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Literature summary for 1.1.1.284 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)

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

Inhibitors

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

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

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/ Products (Substrates)

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

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

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

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 and Products (Substrate)

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

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

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

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

Expression

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

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