Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
evolution
-
in plants, OPRs belong to the old yellow enzyme family and form multigene families, phylogenetic analysis, structural evolution and functional divergence among OPR paralogues in plants, 6 major green plant lineages, overview
evolution
-
in plants, OPRs belong to the old yellow enzyme family and form multigene families, phylogenetic analysis, structural evolution and functional divergence among OPR paralogues in plants, 6 major green plant lineages, overview
evolution
-
in plants, OPRs belong to the old yellow enzyme family and form multigene families, phylogenetic analysis, structural evolution and functional divergence among OPR paralogues in plants, 6 major green plant lineages, overview
evolution
-
in plants, OPRs belong to the old yellow enzyme family and form multigene families, phylogenetic analysis, structural evolution and functional divergence among OPR paralogues in plants, 6 major green plant lineages, overview
evolution
-
in plants, OPRs belong to the old yellow enzyme family and form multigene families, phylogenetic analysis, structural evolution and functional divergence among OPR paralogues in plants, 6 major green plant lineages, overview
evolution
-
in plants, OPRs belong to the old yellow enzyme family and form multigene families, phylogenetic analysis, structural evolution and functional divergence among OPR paralogues in plants, 6 major green plant lineages, overview
evolution
-
in plants, OPRs belong to the old yellow enzyme family and form multigene families, phylogenetic analysis, structural evolution and functional divergence among OPR paralogues in plants, 6 major green plant lineages, overview
evolution
-
in plants, OPRs belong to the old yellow enzyme family and form multigene families, phylogenetic analysis, structural evolution and functional divergence among OPR paralogues in plants, 6 major green plant lineages, overview
evolution
-
in plants, OPRs belong to the old yellow enzyme family and form multigene families, phylogenetic analysis, structural evolution and functional divergence among OPR paralogues in plants, 6 major green plant lineages, overview
evolution
-
in plants, OPRs belong to the old yellow enzyme family and form multigene families, phylogenetic analysis, structural evolution and functional divergence among OPR paralogues in plants, 6 major green plant lineages, overview
evolution
in plants, OPRs belong to the old yellow enzyme family and form multigene families, phylogenetic analysis, structural evolution and functional divergence among OPR paralogues in plants, 6 major green plant lineages, overview
evolution
-
the TaOPR1 sequence retains the conserved residues that account for the NADPH- and FMN-binding sites of the OYE family
metabolism
-
enzyme TaOPR1 stimulated the abscisic acid-dependent stress-responsive pathway
metabolism
one of the key genes of the jasmonic acid biosynthesis pathway
physiological function
-
12-oxo-phytodienoic acid reductases are enzymes that catalyze the reduction of double-bonds in alpha,beta-unsaturated aldehydes or ketones and are part of the octadecanoid pathway that converts linolenic acid to jasmonic acid
physiological function
-
12-oxo-phytodienoic acid reductases are enzymes that catalyze the reduction of double-bonds in alpha,beta-unsaturated aldehydes or ketones and are part of the octadecanoid pathway that converts linolenic acid to jasmonic acid
physiological function
-
12-oxo-phytodienoic acid reductases are enzymes that catalyze the reduction of double-bonds in alpha,beta-unsaturated aldehydes or ketones and are part of the octadecanoid pathway that converts linolenic acid to jasmonic acid
physiological function
-
12-oxo-phytodienoic acid reductases are enzymes that catalyze the reduction of double-bonds in alpha,beta-unsaturated aldehydes or ketones and are part of the octadecanoid pathway that converts linolenic acid to jasmonic acid
physiological function
-
12-oxo-phytodienoic acid reductases are enzymes that catalyze the reduction of double-bonds in alpha,beta-unsaturated aldehydes or ketones and are part of the octadecanoid pathway that converts linolenic acid to jasmonic acid
physiological function
-
12-oxo-phytodienoic acid reductases are enzymes that catalyze the reduction of double-bonds in alpha,beta-unsaturated aldehydes or ketones and are part of the octadecanoid pathway that converts linolenic acid to jasmonic acid
physiological function
-
12-oxo-phytodienoic acid reductases are enzymes that catalyze the reduction of double-bonds in alpha,beta-unsaturated aldehydes or ketones and are part of the octadecanoid pathway that converts linolenic acid to jasmonic acid
physiological function
-
12-oxo-phytodienoic acid reductases are enzymes that catalyze the reduction of double-bonds in alpha,beta-unsaturated aldehydes or ketones and are part of the octadecanoid pathway that converts linolenic acid to jasmonic acid
physiological function
-
12-oxo-phytodienoic acid reductases are enzymes that catalyze the reduction of double-bonds in alpha,beta-unsaturated aldehydes or ketones and are part of the octadecanoid pathway that converts linolenic acid to jasmonic acid
physiological function
-
12-oxo-phytodienoic acid reductases are enzymes that catalyze the reduction of double-bonds in alpha,beta-unsaturated aldehydes or ketones and are part of the octadecanoid pathway that converts linolenic acid to jasmonic acid
physiological function
12-oxo-phytodienoic acid reductases are enzymes that catalyze the reduction of double-bonds in alpha,beta-unsaturated aldehydes or ketones and are part of the octadecanoid pathway that converts linolenic acid to jasmonic acid
physiological function
-
12-oxophytodienoate reductase (OPR) is a key enzyme in the biosynthesis of jasmonic acid (JA), which plays an important role in plant defense responses. Enzyme CsOPR3 plays an important role in jasmonate biosynthesis and tea plant defense against herbivorous insects
physiological function
-
enzyme TaOPR1 does not interact with jasmonate synthesis or the jasmonate signaling pathway. Rather than serving purely as an antioxidant, TaOPR1 acts during episodes of abiotic stress response as a signaling compound associated with the regulation of the abscisic acid-mediated signaling network. Overexpression of TaOPR1 in wheat significantly enhances the level of salinity tolerance, while its heterologous expression in Arabidopsis thaliana alleviates root growth restriction in the presence of salinity and oxidants and raises the sensitivity to abscisic acid. In Arabidopsis, recombinant TaOPR1 promotes abscisic acid synthesis. and the abscisic acid-dependent stress-responsive pathway. Recombinant TaOPR1 partially rescues the sensitivity of the Arabidopsis thaliana aba2 mutant defective in abscisic acid synthesis to salinity, and improves the activities of reactive oxygen species scavengers and the transcription of their encoding genes while reducing malondialdehyde and reactive oxygen species levels. TaOPR1 enhanced the salinity tolerance of wheat and in transgenic Arabidopsis thaliana. TaOPR1-overexpressing lines show insensitivity to H2O2
physiological function
transgenic wheat plants with high AtOPR3 expression levels are characterized by delayed germination, slower growth, late flowering and senescence, and improved tolerance to short-term freezing
physiological function
OPR3 is a bifunctional enzyme with NADPH-dependent alpha,beta-ketoalkene double-bond reductase and monodehydroascorbate reductase activities. OPR3 mutants show a slightly less-reduced ascorbate pool in leaves in line with the MDHAR activity of OPR3 in vitro. OPR3 catalyzes the reduction of a wide spectrum of electrophilic species that share a reactivity toward the glutathione and ascorbate. 12-oxophytodienoic acid reacts with ascorbate to form an ascorbate-12-oxophytodienoic acid adduct, but in addition OPR3 has the ability to regenerate ascorbate from monodehydroascorbate