Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:1.6.5.4 (SOR)
 720 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The importance of redox-regulation in Arabidopsis thaliana roots has been investigated through the identification of the proteins interacting with thioredoxin (TRX), an ubiquitous thiol-disulfide reductase. We have applied a proteomic approach based on affinity chromatography on a monocysteinic mutant of plastidial y-type TRX used as a bait to trap putative partners in a crude extract of root proteins. Seventy-two proteins have been identified, functioning mainly in metabolism, detoxification and response to stress, protein processing and signal transduction. This study allowed us to isolate 24 putative new targets and to propose the mevalonic acid-dependent biosynthesis of isoprenoids as a new redox-mediated process. The redox-regulation of phenylpropanoid biosynthesis is also suggested, three enzymes of this pathway being retained on the column. We also provided experimental evidence that phenylammonia-lyase was enzymatically more active when reduced by TRXy in root crude extract. Among the high number of partners involved in defense against stress we isolated from the column, we focused on plastidial monodehydroascorbate reductase and showed that its activity was dramatically increased in vitro in the presence of DTT-reduced TRXy1 in root crude extracts. Our data strongly suggest that TRXy1 could be the physiological regulator of monodehydroascorbate reductase in root plastids.
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PMID:Thioredoxin targets in Arabidopsis roots. 2040 73

In recent years, nitric oxide (NO) has been considered a plant signaling compound involved in antioxidant systems and flavonoid production enhancement. Nevertheless, its mechanism of action, from the perspective of protein expression, remains largely unknown. In this study, isobaric tags for relative and absolute quantitation (iTRAQ) was employed to investigate NO donor sodium nitroprusside treatment-induced proteomic changes in soybean sprouts. Among the 3033 proteins identified, compared with the control, sodium nitroprusside treatment up- and down-regulated 256 proteins. These proteins were involved in antioxidant system pathways, such as the thioredoxin, superoxide dismutase (SOD), peroxidase (POD), catalase (CAT), glutathione reductase (GR), glutathione S-transferase (GST), ascorbate peroxidase (APX), monodehydroascorbate reductase (MDAR) and lipoxygenase (LOX) pathways, including allene oxide synthase and lipoxygenase. In addition, heat shock proteins (HSPs) and flavonoid biosynthetic proteins, such as cinnamate 4-hydroxylase, chalcone isomerase, chalcone synthase, isoflavone synthase and isoflavone reductase, were also modulated in response to sodium nitroprusside treatment.
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PMID:iTRAQ-based proteomic analysis reveals changes in response to sodium nitroprusside treatment in soybean sprouts. 3105 89