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Literature summary for 1.1.1.284 extracted from
- S-nitrosoglutathione reductase - the master regulator of protein S-nitrosation in plant NO signaling (2019), Plants (Basel), 8, 48 .
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| crystal structures of SlGSNOR apoenzyme, binary complex with NAD+ and a structure crystallized in the presence of NADH and GSH. Catalytic domains of the apoenzyme and of the binary complex with NAD+ are both in the semi-open conformation. The catalytic zinc atoms in the apoenzyme are in a tetrahedral configuration, H-bonded to Cys47, Cys177, His69 and coordinated to the molecule of water in the active site. The coenzyme binding is associated with the catalytic zinc atoms movement towards Glu70 in the catalytic domain in a hydrogen-bonding interaction with the carboxylate oxygen of Glu70. Zinc atoms are in a tetrahedral configuration coordinated with Cys47, Cys177, His69, and Glu70, and they are no longer coordinated with the water molecule. In the SlGSNOR structure crystallized with NADH and GSH, the enzyme appears in closed conformation. Structue analysis, overview | Solanum lycopersicum |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Cd2+ | in pea leaves treated with 0.05 mM cadmium, GSNOR expression and activity are decreased by about 30% | Pisum sativum |  |
| Decanoic acid | noncompetitive inhibitor | Solanum lycopersicum | |
| dodecanoic acid | noncompetitive inhibitor | Solanum lycopersicum | |
| GSH | - |
Solanum lycopersicum | |
| additional information | GSNOR enzymatic activity, but not gene expression, is inhibited by the nitrogen assimilatory pathway via post-transcriptional S-nitrosation, preventing any scavenging of GSNO | Arabidopsis thaliana | |
| additional information | lacking an S-nitrosyl or S-hydroxymethyl group that binds to the active site zinc atom, the affinity of inhibitors GSH and S-methylglutathione is reduced by 2-3 orders of magnitude compared to GSNO and HMGSH | Solanum lycopersicum | |
| N6022 | a pyrolle-based compound, that is a significantly stronger noncompetitive inhibitor compared to fatty acids, inhibiting SlGSNOR at nanomolar concentrations | Solanum lycopersicum | |
| NO | susceptibility of the enzymatic activity to NO donors in vitro and its subsequent restoration after treatment with reducing agent dithiothreitol (DTT) | Arabidopsis thaliana | |
| octanoic acid | noncompetitive inhibitor | Solanum lycopersicum | |
| S-Methylglutathione | - |
Solanum lycopersicum | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.057 | - |
S-nitrosoglutathione | pH and temperature not specified in the publication | Solanum lycopersicum | |
| 0.058 | - |
S-(hydroxymethyl)glutathione | pH and temperature not specified in the publication | Solanum lycopersicum | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| cytosol | - |
Oryza sativa | 5829 | - |
| cytosol | - |
Solanum lycopersicum | 5829 | - |
| cytosol | - |
Arabidopsis thaliana | 5829 | - |
| cytosol | - |
Nicotiana tabacum | 5829 | - |
| cytosol | - |
Helianthus annuus | 5829 | - |
| cytosol | - |
Cucumis sativus | 5829 | - |
| cytosol | - |
Cucumis melo | 5829 | - |
| cytosol | - |
Nicotiana attenuata | 5829 | - |
| cytosol | - |
Solanum tuberosum | 5829 | - |
| cytosol | - |
Pisum sativum | 5829 | - |
| cytosol | - |
Lotus japonicus | 5829 | - |
| cytosol | - |
Chlamydomonas reinhardtii | 5829 | - |
| mitochondrion | the enzyme contains a mitochondrial targeting peptide | Physcomitrium patens | 5739 | - |
| additional information | modulation of the mitochondrial functionality by GSNOR, using cell suspension cultures with both higher and lower GSNOR levels, is demonstrated in Arabidopsis thaliana plants | Arabidopsis thaliana | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zn2+ | each catalytic domain includes two zinc atoms. One of them is involved in the catalytic mechanism by activating the hydroxyl and carbonyl groups of substrates for transfer of hydride, and is bonded to Cys47, Cys177, His69, and either Glu70 or a water molecule. The second zinc atom is considered to have purely a structural role and is coordinated to four cysteine residues, Cys99, Cys102, Cys105, and Cys113. From the crystal structure is determined, that the catalytic zinc atoms in the apoenzyme are in a tetrahedral configuration, H-bonded to Cys47, Cys177, His69 and coordinated to the molecule of water in the active site. The coenzyme binding is associated with the catalytic zinc atoms movement towards Glu70 in the catalytic domain in a hydrogen-bonding interaction with the carboxylate oxygen of Glu70. Zinc atoms are in a tetrahedral configuration coordinated with Cys47, Cys177, His69, and Glu70, and they are no longer coordinated with the water molecule | Solanum lycopersicum | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Oryza sativa | in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO | ? | - |
- |
|
| additional information | Solanum lycopersicum | in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO | ? | - |
- |
|
| additional information | Arabidopsis thaliana | in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO | ? | - |
- |
|
| additional information | Solanum tuberosum | in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO | ? | - |
- |
|
| additional information | Pisum sativum | in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO | ? | - |
- |
|
| additional information | Lotus japonicus | in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO | ? | - |
- |
|
| additional information | Chlamydomonas reinhardtii | in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a cosubstrate in the reduction of GSNO | ? | - |
- |
|
| additional information | Physcomitrium patens | in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO | ? | - |
- |
|
| additional information | Nicotiana tabacum | in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO | ? | - |
- |
|
| additional information | Helianthus annuus | in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO | ? | - |
- |
|
| additional information | Cucumis sativus | in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO | ? | - |
- |
|
| additional information | Cucumis melo | in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO | ? | - |
- |
|
| additional information | Nicotiana attenuata | in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO | ? | - |
- |
|
| S-(hydroxymethyl)glutathione + NAD+ | Oryza sativa | - |
S-formylglutathione + NADH + H+ | - |
? | |
| S-(hydroxymethyl)glutathione + NAD+ | Solanum lycopersicum | - |
S-formylglutathione + NADH + H+ | - |
? | |
| S-(hydroxymethyl)glutathione + NAD+ | Arabidopsis thaliana | - |
S-formylglutathione + NADH + H+ | - |
? | |
| S-(hydroxymethyl)glutathione + NAD+ | Physcomitrium patens | - |
S-formylglutathione + NADH + H+ | - |
? | |
| S-(hydroxymethyl)glutathione + NAD+ | Nicotiana tabacum | - |
S-formylglutathione + NADH + H+ | - |
? | |
| S-(hydroxymethyl)glutathione + NAD+ | Helianthus annuus | - |
S-formylglutathione + NADH + H+ | - |
? | |
| S-(hydroxymethyl)glutathione + NAD+ | Cucumis sativus | - |
S-formylglutathione + NADH + H+ | - |
? | |
| S-(hydroxymethyl)glutathione + NAD+ | Cucumis melo | - |
S-formylglutathione + NADH + H+ | - |
? | |
| S-(hydroxymethyl)glutathione + NAD+ | Nicotiana attenuata | - |
S-formylglutathione + NADH + H+ | - |
? | |
| S-(hydroxymethyl)glutathione + NAD+ | Solanum tuberosum | - |
S-formylglutathione + NADH + H+ | - |
? | |
| S-(hydroxymethyl)glutathione + NAD+ | Pisum sativum | - |
S-formylglutathione + NADH + H+ | - |
? | |
| S-(hydroxymethyl)glutathione + NAD+ | Lotus japonicus | - |
S-formylglutathione + NADH + H+ | - |
? | |
| S-(hydroxymethyl)glutathione + NAD+ | Chlamydomonas reinhardtii | - |
S-formylglutathione + NADH + H+ | - |
? | |
| S-nitrosoglutathione + NADH + H+ | Oryza sativa | - |
GSSG + ammonia + NAD+ | - |
ir | |
| S-nitrosoglutathione + NADH + H+ | Solanum lycopersicum | - |
GSSG + ammonia + NAD+ | - |
ir | |
| S-nitrosoglutathione + NADH + H+ | Arabidopsis thaliana | - |
GSSG + ammonia + NAD+ | - |
ir | |
| S-nitrosoglutathione + NADH + H+ | Physcomitrium patens | - |
GSSG + ammonia + NAD+ | - |
ir | |
| S-nitrosoglutathione + NADH + H+ | Nicotiana tabacum | - |
GSSG + ammonia + NAD+ | - |
ir | |
| S-nitrosoglutathione + NADH + H+ | Helianthus annuus | - |
GSSG + ammonia + NAD+ | - |
ir | |
| S-nitrosoglutathione + NADH + H+ | Cucumis sativus | - |
GSSG + ammonia + NAD+ | - |
ir | |
| S-nitrosoglutathione + NADH + H+ | Cucumis melo | - |
GSSG + ammonia + NAD+ | - |
ir | |
| S-nitrosoglutathione + NADH + H+ | Nicotiana attenuata | - |
GSSG + ammonia + NAD+ | - |
ir | |
| S-nitrosoglutathione + NADH + H+ | Solanum tuberosum | - |
GSSG + ammonia + NAD+ | - |
ir | |
| S-nitrosoglutathione + NADH + H+ | Pisum sativum | - |
GSSG + ammonia + NAD+ | - |
ir | |
| S-nitrosoglutathione + NADH + H+ | Lotus japonicus | - |
GSSG + ammonia + NAD+ | - |
ir | |
| S-nitrosoglutathione + NADH + H+ | Chlamydomonas reinhardtii | - |
GSSG + ammonia + NAD+ | - |
ir | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Arabidopsis thaliana | Q96533 | - |
- |
| Chlamydomonas reinhardtii | A0A2K3D6Q9 | - |
- |
| Cucumis melo | A0A1S3CB00 | - |
- |
| Cucumis sativus | A0A0A0KBZ1 | - |
- |
| Helianthus annuus | A0A251UXN7 | - |
- |
| Lotus japonicus | I3ST14 | Lotus corniculatus var. japonicus | - |
| Nicotiana attenuata | A0A314KZZ1 | - |
- |
| Nicotiana tabacum | A0A1S3ZYT7 | - |
- |
| Oryza sativa | - |
- |
- |
| Physcomitrium patens | A0A2K1JM97 | - |
- |
| Pisum sativum | P80572 | - |
- |
| Solanum lycopersicum | D2Y3F4 | - |
- |
| Solanum tuberosum | Q2XPW7 | - |
- |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| nitrosylation | regulation of GSNOR activity through S-nitrosation of conserved cysteines is observed in Arabidopsis thaliana plants. Mono-, di-, and trinitrosation, which are confirmed by mass spectrometry, lead to subtle changes in enzyme conformation. GSNOR enzymatic activity, but not gene expression, is inhibited by the nitrogen assimilatory pathway via post-transcriptional S-nitrosation, preventing any scavenging of GSNO | Arabidopsis thaliana |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| cell suspension culture | - |
Arabidopsis thaliana | - |
| leaf | - |
Solanum lycopersicum | - |
| leaf | - |
Arabidopsis thaliana | - |
| leaf | - |
Nicotiana tabacum | - |
| leaf | - |
Cucumis sativus | - |
| leaf | - |
Cucumis melo | - |
| leaf | - |
Solanum tuberosum | - |
| leaf | - |
Pisum sativum | - |
| root | - |
Cucumis sativus | - |
| root | - |
Cucumis melo | - |
| root | - |
Pisum sativum | - |
| seedling | - |
Helianthus annuus | - |
| stem | - |
Cucumis sativus | - |
| stem | - |
Cucumis melo | - |
| stem | - |
Solanum tuberosum | - |
| stem | - |
Pisum sativum | - |
| TBY-2 cell | - |
Nicotiana tabacum | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO | Oryza sativa | ? | - |
- |
|
| additional information | in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO | Solanum lycopersicum | ? | - |
- |
|
| additional information | in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO | Arabidopsis thaliana | ? | - |
- |
|
| additional information | in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO | Solanum tuberosum | ? | - |
- |
|
| additional information | in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO | Pisum sativum | ? | - |
- |
|
| additional information | in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO | Lotus japonicus | ? | - |
- |
|
| additional information | in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamid (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a cosubstrate in the reduction of GSNO | Chlamydomonas reinhardtii | ? | - |
- |
|
| additional information | in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO | Physcomitrium patens | ? | - |
- |
|
| additional information | in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO | Nicotiana tabacum | ? | - |
- |
|
| additional information | in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO | Helianthus annuus | ? | - |
- |
|
| additional information | in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO | Cucumis sativus | ? | - |
- |
|
| additional information | in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO | Cucumis melo | ? | - |
- |
|
| additional information | in the dehydrogenase mode, GSNOR using NAD+ as a coenzyme the oxidation of S-hydroxymethylglutathione (HMGSH), spontaneously formed from formaldehyde and glutathione to S-formylglutathione, which is further hydrolyzed to glutathione and formate by S-formylglutathione hydrolase. In the reductase mode, GSNOR catalyzes the reduction of S-nitrosoglutathione (GSNO) using NADH to an unstable intermediate N-hydroxysulfinamide (GSNHOH). Depending on the local concentration of GSH, GSNHOH is either decomposed to glutathione disulfide (GSSG) and hydroxylamine at high GSH levels, or at low GSH levels spontaneously converts to glutathione sulfinamide (GSONH2), which can be hydrolyzed to glutathione sulfinic acid (GSOOH) and ammonia. Another factor involved in the regulation of GSNO turnover is the accessibility of NADH, a co-substrate in the reduction of GSNO | Nicotiana attenuata | ? | - |
- |
|
| additional information | plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant | Arabidopsis thaliana | ? | - |
- |
|
| additional information | plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant | Physcomitrium patens | ? | - |
- |
|
| additional information | plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant | Nicotiana tabacum | ? | - |
- |
|
| additional information | plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant | Helianthus annuus | ? | - |
- |
|
| additional information | plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant | Cucumis sativus | ? | - |
- |
|
| additional information | plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant | Cucumis melo | ? | - |
- |
|
| additional information | plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant | Nicotiana attenuata | ? | - |
- |
|
| additional information | plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant. GSNO is reduced with 15-20times higher catalytic efficiency compared to the oxidation of HMGSH | Oryza sativa | ? | - |
- |
|
| additional information | plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant. GSNO is reduced with 15-20times higher catalytic efficiency compared to the oxidation of HMGSH | Solanum lycopersicum | ? | - |
- |
|
| additional information | plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant. GSNO is reduced with 15-20times higher catalytic efficiency compared to the oxidation of HMGSH | Solanum tuberosum | ? | - |
- |
|
| additional information | plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant. GSNO is reduced with 15-20times higher catalytic efficiency compared to the oxidation of HMGSH | Pisum sativum | ? | - |
- |
|
| additional information | plant GSNOR catalyzes the oxidation of HMGSH, geraniol, cinnamyl alcohol, omega-hydroxyfatty acids, and aliphatic alcohols with chains longer than four carbons, to corresponding aldehydes using NAD+ as a coenzyme. Short-chain alcohols, e.g. ethanol and propanol, are not enzyme substrates. In the reductase mode, plant GSNOR preferentially catalyzes the reduction of GSNO, while reactions with either aliphatic or aromatic aldehydes are insignificant. GSNO is reduced with 15-20times higher catalytic efficiency compared to the oxidation of HMGSH | Lotus japonicus | ? | - |
- |
|
| S-(hydroxymethyl)glutathione + NAD+ | - |
Oryza sativa | S-formylglutathione + NADH + H+ | - |
? | |
| S-(hydroxymethyl)glutathione + NAD+ | - |
Solanum lycopersicum | S-formylglutathione + NADH + H+ | - |
? | |
| S-(hydroxymethyl)glutathione + NAD+ | - |
Arabidopsis thaliana | S-formylglutathione + NADH + H+ | - |
? | |
| S-(hydroxymethyl)glutathione + NAD+ | - |
Physcomitrium patens | S-formylglutathione + NADH + H+ | - |
? | |
| S-(hydroxymethyl)glutathione + NAD+ | - |
Nicotiana tabacum | S-formylglutathione + NADH + H+ | - |
? | |
| S-(hydroxymethyl)glutathione + NAD+ | - |
Helianthus annuus | S-formylglutathione + NADH + H+ | - |
? | |
| S-(hydroxymethyl)glutathione + NAD+ | - |
Cucumis sativus | S-formylglutathione + NADH + H+ | - |
? | |
| S-(hydroxymethyl)glutathione + NAD+ | - |
Cucumis melo | S-formylglutathione + NADH + H+ | - |
? | |
| S-(hydroxymethyl)glutathione + NAD+ | - |
Nicotiana attenuata | S-formylglutathione + NADH + H+ | - |
? | |
| S-(hydroxymethyl)glutathione + NAD+ | - |
Solanum tuberosum | S-formylglutathione + NADH + H+ | - |
? | |
| S-(hydroxymethyl)glutathione + NAD+ | - |
Pisum sativum | S-formylglutathione + NADH + H+ | - |
? | |
| S-(hydroxymethyl)glutathione + NAD+ | - |
Lotus japonicus | S-formylglutathione + NADH + H+ | - |
? | |
| S-(hydroxymethyl)glutathione + NAD+ | - |
Chlamydomonas reinhardtii | S-formylglutathione + NADH + H+ | - |
? | |
| S-nitrosoglutathione + NADH + H+ | - |
Oryza sativa | GSSG + ammonia + NAD+ | - |
ir | |
| S-nitrosoglutathione + NADH + H+ | - |
Solanum lycopersicum | GSSG + ammonia + NAD+ | - |
ir | |
| S-nitrosoglutathione + NADH + H+ | - |
Arabidopsis thaliana | GSSG + ammonia + NAD+ | - |
ir | |
| S-nitrosoglutathione + NADH + H+ | - |
Physcomitrium patens | GSSG + ammonia + NAD+ | - |
ir | |
| S-nitrosoglutathione + NADH + H+ | - |
Nicotiana tabacum | GSSG + ammonia + NAD+ | - |
ir | |
| S-nitrosoglutathione + NADH + H+ | - |
Helianthus annuus | GSSG + ammonia + NAD+ | - |
ir | |
| S-nitrosoglutathione + NADH + H+ | - |
Cucumis sativus | GSSG + ammonia + NAD+ | - |
ir | |
| S-nitrosoglutathione + NADH + H+ | - |
Cucumis melo | GSSG + ammonia + NAD+ | - |
ir | |
| S-nitrosoglutathione + NADH + H+ | - |
Nicotiana attenuata | GSSG + ammonia + NAD+ | - |
ir | |
| S-nitrosoglutathione + NADH + H+ | - |
Solanum tuberosum | GSSG + ammonia + NAD+ | - |
ir | |
| S-nitrosoglutathione + NADH + H+ | - |
Pisum sativum | GSSG + ammonia + NAD+ | - |
ir | |
| S-nitrosoglutathione + NADH + H+ | - |
Lotus japonicus | GSSG + ammonia + NAD+ | - |
ir | |
| S-nitrosoglutathione + NADH + H+ | - |
Chlamydomonas reinhardtii | GSSG + ammonia + NAD+ | - |
ir | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| homodimer | 2 * 40000, SDS-PAGE | Solanum lycopersicum |
| More | tomato GSNOR is a homodimeric enzyme consisting of two 40 kDa subunits containing a big catalytic and a small coenzyme-binding domain with an active site localized in a cleft between them. Non-catalytic domain includes a binding site for NAD+ coenzyme: six beta-strands of each coenzyme-binding domain form 12 pseudo-continuous beta-sheets. Each catalytic domain includes two zinc atoms. One of them is involved in the catalytic mechanism by activating the hydroxyl and carbonyl groups of substrates for transfer of hydride, and is bonded to Cys47, Cys177, His69, and either Glu70 or a water molecule. The second zinc atom is considered to have purely a structural role and is coordinated to four cysteine residues, Cys99, Cys102, Cys105, and Cys113 | Solanum lycopersicum |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ADH3 | - |
Oryza sativa |
| ADH3 | - |
Solanum lycopersicum |
| ADH3 | - |
Arabidopsis thaliana |
| ADH3 | - |
Physcomitrium patens |
| ADH3 | - |
Nicotiana tabacum |
| ADH3 | - |
Helianthus annuus |
| ADH3 | - |
Cucumis sativus |
| ADH3 | - |
Cucumis melo |
| ADH3 | - |
Nicotiana attenuata |
| ADH3 | - |
Solanum tuberosum |
| ADH3 | - |
Pisum sativum |
| ADH3 | - |
Lotus japonicus |
| ADH3 | - |
Chlamydomonas reinhardtii |
| alcohol dehydrogenase class-3 | UniProt | Arabidopsis thaliana |
| AtGSNOR | - |
Arabidopsis thaliana |
| FALDH | - |
Oryza sativa |
| FALDH | - |
Solanum lycopersicum |
| FALDH | - |
Arabidopsis thaliana |
| FALDH | - |
Physcomitrium patens |
| FALDH | - |
Nicotiana tabacum |
| FALDH | - |
Helianthus annuus |
| FALDH | - |
Cucumis sativus |
| FALDH | - |
Cucumis melo |
| FALDH | - |
Nicotiana attenuata |
| FALDH | - |
Solanum tuberosum |
| FALDH | - |
Pisum sativum |
| FALDH | - |
Lotus japonicus |
| FALDH | - |
Chlamydomonas reinhardtii |
| GSNOR | - |
Oryza sativa |
| GSNOR | - |
Solanum lycopersicum |
| GSNOR | - |
Arabidopsis thaliana |
| GSNOR | - |
Physcomitrium patens |
| GSNOR | - |
Nicotiana tabacum |
| GSNOR | - |
Helianthus annuus |
| GSNOR | - |
Cucumis sativus |
| GSNOR | - |
Cucumis melo |
| GSNOR | - |
Nicotiana attenuata |
| GSNOR | - |
Solanum tuberosum |
| GSNOR | - |
Pisum sativum |
| GSNOR | - |
Lotus japonicus |
| GSNOR | - |
Chlamydomonas reinhardtii |
| HMGSH dehydrogenase | - |
Oryza sativa |
| HMGSH dehydrogenase | - |
Solanum lycopersicum |
| HMGSH dehydrogenase | - |
Arabidopsis thaliana |
| HMGSH dehydrogenase | - |
Physcomitrium patens |
| HMGSH dehydrogenase | - |
Nicotiana tabacum |
| HMGSH dehydrogenase | - |
Helianthus annuus |
| HMGSH dehydrogenase | - |
Cucumis sativus |
| HMGSH dehydrogenase | - |
Cucumis melo |
| HMGSH dehydrogenase | - |
Nicotiana attenuata |
| HMGSH dehydrogenase | - |
Solanum tuberosum |
| HMGSH dehydrogenase | - |
Pisum sativum |
| HMGSH dehydrogenase | - |
Lotus japonicus |
| HMGSH dehydrogenase | - |
Chlamydomonas reinhardtii |
| PmGSNOR | - |
Physcomitrium patens |
| S-nitrosoglutathione reductase | - |
Oryza sativa |
| S-nitrosoglutathione reductase | - |
Solanum lycopersicum |
| S-nitrosoglutathione reductase | - |
Arabidopsis thaliana |
| S-nitrosoglutathione reductase | - |
Physcomitrium patens |
| S-nitrosoglutathione reductase | - |
Nicotiana tabacum |
| S-nitrosoglutathione reductase | - |
Helianthus annuus |
| S-nitrosoglutathione reductase | - |
Cucumis sativus |
| S-nitrosoglutathione reductase | - |
Cucumis melo |
| S-nitrosoglutathione reductase | - |
Nicotiana attenuata |
| S-nitrosoglutathione reductase | - |
Solanum tuberosum |
| S-nitrosoglutathione reductase | - |
Pisum sativum |
| S-nitrosoglutathione reductase | - |
Lotus japonicus |
| S-nitrosoglutathione reductase | - |
Chlamydomonas reinhardtii |
| SlGSNOR | - |
Solanum lycopersicum |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| additional information | GSNOR cannot use NADPH in the reduction of GSNO | Oryza sativa | |
| additional information | GSNOR cannot use NADPH in the reduction of GSNO | Solanum lycopersicum | |
| additional information | GSNOR cannot use NADPH in the reduction of GSNO | Arabidopsis thaliana | |
| additional information | GSNOR cannot use NADPH in the reduction of GSNO | Physcomitrium patens | |
| additional information | GSNOR cannot use NADPH in the reduction of GSNO | Nicotiana tabacum | |
| additional information | GSNOR cannot use NADPH in the reduction of GSNO | Helianthus annuus | |
| additional information | GSNOR cannot use NADPH in the reduction of GSNO | Cucumis sativus | |
| additional information | GSNOR cannot use NADPH in the reduction of GSNO | Cucumis melo | |
| additional information | GSNOR cannot use NADPH in the reduction of GSNO | Nicotiana attenuata | |
| additional information | GSNOR cannot use NADPH in the reduction of GSNO | Solanum tuberosum | |
| additional information | GSNOR cannot use NADPH in the reduction of GSNO | Pisum sativum | |
| additional information | GSNOR cannot use NADPH in the reduction of GSNO | Lotus japonicus | |
| additional information | GSNOR cannot use NADPH in the reduction of GSNO | Chlamydomonas reinhardtii | |
| NADH | - |
Oryza sativa | |
| NADH | - |
Arabidopsis thaliana | |
| NADH | - |
Physcomitrium patens | |
| NADH | - |
Nicotiana tabacum | |
| NADH | - |
Helianthus annuus | |
| NADH | - |
Cucumis sativus | |
| NADH | - |
Cucumis melo | |
| NADH | - |
Nicotiana attenuata | |
| NADH | - |
Solanum tuberosum | |
| NADH | - |
Pisum sativum | |
| NADH | - |
Lotus japonicus | |
| NADH | - |
Chlamydomonas reinhardtii | |
| NADH | the coenzyme binding is associated with the catalytic zinc atoms movement towards Glu70 in the catalytic domain in a hydrogen-bonding interaction with the carboxylate oxygen of Glu70. In the SlGSNOR structure crystallized with NADH and GSH, the enzyme appears in closed conformation | Solanum lycopersicum | |
Expression
| Organism | Comment | Expression |
|---|---|---|
| Nicotiana tabacum | both GSNOR mRNA and protein levels are decreased in tobacco plants after treatment with jasmonic acid, the hormone implicated in the wounding signal transduction | down |
| Nicotiana attenuata | both GSNOR mRNA and protein levels are decreased in tobacco plants after treatment with jasmonic acid, the hormone implicated in the wounding signal transduction | down |
| Arabidopsis thaliana | GSNOR gene expression is downregulated in Arabidopsis after wounding | down |
| Helianthus annuus | GSNOR is downregulated, at the level of gene and protein expression and enzymatic activity, in mechanically damaged sunflower (Helianthus annuus) seedlings, which in turn leads to an accumulation of S-nitrosothiols, specifically GSNO | down |
| Pisum sativum | in pea leaves treated with 0.05 mM cadmium, GSNOR expression and activity are decreased by about 30% | down |
| Lotus japonicus | water stress, a problem for plant growth and productivity, in Lotus japonicus leads to both oxidative and nitrosative stress. Among others, cellular NO and S-nitrosothiol content are increased, GSNOR activity is reduced, and protein tyrosine nitration is stimulated | down |
| Chlamydomonas reinhardtii | an important role of NO, GSNOR, and S-nitrosation in response to salt stress is described in Chlamydomonas reinhardtii. NO production via increased nitrate reductase, but not NOS-like enzyme, activity is induced by salt stress to trigger the defense response. Induction or inactivation of antioxidant enzymes and GSNOR varied in connection with the duration of salt stress. Short-term stress causes the enzymes to scavenge ROSs and RNSs and balance cellular redox status. Long-term stress inactivates them significantly by RNS-induced protein S-nitrosation, resulting in oxidative damage and reduced cell viability. Salt stress induced the accumulation of S-nitrosothiols and S-nitrosation of GSNOR, glutathione S-transferase, and ubiquitin-like protein; S-nitrosation is reduced by thioredoxin-h5 (TRXh5), while it is enhanced by GSNOR inhibitor DA | additional information |
| Cucumis sativus | enzyme expression levels at different light conditions in different tissues, overview | additional information |
| Cucumis melo | enzyme expression levels at different light conditions in different tissues, overview | additional information |
| Pisum sativum | enzyme expression levels at different light conditions in different tissues, overview | additional information |
| Arabidopsis thaliana | GSNOR enzymatic activity, but not gene expression, is inhibited by the nitrogen assimilatory pathway via post-transcriptional S-nitrosation, preventing any scavenging of GSNO. GSNOR activity is modulated in response to altered light conditions, as described for the first time in Arabidopsis thaliana HOT5 mutant plants grown in the dark | additional information |
| Arabidopsis thaliana | 40% increase in GSNOR activity is observed in plants grown in the presence of 0.5 mM arsenate, accompanied with a significant reduction of GSNO content and a significant increase in NO content | up |
| Pisum sativum | a significant increase in enzyme expression is observed in leaves of pea plants exposed to continuous light and continuous dark | up |
| Cucumis sativus | an increase in GSNOR activity in roots, stems, and leaves is observed in two genotypes of Cucumis spp., Curcumis sativus and Curcumis melo, exposed to mechanical damage of stem and leaf | up |
| Cucumis melo | an increase in GSNOR activity in roots, stems, and leaves is observed in two genotypes of Cucumis spp., Curcumis sativus and Curcumis melo, exposed to mechanical damage of stem and leaf | up |
| Oryza sativa | GSNOR gene expression and enzymatic activity are slightly higher and the enzymatic activity is significantly increased by NO treatment in rice plants grown under aluminum stress | up |
| Solanum tuberosum | in potato plants exposed to aluminum, GSNOR activity is not affected in roots and it is increased by about 20% and 45% in leaves and stems, respectively | up |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1) | Physcomitrium patens |
| evolution | GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins | Oryza sativa |
| evolution | GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins | Solanum lycopersicum |
| evolution | GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins | Arabidopsis thaliana |
| evolution | GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins | Nicotiana tabacum |
| evolution | GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins | Helianthus annuus |
| evolution | GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins | Cucumis sativus |
| evolution | GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins | Cucumis melo |
| evolution | GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins | Nicotiana attenuata |
| evolution | GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins | Solanum tuberosum |
| evolution | GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins | Pisum sativum |
| evolution | GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins | Lotus japonicus |
| evolution | GSNOR is evolutionarily conserved, it is reclassified as S-(hydroxymethyl)glutathione dehydrogenase (EC 1.1.1.284). FALDH and ADH3 are identical enzymes. GSNOR also is a Zn-dependent medium-chain class III alcohol dehydrogenase (ADH3, EC 1.1.1.1). GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). Eukaryotic GSNORs are highly conserved and unusually cysteine-rich proteins | Chlamydomonas reinhardtii |
| malfunction | a fast increase in S-nitrosothiol content and a reduction of the leaf photosynthesis ratio are a result of suppressed GSNOR activity with specific inhibitors | Oryza sativa |
| malfunction | a fast increase in S-nitrosothiol content and a reduction of the leaf photosynthesis ratio are a result of suppressed GSNOR activity with specific inhibitors | Solanum tuberosum |
| malfunction | a fast increase in S-nitrosothiol content and a reduction of the leaf photosynthesis ratio are a result of suppressed GSNOR activity with specific inhibitors | Pisum sativum |
| malfunction | a potential role of GSNOR in plant resistance to herbivory Manduca sexta is examined in coyote tobacco (Nicotiana attenuata) plants using a virus-induced silencing of GSNOR. GSNOR-silenced plants are more susceptible to herbivore attack and decreased the herbivore-induced accumulation of phytohormones jasmonic acid (JA) and ethylene and activity of trypsin proteinase inhibitors | Nicotiana attenuata |
| malfunction | Arabidopsis thaliana plants overexpressing the GSNOR gene exhibit increased nitrate reductase (NR) activity, conversely, GSNOR mutant plants show a significant decrease in NR activity. GSNOR enzymatic activity, but not gene expression, is inhibited by the nitrogen assimilatory pathway via post-transcriptional S-nitrosation, preventing any scavenging of GSNO. Enzymatic activity of GSNOR is essential for the acclimation of Arabidopsis thaliana plants to high temperature, since HOT5 mutants, plants with defect GSNOR gene, are more sensitive to high temperature as a consequence of disturbed homeostasis of S-nitrosothiols and NO-derived ROS signaling pathways. Enzyme mutant Nox1 is an NO overproducing plant with higher levels of L-arginine and L-citrulline, while mutant Gsnor1-3 is a plant with reduced GSNOR activity with higher levels of NO, S-nitrosothiols, and nitrate. Gsnor1-3 mutant Arabidopsis thaliana plants with a high S-nitrosothiols level show an increased selenite tolerance. high NO level, due to the reduced GSNOR activity, increases sensitivity under mild stress conditions, while it supports tolerance under severe stress conditions. Gsnor1-3 mutant plants with a high S-nitrosothiols level show an increased selenite tolerance | Arabidopsis thaliana |
| malfunction | GSNOR overexpression in tomato plant has little effect on growth and development, whereas GSNOR downregulated plants are significantly smaller, suggesting a role for NO and S-nitrosothiol signaling | Solanum lycopersicum |
| malfunction | water stress, a problem for plant growth and productivity, in Lotus japonicus leads to both oxidative and nitrosative stress. Among others, cellular NO and S-nitrosothiol content are increased, GSNOR activity is reduced, and protein tyrosine nitration is stimulated | Lotus japonicus |
| physiological function | S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Important role of GSNOR and S-nitrosation in adaptation of Chlamydomonas reinhardtii to salt stress | Chlamydomonas reinhardtii |
| physiological function | S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymatically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. GSNOR is involved in plant responses to cold and heat stress | Solanum lycopersicum |
| physiological function | S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymatically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. GSNOR is involved in plant responses to cold and heat stress | Physcomitrium patens |
| physiological function | S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymatically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. GSNOR is involved in plant responses to cold and heat stress | Helianthus annuus |
| physiological function | S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymatically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. GSNOR is involved in plant responses to cold and heat stress | Cucumis melo |
| physiological function | S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymatically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. Regulation of GSNOR activity through S-nitrosation of conserved cysteines is observed in Arabidopsis thaliana plants. GSNOR activity might be regulated by high levels of NO donors. Changes in GSNOR levels have an influence on the activities of mitochondrial complex I, external NADH dehydrogenase, alternative oxidase and uncoupling protein. GSNOR modulates the activity of the mitochondrial respiratory chain through controlling NO/SNO homeostasis under physiological conditions and under nutritional stress. Regulatory mechanisms of GSNOR in protein denitrosation on the intersection of signaling pathways of ROSs and RNSs. GSNOR is involved in plant responses to cold and heat stress | Arabidopsis thaliana |
| physiological function | S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymatically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. GSNOR is involved in plant responses to cold and heat stress. NO and GSNO, as S-nitrosating agents, and GSNOR are found to be involved in the programmed cell death (PCD) induced by heat shock or H2O2 in tobacco (Nicotiana tabacum) bright yellow-2 cells | Nicotiana tabacum |
| physiological function | S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. GSNOR is involved in plant responses to cold and heat stress | Cucumis sativus |
| physiological function | S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymatically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. GSNOR mediates some jasmonate-dependent responses, e.g., the accumulation of defense secondary metabolites. GSNOR is involved in plant responses to cold and heat stress | Nicotiana attenuata |
| physiological function | S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymatically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. GSNOR modulates NO-induced nitrosative stress in rice plants grown under aluminum stress, which leads to accumulation of both ROSs and RNSs | Oryza sativa |
| physiological function | S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymatically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. GSNOR modulates NO-induced nitrosative stress in rice plants grown under aluminum stress, which leads to accumulation of both ROSs and RNSs | Solanum tuberosum |
| physiological function | S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymatically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. GSNOR modulates NO-induced nitrosative stress in rice plants grown under aluminum stress, which leads to accumulation of both ROSs and RNSs | Pisum sativum |
| physiological function | S-nitrosoglutathione reductase (GSNOR) is the master regulator of protein S-nitrosation in plant NO signaling. GSNOR functions are mediated by its enzymatic activity, which catalyzes irreversible GSNO conversion to oxidized glutathione within the cellular catabolism of nitric oxide. GSNOR is involved in the maintenance of balanced levels of reactive nitrogen species and in the control of cellular redox state. Multiple functions of GSNOR in plant development via NO-dependent and -independent signaling mechanisms and in plant defense responses to abiotic and biotic stress conditions. It is the key enzyme of the regulation of S-nitrosation and formaldehyde detoxification. Via removing GSNO, GSNOR plays a critical role in the metabolism of RNSs, in the homeostasis of intracellular levels of NO and in control of the trans-nitrosation equilibrium between S-nitrosylated proteins and GSNO, the most common low-molecular weight S-nitrosothiol. In trans-nitrosation reactions, the nitroso group is transferred among thiols on proteins and low-molecular weight peptides. GSNO reduction by GSNOR is an irreversible reaction, and the products can no longer nitrosate cellular proteins. GSNOR is a cytosolic enzyme that catalyzes the NADH-dependent reduction of GSNO, leading to the formation of glutathione disulfide (GSSG) and ammonium. GSNOR also is glutathione-dependent formaldehyde dehydrogenase (FALDH, EC 1.2.1.1). The proper substrate for FALDH is the hemithioacetal S-hydroxymethylglutathione (HMGSH), formed nonenzymatically from formaldehyde and glutathione. The enzyme is reclassified as S-(hydroxymethyl)glutathione dehydrogenase. Enzyme reactions overview. Since GSNOR cannot use NADPH in the reduction of GSNO, it is controlled by NADH availability and increasing levels of NADH are proposed to trigger the GSNO reduction. GSNOR enzymes themselves produce NADH in the process of the oxidation of formaldehyde, formaldehyde likely triggers the reduction of GSNO, regulation of the enzyme, overview. GSNOR modulates NO-induced nitrosative stress in rice plants grown under aluminum stress, which leads to accumulation of both ROSs and RNSs | Lotus japonicus |
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