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Literature summary for 1.1.1.284 extracted from

  • Kubienova, L.; Kopecny, D.; Tylichova, M.; Briozzo, P.; Skopalova, J.; Sebela, M.; Navratil, M.; Tache, R.; Luhova, L.; Barroso, J.B.; Petrivalsky, M.
    Structural and functional characterization of a plant S-nitrosoglutathione reductase from Solanum lycopersicum (2013), Biochimie, 95, 889-902.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
real-time PCR expression analysis, recombinant expression in Escherichia coli as N-terminally His-tagged enzyme Solanum lycopersicum

Crystallization (Commentary)

Crystallization (Comment) Organism
purified recombinant His-tagged enzyme, in complex with NAD+ and with NADH, hanging drop vapour diffusion, mixing of 0.003 ml of 22 mg/ml protein in 20 mM Tris-HCl, pH 8.0, 100 mM NaCl, 2.5 mM NAD+, or 2.5 mM NADH and 5.0 mM GSH, 20°C, X-ray diffraction tructure determination and analysis at 1.85-2.14 A resolution, molecular replacement and modeling Solanum lycopersicum

Inhibitors

Inhibitors Comment Organism Structure
2-mercaptoethanol inhibits both the reductase and dehydrogenase reactions by 30% at 1 mM Solanum lycopersicum
Ag+
-
Solanum lycopersicum
ascorbic acid inhibits both the reductase and dehydrogenase reactions by 30% at 1 mM Solanum lycopersicum
Decanoic acid
-
Solanum lycopersicum
dithiothreitol inhibits both the reductase and dehydrogenase reactions by 30% at 1 mM Solanum lycopersicum
dodecanoic acid noncompetitive Solanum lycopersicum
EDTA complete inactivation Solanum lycopersicum
glutathione noncompetitive inhibitor, inhibits GSNO reduction Solanum lycopersicum
Hg2+
-
Solanum lycopersicum
N6022 noncompetitive Solanum lycopersicum
octanoic acid
-
Solanum lycopersicum
S-Methylglutathione noncompetitive inhibitor, inhibits GSNO reduction Solanum lycopersicum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.04
-
NAD+ pH 8.0, 30°C, recombinant enzyme Solanum lycopersicum
0.057
-
S-nitrosylglutathione pH 8.0, 30°C, recombinant enzyme Solanum lycopersicum
0.058
-
NADH pH 8.0, 30°C, recombinant enzyme Solanum lycopersicum
0.058
-
S-(hydroxymethyl)glutathione pH 8.0, 30°C, recombinant enzyme Solanum lycopersicum

Localization

Localization Comment Organism GeneOntology No. Textmining
cytosol
-
Solanum lycopersicum 5829
-

Metals/Ions

Metals/Ions Comment Organism Structure
additional information other monovalent and bivalent cations, besides Hg2+ or Ag+, have only a small effect Solanum lycopersicum
Zn2+ required for the oxidation reaction. The catalytic zinc ion functions as a Lewis acid, is bound by Cys177 and Cys47, His69 and either Glu70 or water (hydroxide anion). The structural zinc is bound by four cysteines, Cys99, Cys102, Cys105, and Cys113 Solanum lycopersicum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
40000
-
2 * 40000, SDS-PAGE Solanum lycopersicum
81090
-
native enzyme, sequence calculation Solanum lycopersicum

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-(hydroxymethyl)glutathione + NAD+ Solanum lycopersicum
-
S-formylglutathione + NADH + H+
-
?
S-(hydroxymethyl)glutathione + NAD+ Solanum lycopersicum Amateur
-
S-formylglutathione + NADH + H+
-
?
S-nitrosoglutathione + NADH Solanum lycopersicum
-
? + NAD+ a variety of products depending on cellular conditions, including glutathione disulfide, glutathione sulfinamide and hydroxylamine ?
S-nitrosoglutathione + NADH Solanum lycopersicum Amateur
-
? + NAD+ a variety of products depending on cellular conditions, including glutathione disulfide, glutathione sulfinamide and hydroxylamine ?

Organism

Organism UniProt Comment Textmining
Solanum lycopersicum D2Y3F4
-
-
Solanum lycopersicum Amateur D2Y3F4
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminally His-tagged enzyme from Escherichia coli by methal chelating chromatography Solanum lycopersicum

Reaction

Reaction Comment Organism Reaction ID
S-(hydroxymethyl)glutathione + NAD(P)+ = S-formylglutathione + NAD(P)H + H+ structure-function analysis, active site and ligand binding structures,reaction mechanism, overview Solanum lycopersicum

Source Tissue

Source Tissue Comment Organism Textmining
cotyledon
-
Solanum lycopersicum
-
flower
-
Solanum lycopersicum
-
fruit the enzyme is highly expressed in the pistil and stamens and in fruits during ripening Solanum lycopersicum
-
leaf
-
Solanum lycopersicum
-
additional information expression is higher in roots and stems compared to leaves of young plants Solanum lycopersicum
-
pistil
-
Solanum lycopersicum
-
root
-
Solanum lycopersicum
-
shoot apex
-
Solanum lycopersicum
-
stamen
-
Solanum lycopersicum
-
stem
-
Solanum lycopersicum
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the reaction mechanism involved the oxidation of a hydroxyl group of S-(hydroxymethyl)glutathione, spontaneous adduct of formaldehyde and glutathione, to form S-formylglutathione. Substrate specificity with alcohols and omega-hydroxyfatty acids, overview Solanum lycopersicum ?
-
?
additional information the reaction mechanism involved the oxidation of a hydroxyl group of S-(hydroxymethyl)glutathione, spontaneous adduct of formaldehyde and glutathione, to form S-formylglutathione. Substrate specificity with alcohols and omega-hydroxyfatty acids, overview Solanum lycopersicum Amateur ?
-
?
S-(hydroxymethyl)glutathione + NAD+
-
Solanum lycopersicum S-formylglutathione + NADH + H+
-
?
S-(hydroxymethyl)glutathione + NAD+
-
Solanum lycopersicum Amateur S-formylglutathione + NADH + H+
-
?
S-nitrosoglutathione + NADH
-
Solanum lycopersicum ? + NAD+ a variety of products depending on cellular conditions, including glutathione disulfide, glutathione sulfinamide and hydroxylamine ?
S-nitrosoglutathione + NADH
-
Solanum lycopersicum Amateur ? + NAD+ a variety of products depending on cellular conditions, including glutathione disulfide, glutathione sulfinamide and hydroxylamine ?

Subunits

Subunits Comment Organism
homodimer 2 * 40000, SDS-PAGE Solanum lycopersicum

Synonyms

Synonyms Comment Organism
GSNOR
-
Solanum lycopersicum
HMGSH dehydrogenase
-
Solanum lycopersicum
S-nitrosoglutathione reductase
-
Solanum lycopersicum

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Solanum lycopersicum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
assay at Solanum lycopersicum

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.00043
-
N6022 pH 8.0, 30°C, recombinant enzyme Solanum lycopersicum
0.76
-
dodecanoic acid pH 8.0, 30°C, recombinant enzyme Solanum lycopersicum

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.0003
-
pH 8.0, 30°C, recombinant enzyme Solanum lycopersicum N6022
0.526
-
pH 8.0, 30°C, recombinant enzyme Solanum lycopersicum dodecanoic acid
3.9
-
pH 8.0, 30°C, recombinant enzyme Solanum lycopersicum glutathione
5.1
-
pH 8.0, 30°C, recombinant enzyme Solanum lycopersicum Decanoic acid
5.8
-
pH 8.0, 30°C, recombinant enzyme Solanum lycopersicum S-Methylglutathione
6.1
-
pH 8.0, 30°C, recombinant enzyme Solanum lycopersicum octanoic acid

General Information

General Information Comment Organism
evolution the enzyme belongs to the large alcohol dehydrogenase superfamily, namely to the class III ADHs Solanum lycopersicum
additional information structure-function analysis, overview Solanum lycopersicum
physiological function in plants, GSNOR plays an important role in biotic and abiotic stress responses. S-nitrosylglutathione serves as a nitric oxide reservoir locally or possibly as NO donor in distant cells and tissues. NO and NO-related molecules such as S-nitrosothiols play a central role in the regulation of normal plant physiological processes and host defence. The key enzyme participates in the cellular homeostasis of S-NOs and in the metabolism of reactive nitrogen species Solanum lycopersicum