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Literature summary extracted from

  • Lindermayr, C.
    Crosstalk between reactive oxygen species and nitric oxide in plants key role of S-nitrosoglutathione reductase (2018), Free Radic. Biol. Med., 122, 110-115 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.284 gene GSNOR, sequence comparisons Arabidopsis thaliana

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 peroxynitrite treatment of AtGSNOR with peroxynitrite, known as tyrosine nitrating agent, modifies this enzyme and inhibits its activity Arabidopsis thaliana

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.1.284 chloroplast
-
 Pisum sativum 9507
-
1.1.1.284 cytosol
-
 Helianthus annuus 5829
-
1.1.1.284 cytosol
-
 Arabidopsis thaliana 5829
-
1.1.1.284 cytosol
-
 Pisum sativum 5829
-
1.1.1.284 mitochondrion
-
 Pisum sativum 5739
-
1.1.1.284 nucleus
-
 Helianthus annuus 5634
-
1.1.1.284 nucleus
-
 Arabidopsis thaliana 5634
-
1.1.1.284 nucleus
-
 Pisum sativum 5634
-
1.1.1.284 peroxisome
-
 Pisum sativum 5777
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.284 Zn2+ the enzyme is a homodimer coordinating two zinc atoms per subunit Camelina sativa
1.1.1.284 Zn2+ the enzyme is a homodimer coordinating two zinc atoms per subunit Solanum lycopersicum
1.1.1.284 Zn2+ the enzyme is a homodimer coordinating two zinc atoms per subunit Lactuca sativa
1.1.1.284 Zn2+ the enzyme is a homodimer coordinating two zinc atoms per subunit Helianthus annuus
1.1.1.284 Zn2+ the enzyme is a homodimer coordinating two zinc atoms per subunit Arabidopsis thaliana
1.1.1.284 Zn2+ the enzyme is a homodimer coordinating two zinc atoms per subunit Pisum sativum
1.1.1.284 Zn2+ the enzyme is a homodimer coordinating two zinc atoms per subunit Capsella rubella
1.1.1.284 Zn2+ the enzyme is a homodimer coordinating two zinc atoms per subunit Noccaea caerulescens
1.1.1.284 Zn2+ the enzyme is a homodimer coordinating two zinc atoms per subunit Brassica juncea
1.1.1.284 Zn2+ the enzyme is a homodimer coordinating two zinc atoms per subunit Nicotiana sylvestris
1.1.1.284 Zn2+ the enzyme is a homodimer coordinating two zinc atoms per subunit Medicago truncatula
1.1.1.284 Zn2+ the enzyme is a homodimer coordinating two zinc atoms per subunit Ricinus communis
1.1.1.284 Zn2+ the enzyme is a homodimer coordinating two zinc atoms per subunit Populus trichocarpa
1.1.1.284 Zn2+ the enzyme is a homodimer coordinating two zinc atoms per subunit Zea mays
1.1.1.284 Zn2+ the enzyme is a homodimer coordinating two zinc atoms per subunit Oryza sativa Indica Group
1.1.1.284 Zn2+ the enzyme is a homodimer coordinating two zinc atoms per subunit Volvox carteri f. nagariensis
1.1.1.284 Zn2+ the enzyme is a homodimer coordinating two zinc atoms per subunit Chlamydomonas reinhardtii

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+ Camelina sativa
-
 GSSG + ammonia + NAD(P)+
-
 ir
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+ Solanum lycopersicum
-
 GSSG + ammonia + NAD(P)+
-
 ir
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+ Lactuca sativa
-
 GSSG + ammonia + NAD(P)+
-
 ir
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+ Helianthus annuus
-
 GSSG + ammonia + NAD(P)+
-
 ir
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+ Arabidopsis thaliana
-
 GSSG + ammonia + NAD(P)+
-
 ir
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+ Pisum sativum
-
 GSSG + ammonia + NAD(P)+
-
 ir
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+ Capsella rubella
-
 GSSG + ammonia + NAD(P)+
-
 ir
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+ Noccaea caerulescens
-
 GSSG + ammonia + NAD(P)+
-
 ir
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+ Brassica juncea
-
 GSSG + ammonia + NAD(P)+
-
 ir
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+ Nicotiana sylvestris
-
 GSSG + ammonia + NAD(P)+
-
 ir
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+ Medicago truncatula
-
 GSSG + ammonia + NAD(P)+
-
 ir
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+ Ricinus communis
-
 GSSG + ammonia + NAD(P)+
-
 ir
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+ Populus trichocarpa
-
 GSSG + ammonia + NAD(P)+
-
 ir
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+ Zea mays
-
 GSSG + ammonia + NAD(P)+
-
 ir
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+ Oryza sativa Indica Group
-
 GSSG + ammonia + NAD(P)+
-
 ir
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+ Volvox carteri f. nagariensis
-
 GSSG + ammonia + NAD(P)+
-
 ir
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+ Chlamydomonas reinhardtii
-
 GSSG + ammonia + NAD(P)+
-
 ir

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.284 Arabidopsis thaliana F4K7D6
-
-
1.1.1.284 Brassica juncea C4PKK5
-
-
1.1.1.284 Camelina sativa
-
-
-
1.1.1.284 Capsella rubella R0EWH3
-
-
1.1.1.284 Chlamydomonas reinhardtii A8IY20
-
-
1.1.1.284 Helianthus annuus A0A251UXN7
-
-
1.1.1.284 Lactuca sativa J7GHV7
-
-
1.1.1.284 Medicago truncatula A0A072VKC1
-
-
1.1.1.284 Nicotiana sylvestris A0A1U7Y0I8
-
-
1.1.1.284 Noccaea caerulescens A0A1J3JHF1
-
-
1.1.1.284 Oryza sativa Indica Group A2XAZ3
-
-
1.1.1.284 Pisum sativum P80572
-
-
1.1.1.284 Populus trichocarpa A0A2K2BPI4
-
-
1.1.1.284 Ricinus communis B9T5W1
-
-
1.1.1.284 Solanum lycopersicum D2Y3F4
-
-
1.1.1.284 Volvox carteri f. nagariensis D8U4T8
-
-
1.1.1.284 Zea mays B6T6Q8
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
1.1.1.284 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

EC Number Source Tissue Comment Organism Textmining
1.1.1.284 anther filaments Arabidopsis thaliana
-
1.1.1.284 epidermal cell
-
 Helianthus annuus
-
1.1.1.284 flower
-
 Arabidopsis thaliana
-
1.1.1.284 flower petal vascular tissue Helianthus annuus
-
1.1.1.284 hypocotyl cortex cells Helianthus annuus
-
1.1.1.284 leaf
-
 Arabidopsis thaliana
-
1.1.1.284 leaf
-
 Pisum sativum
-
1.1.1.284 leaf apical meristem Helianthus annuus
-
1.1.1.284 additional information the Arabidopsis GSNOR gene is significantly expressed in all organs with the exception of mature pollen Arabidopsis thaliana
-
1.1.1.284 petal
-
 Arabidopsis thaliana
-
1.1.1.284 plant ovary
-
 Arabidopsis thaliana
-
1.1.1.284 root
-
 Arabidopsis thaliana
-
1.1.1.284 root root tip Helianthus annuus
-
1.1.1.284 stigma
-
 Arabidopsis thaliana
-
1.1.1.284 vascular tissue
-
 Helianthus annuus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+
-
 Camelina sativa GSSG + ammonia + NAD(P)+
-
 ir
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+
-
 Solanum lycopersicum GSSG + ammonia + NAD(P)+
-
 ir
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+
-
 Lactuca sativa GSSG + ammonia + NAD(P)+
-
 ir
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+
-
 Helianthus annuus GSSG + ammonia + NAD(P)+
-
 ir
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+
-
 Arabidopsis thaliana GSSG + ammonia + NAD(P)+
-
 ir
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+
-
 Pisum sativum GSSG + ammonia + NAD(P)+
-
 ir
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+
-
 Capsella rubella GSSG + ammonia + NAD(P)+
-
 ir
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+
-
 Noccaea caerulescens GSSG + ammonia + NAD(P)+
-
 ir
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+
-
 Brassica juncea GSSG + ammonia + NAD(P)+
-
 ir
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+
-
 Nicotiana sylvestris GSSG + ammonia + NAD(P)+
-
 ir
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+
-
 Medicago truncatula GSSG + ammonia + NAD(P)+
-
 ir
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+
-
 Ricinus communis GSSG + ammonia + NAD(P)+
-
 ir
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+
-
 Populus trichocarpa GSSG + ammonia + NAD(P)+
-
 ir
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+
-
 Zea mays GSSG + ammonia + NAD(P)+
-
 ir
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+
-
 Oryza sativa Indica Group GSSG + ammonia + NAD(P)+
-
 ir
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+
-
 Volvox carteri f. nagariensis GSSG + ammonia + NAD(P)+
-
 ir
1.1.1.284 S-nitrosoglutathione + NAD(P)H + H+
-
 Chlamydomonas reinhardtii GSSG + ammonia + NAD(P)+
-
 ir

Subunits

EC Number Subunits Comment Organism
1.1.1.284 homodimer
-
 Camelina sativa
1.1.1.284 homodimer
-
 Solanum lycopersicum
1.1.1.284 homodimer
-
 Lactuca sativa
1.1.1.284 homodimer
-
 Helianthus annuus
1.1.1.284 homodimer
-
 Pisum sativum
1.1.1.284 homodimer
-
 Capsella rubella
1.1.1.284 homodimer
-
 Noccaea caerulescens
1.1.1.284 homodimer
-
 Brassica juncea
1.1.1.284 homodimer
-
 Nicotiana sylvestris
1.1.1.284 homodimer
-
 Medicago truncatula
1.1.1.284 homodimer
-
 Ricinus communis
1.1.1.284 homodimer
-
 Populus trichocarpa
1.1.1.284 homodimer
-
 Zea mays
1.1.1.284 homodimer
-
 Oryza sativa Indica Group
1.1.1.284 homodimer
-
 Volvox carteri f. nagariensis
1.1.1.284 homodimer
-
 Chlamydomonas reinhardtii
1.1.1.284 homodimer 2 * 42500, about, sequence calculation Arabidopsis thaliana
1.1.1.284 More mass spectrometric analysis confirms the presence of monomeric and dimeric S-nitrosylated GSNOR, while unmodified GSNOR exists as dimers Arabidopsis thaliana

Synonyms

EC Number Synonyms Comment Organism
1.1.1.284 GSNOR
-
 Camelina sativa
1.1.1.284 GSNOR
-
 Solanum lycopersicum
1.1.1.284 GSNOR
-
 Lactuca sativa
1.1.1.284 GSNOR
-
 Helianthus annuus
1.1.1.284 GSNOR
-
 Arabidopsis thaliana
1.1.1.284 GSNOR
-
 Pisum sativum
1.1.1.284 GSNOR
-
 Capsella rubella
1.1.1.284 GSNOR
-
 Noccaea caerulescens
1.1.1.284 GSNOR
-
 Brassica juncea
1.1.1.284 GSNOR
-
 Nicotiana sylvestris
1.1.1.284 GSNOR
-
 Medicago truncatula
1.1.1.284 GSNOR
-
 Ricinus communis
1.1.1.284 GSNOR
-
 Populus trichocarpa
1.1.1.284 GSNOR
-
 Zea mays
1.1.1.284 GSNOR
-
 Oryza sativa Indica Group
1.1.1.284 GSNOR
-
 Volvox carteri f. nagariensis
1.1.1.284 GSNOR
-
 Chlamydomonas reinhardtii
1.1.1.284 S-nitrosoglutathione reductase
-
 Camelina sativa
1.1.1.284 S-nitrosoglutathione reductase
-
 Solanum lycopersicum
1.1.1.284 S-nitrosoglutathione reductase
-
 Lactuca sativa
1.1.1.284 S-nitrosoglutathione reductase
-
 Helianthus annuus
1.1.1.284 S-nitrosoglutathione reductase
-
 Arabidopsis thaliana
1.1.1.284 S-nitrosoglutathione reductase
-
 Pisum sativum
1.1.1.284 S-nitrosoglutathione reductase
-
 Capsella rubella
1.1.1.284 S-nitrosoglutathione reductase
-
 Noccaea caerulescens
1.1.1.284 S-nitrosoglutathione reductase
-
 Brassica juncea
1.1.1.284 S-nitrosoglutathione reductase
-
 Nicotiana sylvestris
1.1.1.284 S-nitrosoglutathione reductase
-
 Medicago truncatula
1.1.1.284 S-nitrosoglutathione reductase
-
 Ricinus communis
1.1.1.284 S-nitrosoglutathione reductase
-
 Populus trichocarpa
1.1.1.284 S-nitrosoglutathione reductase
-
 Zea mays
1.1.1.284 S-nitrosoglutathione reductase
-
 Oryza sativa Indica Group
1.1.1.284 S-nitrosoglutathione reductase
-
 Volvox carteri f. nagariensis
1.1.1.284 S-nitrosoglutathione reductase
-
 Chlamydomonas reinhardtii

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.284 NADH
-
 Camelina sativa
1.1.1.284 NADH
-
 Solanum lycopersicum
1.1.1.284 NADH
-
 Lactuca sativa
1.1.1.284 NADH
-
 Helianthus annuus
1.1.1.284 NADH
-
 Arabidopsis thaliana
1.1.1.284 NADH
-
 Pisum sativum
1.1.1.284 NADH
-
 Capsella rubella
1.1.1.284 NADH
-
 Noccaea caerulescens
1.1.1.284 NADH
-
 Brassica juncea
1.1.1.284 NADH
-
 Nicotiana sylvestris
1.1.1.284 NADH
-
 Medicago truncatula
1.1.1.284 NADH
-
 Ricinus communis
1.1.1.284 NADH
-
 Populus trichocarpa
1.1.1.284 NADH
-
 Zea mays
1.1.1.284 NADH
-
 Oryza sativa Indica Group
1.1.1.284 NADH
-
 Volvox carteri f. nagariensis
1.1.1.284 NADH
-
 Chlamydomonas reinhardtii
1.1.1.284 NADPH
-
 Camelina sativa
1.1.1.284 NADPH
-
 Solanum lycopersicum
1.1.1.284 NADPH
-
 Lactuca sativa
1.1.1.284 NADPH
-
 Helianthus annuus
1.1.1.284 NADPH
-
 Arabidopsis thaliana
1.1.1.284 NADPH
-
 Pisum sativum
1.1.1.284 NADPH
-
 Capsella rubella
1.1.1.284 NADPH
-
 Noccaea caerulescens
1.1.1.284 NADPH
-
 Brassica juncea
1.1.1.284 NADPH
-
 Nicotiana sylvestris
1.1.1.284 NADPH
-
 Medicago truncatula
1.1.1.284 NADPH
-
 Ricinus communis
1.1.1.284 NADPH
-
 Populus trichocarpa
1.1.1.284 NADPH
-
 Zea mays
1.1.1.284 NADPH
-
 Oryza sativa Indica Group
1.1.1.284 NADPH
-
 Volvox carteri f. nagariensis
1.1.1.284 NADPH
-
 Chlamydomonas reinhardtii

Expression

EC Number Organism Comment Expression
1.1.1.284 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
1.1.1.284 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
1.1.1.284 Arabidopsis thaliana in Arabidopsis, the GSNOR gene is regulated by wounding and salicylic acid, although the activity additional information
1.1.1.284 Nicotiana sylvestris in tobacco, the GSNOR gene is regulated by wounding and salicylic acid, although the activity additional information

General Information

EC Number General Information Comment Organism
1.1.1.284 evolution GSNOR belongs to the class III alcohol dehydrogenase family Camelina sativa
1.1.1.284 evolution GSNOR belongs to the class III alcohol dehydrogenase family Solanum lycopersicum
1.1.1.284 evolution GSNOR belongs to the class III alcohol dehydrogenase family Lactuca sativa
1.1.1.284 evolution GSNOR belongs to the class III alcohol dehydrogenase family Helianthus annuus
1.1.1.284 evolution GSNOR belongs to the class III alcohol dehydrogenase family Arabidopsis thaliana
1.1.1.284 evolution GSNOR belongs to the class III alcohol dehydrogenase family Pisum sativum
1.1.1.284 evolution GSNOR belongs to the class III alcohol dehydrogenase family Capsella rubella
1.1.1.284 evolution GSNOR belongs to the class III alcohol dehydrogenase family Noccaea caerulescens
1.1.1.284 evolution GSNOR belongs to the class III alcohol dehydrogenase family Brassica juncea
1.1.1.284 evolution GSNOR belongs to the class III alcohol dehydrogenase family Nicotiana sylvestris
1.1.1.284 evolution GSNOR belongs to the class III alcohol dehydrogenase family Medicago truncatula
1.1.1.284 evolution GSNOR belongs to the class III alcohol dehydrogenase family Ricinus communis
1.1.1.284 evolution GSNOR belongs to the class III alcohol dehydrogenase family Populus trichocarpa
1.1.1.284 evolution GSNOR belongs to the class III alcohol dehydrogenase family Zea mays
1.1.1.284 evolution GSNOR belongs to the class III alcohol dehydrogenase family Oryza sativa Indica Group
1.1.1.284 evolution GSNOR belongs to the class III alcohol dehydrogenase family Volvox carteri f. nagariensis
1.1.1.284 evolution GSNOR belongs to the class III alcohol dehydrogenase family Chlamydomonas reinhardtii
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 metabolism S-(hydroxymethyl)glutathione dehydrogenase is involved in the S-nitrosothiol metabolism and GSNO degrading Arabidopsis thaliana
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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
1.1.1.284 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