Cloned (Comment) | Organism |
---|---|
gene GSNOR, sequence comparisons | Arabidopsis thaliana |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between reactive oxygen species (ROS)- and reactive nitrogen species (RNS)-signaling | Arabidopsis thaliana | |
additional information | oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between reactive oxygen species (ROS)- and reactive nitrogen species (RNS)-signaling | Brassica juncea | |
additional information | oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between reactive oxygen species (ROS)- and reactive nitrogen species (RNS)-signaling | Camelina sativa | |
additional information | oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between reactive oxygen species (ROS)- and reactive nitrogen species (RNS)-signaling | Capsella rubella | |
additional information | oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between reactive oxygen species (ROS)- and reactive nitrogen species (RNS)-signaling | Chlamydomonas reinhardtii | |
additional information | oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between reactive oxygen species (ROS)- and reactive nitrogen species (RNS)-signaling | Helianthus annuus | |
additional information | oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between reactive oxygen species (ROS)- and reactive nitrogen species (RNS)-signaling | Lactuca sativa | |
additional information | oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between reactive oxygen species (ROS)- and reactive nitrogen species (RNS)-signaling | Medicago truncatula | |
additional information | oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between reactive oxygen species (ROS)- and reactive nitrogen species (RNS)-signaling | Nicotiana sylvestris | |
additional information | oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between reactive oxygen species (ROS)- and reactive nitrogen species (RNS)-signaling | Noccaea caerulescens | |
additional information | oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between reactive oxygen species (ROS)- and reactive nitrogen species (RNS)-signaling | Oryza sativa Indica Group | |
additional information | oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between reactive oxygen species (ROS)- and reactive nitrogen species (RNS)-signaling | Pisum sativum | |
additional information | oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between reactive oxygen species (ROS)- and reactive nitrogen species (RNS)-signaling | Populus trichocarpa | |
additional information | oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between reactive oxygen species (ROS)- and reactive nitrogen species (RNS)-signaling | Ricinus communis | |
additional information | oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between reactive oxygen species (ROS)- and reactive nitrogen species (RNS)-signaling | Solanum lycopersicum | |
additional information | oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between reactive oxygen species (ROS)- and reactive nitrogen species (RNS)-signaling | Volvox carteri f. nagariensis | |
additional information | oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between reactive oxygen species (ROS)- and reactive nitrogen species (RNS)-signaling | Zea mays | |
peroxynitrite | treatment of AtGSNOR with peroxynitrite, known as tyrosine nitrating agent, modifies this enzyme and inhibits its activity | Arabidopsis thaliana |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
chloroplast | - |
Pisum sativum | 9507 | - |
cytosol | - |
Helianthus annuus | 5829 | - |
cytosol | - |
Arabidopsis thaliana | 5829 | - |
cytosol | - |
Pisum sativum | 5829 | - |
mitochondrion | - |
Pisum sativum | 5739 | - |
nucleus | - |
Helianthus annuus | 5634 | - |
nucleus | - |
Arabidopsis thaliana | 5634 | - |
nucleus | - |
Pisum sativum | 5634 | - |
peroxisome | - |
Pisum sativum | 5777 | - |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Zn2+ | the enzyme is a homodimer coordinating two zinc atoms per subunit | Camelina sativa | |
Zn2+ | the enzyme is a homodimer coordinating two zinc atoms per subunit | Solanum lycopersicum | |
Zn2+ | the enzyme is a homodimer coordinating two zinc atoms per subunit | Lactuca sativa | |
Zn2+ | the enzyme is a homodimer coordinating two zinc atoms per subunit | Helianthus annuus | |
Zn2+ | the enzyme is a homodimer coordinating two zinc atoms per subunit | Arabidopsis thaliana | |
Zn2+ | the enzyme is a homodimer coordinating two zinc atoms per subunit | Pisum sativum | |
Zn2+ | the enzyme is a homodimer coordinating two zinc atoms per subunit | Capsella rubella | |
Zn2+ | the enzyme is a homodimer coordinating two zinc atoms per subunit | Noccaea caerulescens | |
Zn2+ | the enzyme is a homodimer coordinating two zinc atoms per subunit | Brassica juncea | |
Zn2+ | the enzyme is a homodimer coordinating two zinc atoms per subunit | Nicotiana sylvestris | |
Zn2+ | the enzyme is a homodimer coordinating two zinc atoms per subunit | Medicago truncatula | |
Zn2+ | the enzyme is a homodimer coordinating two zinc atoms per subunit | Ricinus communis | |
Zn2+ | the enzyme is a homodimer coordinating two zinc atoms per subunit | Populus trichocarpa | |
Zn2+ | the enzyme is a homodimer coordinating two zinc atoms per subunit | Zea mays | |
Zn2+ | the enzyme is a homodimer coordinating two zinc atoms per subunit | Oryza sativa Indica Group | |
Zn2+ | the enzyme is a homodimer coordinating two zinc atoms per subunit | Volvox carteri f. nagariensis | |
Zn2+ | the enzyme is a homodimer coordinating two zinc atoms per subunit | Chlamydomonas reinhardtii |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
S-nitrosoglutathione + NAD(P)H + H+ | Camelina sativa | - |
GSSG + ammonia + NAD(P)+ | - |
ir | |
S-nitrosoglutathione + NAD(P)H + H+ | Solanum lycopersicum | - |
GSSG + ammonia + NAD(P)+ | - |
ir | |
S-nitrosoglutathione + NAD(P)H + H+ | Lactuca sativa | - |
GSSG + ammonia + NAD(P)+ | - |
ir | |
S-nitrosoglutathione + NAD(P)H + H+ | Helianthus annuus | - |
GSSG + ammonia + NAD(P)+ | - |
ir | |
S-nitrosoglutathione + NAD(P)H + H+ | Arabidopsis thaliana | - |
GSSG + ammonia + NAD(P)+ | - |
ir | |
S-nitrosoglutathione + NAD(P)H + H+ | Pisum sativum | - |
GSSG + ammonia + NAD(P)+ | - |
ir | |
S-nitrosoglutathione + NAD(P)H + H+ | Capsella rubella | - |
GSSG + ammonia + NAD(P)+ | - |
ir | |
S-nitrosoglutathione + NAD(P)H + H+ | Noccaea caerulescens | - |
GSSG + ammonia + NAD(P)+ | - |
ir | |
S-nitrosoglutathione + NAD(P)H + H+ | Brassica juncea | - |
GSSG + ammonia + NAD(P)+ | - |
ir | |
S-nitrosoglutathione + NAD(P)H + H+ | Nicotiana sylvestris | - |
GSSG + ammonia + NAD(P)+ | - |
ir | |
S-nitrosoglutathione + NAD(P)H + H+ | Medicago truncatula | - |
GSSG + ammonia + NAD(P)+ | - |
ir | |
S-nitrosoglutathione + NAD(P)H + H+ | Ricinus communis | - |
GSSG + ammonia + NAD(P)+ | - |
ir | |
S-nitrosoglutathione + NAD(P)H + H+ | Populus trichocarpa | - |
GSSG + ammonia + NAD(P)+ | - |
ir | |
S-nitrosoglutathione + NAD(P)H + H+ | Zea mays | - |
GSSG + ammonia + NAD(P)+ | - |
ir | |
S-nitrosoglutathione + NAD(P)H + H+ | Oryza sativa Indica Group | - |
GSSG + ammonia + NAD(P)+ | - |
ir | |
S-nitrosoglutathione + NAD(P)H + H+ | Volvox carteri f. nagariensis | - |
GSSG + ammonia + NAD(P)+ | - |
ir | |
S-nitrosoglutathione + NAD(P)H + H+ | Chlamydomonas reinhardtii | - |
GSSG + ammonia + NAD(P)+ | - |
ir |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Arabidopsis thaliana | F4K7D6 | - |
- |
Brassica juncea | C4PKK5 | - |
- |
Camelina sativa | - |
- |
- |
Capsella rubella | R0EWH3 | - |
- |
Chlamydomonas reinhardtii | A8IY20 | - |
- |
Helianthus annuus | A0A251UXN7 | - |
- |
Lactuca sativa | J7GHV7 | - |
- |
Medicago truncatula | A0A072VKC1 | - |
- |
Nicotiana sylvestris | A0A1U7Y0I8 | - |
- |
Noccaea caerulescens | A0A1J3JHF1 | - |
- |
Oryza sativa Indica Group | A2XAZ3 | - |
- |
Pisum sativum | P80572 | - |
- |
Populus trichocarpa | A0A2K2BPI4 | - |
- |
Ricinus communis | B9T5W1 | - |
- |
Solanum lycopersicum | D2Y3F4 | - |
- |
Volvox carteri f. nagariensis | D8U4T8 | - |
- |
Zea mays | B6T6Q8 | - |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
S-nitrosylation | the not Zn2+ chelating cysteine residues Cys10, Cys271 and Cys370 of Arabidopsis are targets for S-nitrosylation. Whereas modification of Cys370 seems to promote Snitrosylation of Cys10 and Cys271 by inducing conformational changes that alters the solvent accessibility and electrostatic environment of these cysteine residues. In detail, Snitrosylation of GSNOR slightly changes the solvent accessibility of amino acids from the substrate binding site and/or the dimer interface. Mass spectrometric analysis confirms the presence of monomeric and dimeric S-nitrosylated GSNOR, while unmodified GSNOR exists as dimers | Arabidopsis thaliana |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
anther | filaments | Arabidopsis thaliana | - |
epidermal cell | - |
Helianthus annuus | - |
flower | - |
Arabidopsis thaliana | - |
flower | petal vascular tissue | Helianthus annuus | - |
hypocotyl | cortex cells | Helianthus annuus | - |
leaf | - |
Arabidopsis thaliana | - |
leaf | - |
Pisum sativum | - |
leaf | apical meristem | Helianthus annuus | - |
additional information | the Arabidopsis GSNOR gene is significantly expressed in all organs with the exception of mature pollen | Arabidopsis thaliana | - |
petal | - |
Arabidopsis thaliana | - |
plant ovary | - |
Arabidopsis thaliana | - |
root | - |
Arabidopsis thaliana | - |
root | root tip | Helianthus annuus | - |
stigma | - |
Arabidopsis thaliana | - |
vascular tissue | - |
Helianthus annuus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
S-nitrosoglutathione + NAD(P)H + H+ | - |
Camelina sativa | GSSG + ammonia + NAD(P)+ | - |
ir | |
S-nitrosoglutathione + NAD(P)H + H+ | - |
Solanum lycopersicum | GSSG + ammonia + NAD(P)+ | - |
ir | |
S-nitrosoglutathione + NAD(P)H + H+ | - |
Lactuca sativa | GSSG + ammonia + NAD(P)+ | - |
ir | |
S-nitrosoglutathione + NAD(P)H + H+ | - |
Helianthus annuus | GSSG + ammonia + NAD(P)+ | - |
ir | |
S-nitrosoglutathione + NAD(P)H + H+ | - |
Arabidopsis thaliana | GSSG + ammonia + NAD(P)+ | - |
ir | |
S-nitrosoglutathione + NAD(P)H + H+ | - |
Pisum sativum | GSSG + ammonia + NAD(P)+ | - |
ir | |
S-nitrosoglutathione + NAD(P)H + H+ | - |
Capsella rubella | GSSG + ammonia + NAD(P)+ | - |
ir | |
S-nitrosoglutathione + NAD(P)H + H+ | - |
Noccaea caerulescens | GSSG + ammonia + NAD(P)+ | - |
ir | |
S-nitrosoglutathione + NAD(P)H + H+ | - |
Brassica juncea | GSSG + ammonia + NAD(P)+ | - |
ir | |
S-nitrosoglutathione + NAD(P)H + H+ | - |
Nicotiana sylvestris | GSSG + ammonia + NAD(P)+ | - |
ir | |
S-nitrosoglutathione + NAD(P)H + H+ | - |
Medicago truncatula | GSSG + ammonia + NAD(P)+ | - |
ir | |
S-nitrosoglutathione + NAD(P)H + H+ | - |
Ricinus communis | GSSG + ammonia + NAD(P)+ | - |
ir | |
S-nitrosoglutathione + NAD(P)H + H+ | - |
Populus trichocarpa | GSSG + ammonia + NAD(P)+ | - |
ir | |
S-nitrosoglutathione + NAD(P)H + H+ | - |
Zea mays | GSSG + ammonia + NAD(P)+ | - |
ir | |
S-nitrosoglutathione + NAD(P)H + H+ | - |
Oryza sativa Indica Group | GSSG + ammonia + NAD(P)+ | - |
ir | |
S-nitrosoglutathione + NAD(P)H + H+ | - |
Volvox carteri f. nagariensis | GSSG + ammonia + NAD(P)+ | - |
ir | |
S-nitrosoglutathione + NAD(P)H + H+ | - |
Chlamydomonas reinhardtii | GSSG + ammonia + NAD(P)+ | - |
ir |
Subunits | Comment | Organism |
---|---|---|
homodimer | - |
Camelina sativa |
homodimer | - |
Solanum lycopersicum |
homodimer | - |
Lactuca sativa |
homodimer | - |
Helianthus annuus |
homodimer | - |
Pisum sativum |
homodimer | - |
Capsella rubella |
homodimer | - |
Noccaea caerulescens |
homodimer | - |
Brassica juncea |
homodimer | - |
Nicotiana sylvestris |
homodimer | - |
Medicago truncatula |
homodimer | - |
Ricinus communis |
homodimer | - |
Populus trichocarpa |
homodimer | - |
Zea mays |
homodimer | - |
Oryza sativa Indica Group |
homodimer | - |
Volvox carteri f. nagariensis |
homodimer | - |
Chlamydomonas reinhardtii |
homodimer | 2 * 42500, about, sequence calculation | Arabidopsis thaliana |
More | mass spectrometric analysis confirms the presence of monomeric and dimeric S-nitrosylated GSNOR, while unmodified GSNOR exists as dimers | Arabidopsis thaliana |
Synonyms | Comment | Organism |
---|---|---|
GSNOR | - |
Camelina sativa |
GSNOR | - |
Solanum lycopersicum |
GSNOR | - |
Lactuca sativa |
GSNOR | - |
Helianthus annuus |
GSNOR | - |
Arabidopsis thaliana |
GSNOR | - |
Pisum sativum |
GSNOR | - |
Capsella rubella |
GSNOR | - |
Noccaea caerulescens |
GSNOR | - |
Brassica juncea |
GSNOR | - |
Nicotiana sylvestris |
GSNOR | - |
Medicago truncatula |
GSNOR | - |
Ricinus communis |
GSNOR | - |
Populus trichocarpa |
GSNOR | - |
Zea mays |
GSNOR | - |
Oryza sativa Indica Group |
GSNOR | - |
Volvox carteri f. nagariensis |
GSNOR | - |
Chlamydomonas reinhardtii |
S-nitrosoglutathione reductase | - |
Camelina sativa |
S-nitrosoglutathione reductase | - |
Solanum lycopersicum |
S-nitrosoglutathione reductase | - |
Lactuca sativa |
S-nitrosoglutathione reductase | - |
Helianthus annuus |
S-nitrosoglutathione reductase | - |
Arabidopsis thaliana |
S-nitrosoglutathione reductase | - |
Pisum sativum |
S-nitrosoglutathione reductase | - |
Capsella rubella |
S-nitrosoglutathione reductase | - |
Noccaea caerulescens |
S-nitrosoglutathione reductase | - |
Brassica juncea |
S-nitrosoglutathione reductase | - |
Nicotiana sylvestris |
S-nitrosoglutathione reductase | - |
Medicago truncatula |
S-nitrosoglutathione reductase | - |
Ricinus communis |
S-nitrosoglutathione reductase | - |
Populus trichocarpa |
S-nitrosoglutathione reductase | - |
Zea mays |
S-nitrosoglutathione reductase | - |
Oryza sativa Indica Group |
S-nitrosoglutathione reductase | - |
Volvox carteri f. nagariensis |
S-nitrosoglutathione reductase | - |
Chlamydomonas reinhardtii |
Cofactor | Comment | Organism | Structure |
---|---|---|---|
NADH | - |
Camelina sativa | |
NADH | - |
Solanum lycopersicum | |
NADH | - |
Lactuca sativa | |
NADH | - |
Helianthus annuus | |
NADH | - |
Arabidopsis thaliana | |
NADH | - |
Pisum sativum | |
NADH | - |
Capsella rubella | |
NADH | - |
Noccaea caerulescens | |
NADH | - |
Brassica juncea | |
NADH | - |
Nicotiana sylvestris | |
NADH | - |
Medicago truncatula | |
NADH | - |
Ricinus communis | |
NADH | - |
Populus trichocarpa | |
NADH | - |
Zea mays | |
NADH | - |
Oryza sativa Indica Group | |
NADH | - |
Volvox carteri f. nagariensis | |
NADH | - |
Chlamydomonas reinhardtii | |
NADPH | - |
Camelina sativa | |
NADPH | - |
Solanum lycopersicum | |
NADPH | - |
Lactuca sativa | |
NADPH | - |
Helianthus annuus | |
NADPH | - |
Arabidopsis thaliana | |
NADPH | - |
Pisum sativum | |
NADPH | - |
Capsella rubella | |
NADPH | - |
Noccaea caerulescens | |
NADPH | - |
Brassica juncea | |
NADPH | - |
Nicotiana sylvestris | |
NADPH | - |
Medicago truncatula | |
NADPH | - |
Ricinus communis | |
NADPH | - |
Populus trichocarpa | |
NADPH | - |
Zea mays | |
NADPH | - |
Oryza sativa Indica Group | |
NADPH | - |
Volvox carteri f. nagariensis | |
NADPH | - |
Chlamydomonas reinhardtii |
Organism | Comment | Expression |
---|---|---|
Helianthus annuus | in sunflower seedlings exposed to high temperature (38°C for 4 h), GSNOR gene expression and GSNOR activity are reduced in hypocotyls with the simultaneous accumulation of SNOs | down |
Solanum lycopersicum | in tomato, the expression of GSNOR is significantly affected by alkaline stress. In particular, transcription of GSNOR is inhibited dramatically in response to alkaline stress between 0.5 and 2 d after treatment. Afterwards, the expression of GSNOR starts to increase at 3 d after NaHCO3 treatment, peaks on the sixth day, and then declines | down |
Arabidopsis thaliana | in Arabidopsis, the GSNOR gene is regulated by wounding and salicylic acid, although the activity | additional information |
Nicotiana sylvestris | in tobacco, the GSNOR gene is regulated by wounding and salicylic acid, although the activity | additional information |
General Information | Comment | Organism |
---|---|---|
evolution | GSNOR belongs to the class III alcohol dehydrogenase family | Camelina sativa |
evolution | GSNOR belongs to the class III alcohol dehydrogenase family | Solanum lycopersicum |
evolution | GSNOR belongs to the class III alcohol dehydrogenase family | Lactuca sativa |
evolution | GSNOR belongs to the class III alcohol dehydrogenase family | Helianthus annuus |
evolution | GSNOR belongs to the class III alcohol dehydrogenase family | Arabidopsis thaliana |
evolution | GSNOR belongs to the class III alcohol dehydrogenase family | Pisum sativum |
evolution | GSNOR belongs to the class III alcohol dehydrogenase family | Capsella rubella |
evolution | GSNOR belongs to the class III alcohol dehydrogenase family | Noccaea caerulescens |
evolution | GSNOR belongs to the class III alcohol dehydrogenase family | Brassica juncea |
evolution | GSNOR belongs to the class III alcohol dehydrogenase family | Nicotiana sylvestris |
evolution | GSNOR belongs to the class III alcohol dehydrogenase family | Medicago truncatula |
evolution | GSNOR belongs to the class III alcohol dehydrogenase family | Ricinus communis |
evolution | GSNOR belongs to the class III alcohol dehydrogenase family | Populus trichocarpa |
evolution | GSNOR belongs to the class III alcohol dehydrogenase family | Zea mays |
evolution | GSNOR belongs to the class III alcohol dehydrogenase family | Oryza sativa Indica Group |
evolution | GSNOR belongs to the class III alcohol dehydrogenase family | Volvox carteri f. nagariensis |
evolution | GSNOR belongs to the class III alcohol dehydrogenase family | Chlamydomonas reinhardtii |
malfunction | oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. In tomato, the expression of GSNOR is significantly affected by alkaline stress. Physiological function of ROS-dependent inhibition of GSNOR | Solanum lycopersicum |
malfunction | oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. Physiological function of ROS-dependent inhibition of GSNOR | Camelina sativa |
malfunction | oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. Physiological function of ROS-dependent inhibition of GSNOR | Lactuca sativa |
malfunction | oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. Physiological function of ROS-dependent inhibition of GSNOR | Helianthus annuus |
malfunction | oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. Physiological function of ROS-dependent inhibition of GSNOR | Pisum sativum |
malfunction | oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. Physiological function of ROS-dependent inhibition of GSNOR | Capsella rubella |
malfunction | oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. Physiological function of ROS-dependent inhibition of GSNOR | Noccaea caerulescens |
malfunction | oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. Physiological function of ROS-dependent inhibition of GSNOR | Brassica juncea |
malfunction | oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. Physiological function of ROS-dependent inhibition of GSNOR | Nicotiana sylvestris |
malfunction | oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. Physiological function of ROS-dependent inhibition of GSNOR | Medicago truncatula |
malfunction | oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. Physiological function of ROS-dependent inhibition of GSNOR | Ricinus communis |
malfunction | oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. Physiological function of ROS-dependent inhibition of GSNOR | Populus trichocarpa |
malfunction | oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. Physiological function of ROS-dependent inhibition of GSNOR | Zea mays |
malfunction | oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. Physiological function of ROS-dependent inhibition of GSNOR | Oryza sativa Indica Group |
malfunction | oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. Physiological function of ROS-dependent inhibition of GSNOR | Volvox carteri f. nagariensis |
malfunction | oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. Physiological function of ROS-dependent inhibition of GSNOR | Chlamydomonas reinhardtii |
malfunction | the gsnor-ko plants contain elevated amount of low and high molecular weight S-nitrosothiols (SNO) indicating that GSNOR activity controls the level of both GSNO and indirectly protein-SNOs. GSNOR deficiency has been shown to cause pleiotropic plant growth defects, impaired plant disease responses, heat sensitivity, and resistance to cell death. Oxidative post-translationally modification of GSNOR inhibits the activity of the enzyme suggesting a direct crosstalk between ROS- and RNS-signaling, regulatory effects of reactive oxygen species (ROS) on GSNOR, overview. Physiological function of ROS-dependent inhibition of GSNOR | Arabidopsis thaliana |
metabolism | S-(hydroxymethyl)glutathione dehydrogenase is involved in the S-nitrosothiol metabolism and GSNO degrading | Arabidopsis thaliana |
additional information | cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues | Camelina sativa |
additional information | cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues | Solanum lycopersicum |
additional information | cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues | Lactuca sativa |
additional information | cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues | Helianthus annuus |
additional information | cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues | Pisum sativum |
additional information | cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues | Capsella rubella |
additional information | cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues | Noccaea caerulescens |
additional information | cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues | Brassica juncea |
additional information | cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues | Nicotiana sylvestris |
additional information | cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues | Medicago truncatula |
additional information | cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues | Ricinus communis |
additional information | cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues | Populus trichocarpa |
additional information | cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues | Zea mays |
additional information | cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues | Oryza sativa Indica Group |
additional information | cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues | Volvox carteri f. nagariensis |
additional information | cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues | Chlamydomonas reinhardtii |
additional information | cysteine residues are targets for reversible and irreversible redox-modifications and play an important role in redox signaling. GSNOR is remarkably cysteine rich. In total plant GSNORs have 14 to 16 cysteine residues. Thirteen of them are highly conserved within plant GSNORs. Three of them (Cys10, Cys271, Cys370) are located on the protein surface making them directly accessible for post-translational modifications. Moreover, three cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site, where Cys47 and Cys177 are coordinating the catalytic Zn2+ together with His69 and a water molecule. The structural Zn2+ is coordinated by Cys99, Cys102, Cys105, and Cys113. Accessibility and physico-chemical features of cysteine residues define their redox-reactivity and the 3-dimensional structure of GSNOR allows to identifying such surface-exposed, redox-sensitive cysteine residues. But the Arabidopsis GSNOR has neither intermolecular nor intramolecular redox-sensitive disulfide bridges. Cysteine residues (Cys47, Cys177, Cys271) are located in the substrate binding site where Cys47 and Cys177 are involved in coordinating the catalytic Zn2+. Especially these two cysteine residues are sensitive to oxidation, whereas Cys271 localized in the NAD+ cofactor binding site is resistant to H2O2 induced oxidation | Arabidopsis thaliana |
physiological function | nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling | Camelina sativa |
physiological function | nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling | Solanum lycopersicum |
physiological function | nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling | Lactuca sativa |
physiological function | nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling | Helianthus annuus |
physiological function | nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling | Arabidopsis thaliana |
physiological function | nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling | Pisum sativum |
physiological function | nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling | Capsella rubella |
physiological function | nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling | Noccaea caerulescens |
physiological function | nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling | Brassica juncea |
physiological function | nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling | Nicotiana sylvestris |
physiological function | nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling | Medicago truncatula |
physiological function | nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling | Ricinus communis |
physiological function | nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling | Populus trichocarpa |
physiological function | nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling | Zea mays |
physiological function | nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling | Oryza sativa Indica Group |
physiological function | nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling | Volvox carteri f. nagariensis |
physiological function | nitric oxide radical (radical NO) acts as signaling molecule in plants being involved in diverse physiological processes such as germination, root growth, stomata closing and response to biotic and abiotic stress. S-Nitrosoglutathione (GSNO) is the storage and transport form of radical NO and has a very important function in radical NO signaling since it can transfer its radical NO moiety to other proteins (trans-nitrosylation). The level of GSNO and thus the level of S-nitrosylated proteins are regulated by GSNO-reductase (GSNOR). In this way, this enzyme regulates the S-nitrosothiol levels and plays a balancing role in fine-tuning radical NO signaling | Chlamydomonas reinhardtii |