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.

Search for more literature for 1.1.1.284

Cloned(Commentary)

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

Inhibitors

Inhibitors	Comment	Organism
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	Lathyrus oleraceus
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	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	-	Lathyrus oleraceus	9507	-
cytosol	-	Arabidopsis thaliana	5829	-
cytosol	-	Helianthus annuus	5829	-
cytosol	-	Lathyrus oleraceus	5829	-
mitochondrion	-	Lathyrus oleraceus	5739	-
nucleus	-	Arabidopsis thaliana	5634	-
nucleus	-	Helianthus annuus	5634	-
nucleus	-	Lathyrus oleraceus	5634	-
peroxisome	-	Lathyrus oleraceus	5777	-

Metals/Ions

Metals/Ions	Comment	Organism
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	Brassica juncea
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	Capsella rubella
Zn2+	the enzyme is a homodimer coordinating two zinc atoms per subunit	Chlamydomonas reinhardtii
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	Lactuca sativa
Zn2+	the enzyme is a homodimer coordinating two zinc atoms per subunit	Lathyrus oleraceus
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	Nicotiana sylvestris
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	Oryza sativa Indica Group
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	Ricinus communis
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	Volvox carteri f. nagariensis
Zn2+	the enzyme is a homodimer coordinating two zinc atoms per subunit	Zea mays

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.
S-nitrosoglutathione + NAD(P)H + H+	Arabidopsis thaliana	-	GSSG + ammonia + NAD(P)+	-	ir
S-nitrosoglutathione + NAD(P)H + H+	Capsella rubella	-	GSSG + ammonia + NAD(P)+	-	ir
S-nitrosoglutathione + NAD(P)H + H+	Camelina sativa	-	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+	Solanum lycopersicum	-	GSSG + ammonia + NAD(P)+	-	ir
S-nitrosoglutathione + NAD(P)H + H+	Nicotiana sylvestris	-	GSSG + ammonia + NAD(P)+	-	ir
S-nitrosoglutathione + NAD(P)H + H+	Lactuca sativa	-	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
S-nitrosoglutathione + NAD(P)H + H+	Helianthus annuus	-	GSSG + ammonia + NAD(P)+	-	ir
S-nitrosoglutathione + NAD(P)H + H+	Lathyrus oleraceus	-	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	-	-
Lathyrus oleraceus	P80572	-	-
Medicago truncatula	A0A072VKC1	-	-
Nicotiana sylvestris	A0A1U7Y0I8	-	-
Noccaea caerulescens	A0A1J3JHF1	-	-
Oryza sativa Indica Group	A2XAZ3	-	-
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	apical meristem	Helianthus annuus	-
leaf	-	Lathyrus oleraceus	-
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.
S-nitrosoglutathione + NAD(P)H + H+	-	Arabidopsis thaliana	GSSG + ammonia + NAD(P)+	-	ir
S-nitrosoglutathione + NAD(P)H + H+	-	Capsella rubella	GSSG + ammonia + NAD(P)+	-	ir
S-nitrosoglutathione + NAD(P)H + H+	-	Camelina sativa	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+	-	Solanum lycopersicum	GSSG + ammonia + NAD(P)+	-	ir
S-nitrosoglutathione + NAD(P)H + H+	-	Nicotiana sylvestris	GSSG + ammonia + NAD(P)+	-	ir
S-nitrosoglutathione + NAD(P)H + H+	-	Lactuca sativa	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
S-nitrosoglutathione + NAD(P)H + H+	-	Helianthus annuus	GSSG + ammonia + NAD(P)+	-	ir
S-nitrosoglutathione + NAD(P)H + H+	-	Lathyrus oleraceus	GSSG + ammonia + NAD(P)+	-	ir

Subunits

Subunits	Comment	Organism
homodimer	2 * 42500, about, sequence calculation	Arabidopsis thaliana
homodimer	-	Capsella rubella
homodimer	-	Camelina sativa
homodimer	-	Noccaea caerulescens
homodimer	-	Brassica juncea
homodimer	-	Solanum lycopersicum
homodimer	-	Nicotiana sylvestris
homodimer	-	Lactuca sativa
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	-	Helianthus annuus
homodimer	-	Lathyrus oleraceus
additional information	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	-	Arabidopsis thaliana
GSNOR	-	Capsella rubella
GSNOR	-	Camelina sativa
GSNOR	-	Noccaea caerulescens
GSNOR	-	Brassica juncea
GSNOR	-	Solanum lycopersicum
GSNOR	-	Nicotiana sylvestris
GSNOR	-	Lactuca sativa
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
GSNOR	-	Helianthus annuus
GSNOR	-	Lathyrus oleraceus
S-nitrosoglutathione reductase	-	Arabidopsis thaliana
S-nitrosoglutathione reductase	-	Capsella rubella
S-nitrosoglutathione reductase	-	Camelina sativa
S-nitrosoglutathione reductase	-	Noccaea caerulescens
S-nitrosoglutathione reductase	-	Brassica juncea
S-nitrosoglutathione reductase	-	Solanum lycopersicum
S-nitrosoglutathione reductase	-	Nicotiana sylvestris
S-nitrosoglutathione reductase	-	Lactuca sativa
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
S-nitrosoglutathione reductase	-	Helianthus annuus
S-nitrosoglutathione reductase	-	Lathyrus oleraceus

Cofactor

Cofactor	Comment	Organism
NADH	-	Arabidopsis thaliana
NADH	-	Capsella rubella
NADH	-	Camelina sativa
NADH	-	Noccaea caerulescens
NADH	-	Brassica juncea
NADH	-	Solanum lycopersicum
NADH	-	Nicotiana sylvestris
NADH	-	Lactuca sativa
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
NADH	-	Helianthus annuus
NADH	-	Lathyrus oleraceus
NADPH	-	Arabidopsis thaliana
NADPH	-	Capsella rubella
NADPH	-	Camelina sativa
NADPH	-	Noccaea caerulescens
NADPH	-	Brassica juncea
NADPH	-	Solanum lycopersicum
NADPH	-	Nicotiana sylvestris
NADPH	-	Lactuca sativa
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
NADPH	-	Helianthus annuus
NADPH	-	Lathyrus oleraceus

Expression

Organism	Comment	Expression
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
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
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	Arabidopsis thaliana
evolution	GSNOR belongs to the class III alcohol dehydrogenase family	Capsella rubella
evolution	GSNOR belongs to the class III alcohol dehydrogenase family	Camelina sativa
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	Solanum lycopersicum
evolution	GSNOR belongs to the class III alcohol dehydrogenase family	Nicotiana sylvestris
evolution	GSNOR belongs to the class III alcohol dehydrogenase family	Lactuca sativa
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
evolution	GSNOR belongs to the class III alcohol dehydrogenase family	Helianthus annuus
evolution	GSNOR belongs to the class III alcohol dehydrogenase family	Lathyrus oleraceus
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
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	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	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. 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	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	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	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	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	Lathyrus oleraceus
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. 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
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	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	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	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	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	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	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	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	Lathyrus oleraceus
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	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	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	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	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	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	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	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
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	Lathyrus oleraceus