Protein Variants | Comment | Organism |
---|---|---|
additional information | construction of GSNOR knockout plants that exhibit overall reductions in growth where root development, thought to be directly linked to redox activity. The GSNOR knockout mutant contains a pre-induced antioxidant protection system | Solanum lycopersicum |
additional information | construction of GSNOR knockout plants that exhibit overall reductions in growth where root development, thought to be directly linked to redox activity. The GSNOR knockout mutant contains a pre-induced antioxidant protection system | Arabidopsis thaliana |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | strong oxidizing agents are capable of reducing Arabidopsis thaliana GSNOR activity. Plant systems reversibly inhibit their GSNOR activity in response to oxidative radicals | Arabidopsis thaliana | |
additional information | plant systems reversibly inhibit their GSNOR activity in response to oxidative radicals | Solanum lycopersicum | |
NO | GSNOR1 activity decreases in response to NO donors | Arabidopsis thaliana | |
NO | - |
Solanum lycopersicum |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
cytosol | - |
Solanum lycopersicum | 5829 | - |
cytosol | - |
Arabidopsis thaliana | 5829 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | required | Arabidopsis thaliana | |
Zn2+ | required, Solanum lycopersicum SlGSNOR structure in coordination with NAD+, the active sites on the homodimer coordinate the zinc ion, a possible point of regulation in the presence of oxidative species | Solanum lycopersicum |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
S-nitrosoglutathione + NADPH + H+ | Solanum lycopersicum | - |
GSSG + ammonia + NADP+ | - |
ir | |
S-nitrosoglutathione + NADPH + H+ | Arabidopsis thaliana | - |
GSSG + ammonia + NADP+ | - |
ir |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Arabidopsis thaliana | F4K7D6 | - |
- |
Solanum lycopersicum | D2Y3F4 | - |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
additional information | GSNOR is thought to be localized in the phloem and xylem parenchyma cells of the vasculature | Solanum lycopersicum | - |
additional information | GSNOR is thought to be localized in the phloem and xylem parenchyma cells of the vasculature | Arabidopsis thaliana | - |
parenchyma | - |
Solanum lycopersicum | - |
parenchyma | - |
Arabidopsis thaliana | - |
phloem | - |
Solanum lycopersicum | - |
phloem | - |
Arabidopsis thaliana | - |
root | - |
Solanum lycopersicum | - |
root | - |
Arabidopsis thaliana | - |
root hair | - |
Solanum lycopersicum | - |
root hair | - |
Arabidopsis thaliana | - |
xylem | - |
Solanum lycopersicum | - |
xylem | - |
Arabidopsis thaliana | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
S-nitrosoglutathione + NADPH + H+ | - |
Solanum lycopersicum | GSSG + ammonia + NADP+ | - |
ir | |
S-nitrosoglutathione + NADPH + H+ | - |
Arabidopsis thaliana | GSSG + ammonia + NADP+ | - |
ir |
Synonyms | Comment | Organism |
---|---|---|
GSNOR | - |
Solanum lycopersicum |
GSNOR | - |
Arabidopsis thaliana |
S-nitrosoglutathione reductase | - |
Solanum lycopersicum |
S-nitrosoglutathione reductase | - |
Arabidopsis thaliana |
SlGSNOR | - |
Solanum lycopersicum |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADP+ | - |
Solanum lycopersicum | |
NADP+ | - |
Arabidopsis thaliana | |
NADPH | - |
Solanum lycopersicum | |
NADPH | - |
Arabidopsis thaliana |
Organism | Comment | Expression |
---|---|---|
Solanum lycopersicum | response to highly nitrosative and oxidative conditions its activity is often downregulated, possibly through an S-nitrosation site on GSNOR at Cys271 | down |
Arabidopsis thaliana | response to highly nitrosative and oxidative conditions its activity is often downregulated, possibly through an S-nitrosation site on GSNOR at Cys271 | down |
Solanum lycopersicum | GSNOR is thought to be upregulated under iron deficient conditions. Fe-deficiency leads to NO, GSNO, and GSH decrease leading to changes in growth probably regulated by GSNOR localized in the phloem | up |
Arabidopsis thaliana | GSNOR is thought to be upregulated under iron deficient conditions. Fe-deficiency leads to NO, GSNO, and GSH decrease leading to changes in growth probably regulated by GSNOR localized in the phloem | up |
General Information | Comment | Organism |
---|---|---|
evolution | S-nitrosoglutathione reductase (GSNOR) is highly conserved enzyme amongst eukaryotes and prokaryotes. It is a member of the class III alcohol dehydrogenase family | Solanum lycopersicum |
evolution | S-nitrosoglutathione reductase (GSNOR) is highly conserved enzyme amongst eukaryotes and prokaryotes. It is a member of the class III alcohol dehydrogenase family | Arabidopsis thaliana |
malfunction | GSNOR knockout mutated plants often display a stunted growth phenotype in all structures, and exhibit a pre-induced protective effect against oxidative stressors, as well as an improved immune response associated with NO accumulation in roots. GSNOR knockout strains display reduced primary root growth under high iron conditions, but relatively no change is observed in wild-type seedlings. Plant systems reversibly inhibit their GSNOR activity in response to oxidative radicals | Arabidopsis thaliana |
malfunction | GSNOR knockout mutated plants often display a stunted growth phenotype in all structures, and exhibit a pre-induced protective effect against oxidative stressors, as well as an improved immune response associated with NO accumulation in roots. The action of increasing NO levels and GSNOR1 inhibition is often coupled with increased ROSs associated with plant immune response. Plant systems reversibly inhibit their GSNOR activity in response to oxidative radicals | Solanum lycopersicum |
metabolism | along with its more stable NO donor, S-nitroso-glutathione (GSNO), formed by NO non-enzymatically in the presence of glutathione (GSH), NO is a redox-active molecule capable of mediating target protein cysteine thiols through the post translational modification, S-nitrosation. S-nitroso-glutathione reductase (GSNOR) thereby acts as a mediator to pathways regulated by NO due to its activity in the irreversible reduction of GSNO to oxidized glutathione (GSSG) and ammonia. GSNOR is thought to be pleiotropic and often acts by mediating the cellular environment in response to stress conditions. Under optimal conditions its activity leads to growth by transcriptional upregulation of the nitrate transporter, NRT2.1, and through its interaction with phytohormones like auxin and strigolactones associated with root development. GSNOR is required in times of iron toxicity. Mechanism for control of the nitrogen assimilation pathway. GSNOR activity is thought to increase NRT2.1 and nitrate reductase (NR) function thereby leading to eventual increases in NO levels, which are ultimately thought to have an inhibitory effect on GSNOR | Solanum lycopersicum |
metabolism | along with its more stable NO donor, S-nitroso-glutathione (GSNO), formed by NO non-enzymatically in the presence of glutathione (GSH), NO is a redox-active molecule capable of mediating target protein cysteine thiols through the post translational modification, S-nitrosation. S-nitroso-glutathione reductase (GSNOR) thereby acts as a mediator to pathways regulated by NO due to its activity in the irreversible reduction of GSNO to oxidized glutathione (GSSG) and ammonia. GSNOR is thought to be pleiotropic and often acts by mediating the cellular environment in response to stress conditions. Under optimal conditions its activity leads to growth by transcriptional upregulation of the nitrate transporter, NRT2.1, and through its interaction with phytohormones like auxin and strigolactones associated with root development. GSNOR is required in times of iron toxicity. Mechanism for control of the nitrogen assimilation pathway. GSNOR activity is thought to increase NRT2.1 and nitrate reductase (NR) function thereby leading to eventual increases in NO levels, which are ultimately thought to have an inhibitory effect on GSNOR | Arabidopsis thaliana |
additional information | Solanum lycopersicum SlGSNOR structure in coordination with NAD+, the active sites on the homodimer coordinate the zinc ion, a possible point of regulation in the presence of oxidative species | Solanum lycopersicum |
physiological function | S-nitrosoglutathione reductase (GSNOR) is capable of the NADH-dependent reduction of GSNO to glutathione disulfide (GSSG), the oxidized form of GSH, and ammonium (NH3). It has been originally identified in plants as a glutathione-dependent formaldehyde dehydrogenase (FALDH), and a member of the class III alcohol dehydrogenase family, where the primary substrate is hemithioacetal S-hydroxymethylglutathione (HMGSH), which is formed in an oxidizing environment through the favorable reaction of formaldehyde and GSH, using a catalytic zinc, and in the presence of the coenzyme NAD+. The redox-active enzyme acts in the homeostasis of S-nitrosothiols (SNOs) and is capable of regulating many cellular processes in that manner. Role of GSNOR in root development, overview. Although it is expressed within many plant tissues, GSNOR is thought to be localized in the phloem and xylem parenchyma cells of the vasculature, capable of regulating NO levels throughout the plant. GSNOR activity is related to NO production. Auxin is an important hormone capable of mediating cellular growth in concert with GSNOR. Auxin signalling is specifically relevant when considering the growth of root structures in response to GSNO levels, where a mechanism has been identified to regulate TIR1, a nuclear F-box protein and the auxin receptor. At increased GSNO levels, and thereby reduced GSNOR activity, S-nitrosation of TIR1 receptor is thought to increase its affinity for auxin and in turn increase transcription of target proteins. GSNOR may play a role in controlling strigolactones (SL) induced primary root elongation | Arabidopsis thaliana |
physiological function | S-nitrosoglutathione reductase (GSNOR) is capable of the NADH-dependent reduction of GSNO to glutathione disulfide (GSSG), the oxidized form of GSH, and ammonium (NH3). It has been originally identified in plants as a glutathione-dependent formaldehyde dehydrogenase (FALDH), and a member of the class III alcohol dehydrogenase family, where the primary substrate is hemithioacetal S-hydroxymethylglutathione (HMGSH), which is formed in an oxidizing environment through the favorable reaction of formaldehyde and GSH, using a catalytic zinc, and in the presence of the coenzyme NAD+. The redox-active enzyme acts in the homeostasis of S-nitrosothiols (SNOs) and is capable of regulating many cellular processes in that manner. Role of GSNOR in root development, overview. Although it is expressed within many plant tissues, GSNOR is thought to be localized in the phloem and xylem parenchyma cells of the vasculature, capable of regulating NO levels throughout the plant. GSNOR activity is related to NO production. Auxin is an important hormone capable of mediating cellular growth in concert with GSNOR. Auxin signalling is specifically relevant when considering the growth of root structures in response to GSNO levels, where a mechanism has been identified to regulate TIR1, a nuclear F-box protein and the auxin receptor. At increased GSNO levels, and thereby reduced GSNOR activity, S-nitrosation of TIR1 receptor is thought to increase its ax0enity for auxin and in turn increase transcription of target proteins. GSNOR may play a role in controlling strigolactones (SL) induced primary root elongation | Solanum lycopersicum |