medium, 50% inhibition of aPX 1, 65% inhibition of APX 2 with increase in enzyme Km values, incorporation of 1 M proline, glycine betaine or sucrose in presence of PEG in the assay medium restores
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
effect of dfferent storage methods such as freeze-drying, freezing at -20°C, and freezing at -80°C on the activity of enzyme ascorbate peroxidase from two rice varieties, overview. When subjected to different storage methods, there are no differences between varieties, but strong effects of the different storage methods on enzyme activities are found strongly differing between extracts from stored tissue samples or extracts stored from freshly sampled material. Enzyme-specific storage methods and durations allow for expanding the window for analyses in large experimental studies involving destructive samplings for enzyme kinetics
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Arabidopsis. Transgenic lines over-expressing OsAPXb showed higher salt tolerance than OsAPXa transgenic lines. Overproduction of OsAPXb enhances and maintains APX activity to a much higher degree than OsAPXa in transgenic Arabidopsis during treatment with different concentrations of NaCl, enhances the active oxygen scavenging system, and protects plants from salt stress by equilibrating H2O2 metabolism
overexpression in Arabidopsis. Transgenic lines over-expressing OsAPXb show higher salt tolerance than OsAPXa transgenic lines. Overproduction of OsAPXb enhances and maintains APX activity to a much higher degree than OsAPXa in transgenic Arabidopsis during treatment with different concentrations of NaCl, enhances the active oxygen scavenging system, and protects plants from salt stress by equilibrating H2O2 metabolism
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
salt stress, Na+ induces expression of OsAPx8, , NaCl-enhanced expression of OsAPx8 in rice roots is mediated through an accumulation of the plant hormone ABA
Extraction, storage duration, and storage temperature affect the activity of ascorbate peroxidase, glutathione reductase, and superoxide dismutase in rice tissue