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Literature summary for 1.1.1.284 extracted from
- Evidence for an allosteric S-nitrosoglutathione binding site in S-nitrosoglutathione reductase (GSNOR) (2019), Antioxidants (Basel), 8, 545 .
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| S-nitrosoglutathione | i.e. GSNO, kinetic activation of GSNOR by its substrate S-nitrosoglutathione (GSNO). Enzyme GSNOR kinetic analysis data results in nonhyperbolic behavior that was successfully accommodated by the Hill-Langmuir equation with a Hill coex0ecient of +1.75, indicating that the substrate, GSNO, is acting as a positive allosteric affector. GSNO activates GSNOR by binding to an allosteric site comprised of the residues Asn185, Lys188, Gly321, and Lys323 | Homo sapiens |  |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene ADH5, recombinant expression of His-tagged enzyme in Escherichia coli | Homo sapiens |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| K188A | site-directed mutagenesis, the mutation results in the loss of allosteric behavior of the enzyme | Homo sapiens |
| K323A | site-directed mutagenesis, the mutation results in the loss of allosteric behavior of the enzyme | Homo sapiens |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | enzyme GSNOR kinetic analysis data results in nonhyperbolic behavior that is successfully accommodated by the Hill-Langmuir equation with a Hill coefficient of +1.75, indicating that the substrate, GSNO, is acting as a positive allosteric affector. GSNOR Michaelis-Menten steady-state kinetics display allosteric behavior | Homo sapiens | |
| 0.0113 | - |
S-nitrosoglutathione | wild-type enzyme, pH and temperature not specified in the publication | Homo sapiens | |
| 0.0284 | - |
S-nitrosoglutathione | mutant K188A, pH and temperature not specified in the publication | Homo sapiens | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| mitochondrion | - |
Homo sapiens | 5739 | - |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Zn2+ | required | Homo sapiens | |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| S-nitrosoglutathione + NADH + H+ | Homo sapiens | - |
GSSG + hydroxylamine + NAD+ | - |
ir | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Homo sapiens | P11766 | - |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Escherichia coli by nickel affinity chromatography and ultrafiltration | Homo sapiens |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | S-nitrosoglutathione (GSNO) binding to Lys188, Gly321, and Lys323. In the presence of glutathione (GSH), N-hydroxysulfenamido glutathione is converted to hydroxylamine and glutathione disulfide (GSSG) | Homo sapiens | ? | - |
- |
|
| S-nitrosoglutathione + NADH + H+ | - |
Homo sapiens | GSSG + hydroxylamine + NAD+ | - |
ir | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| ADH5 | - |
Homo sapiens |
| alcohol dehydrogenase class-3 | UniProt | Homo sapiens |
| GSNOR | - |
Homo sapiens |
| S-nitrosoglutathione reductase | - |
Homo sapiens |
Cofactor
| Cofactor | Comment | Organism | Structure |
|---|---|---|---|
| NAD+ | - |
Homo sapiens | |
| NADH | - |
Homo sapiens | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| malfunction | the dysregulation of GSNOR expression is implicated in several organ system pathologies including respiratory, cardiovascular, hematologic, and neurologic, making GSNOR a primary target for pharmacological intervention | Homo sapiens |
| additional information | location of the GSNO allosteric domain comprising the residues Asn185, Lys188, Gly321, and Lys323 in the vicinity of the structural Zn2+-binding site, docking and molecular dynamics simulations utilizing the GSNOR crystal structure (PDB ID 3QJ5)as the template structure, HDX-MS data, overview | Homo sapiens |
| physiological function | S-nitrosoglutathione reductase (GSNOR) is the central enzyme for regulating protein S-nitrosylation. GSNOR is a NAD+-dependent aldehyde dehydrogenase. It can also catalyze the NADH-coupled reduction of S-nitrosoglutathione (GSNO) to N-hydroxysulfenamido glutathione. In the presence of glutathione (GSH), N-hydroxysulfenamido glutathione is converted to hydroxylamine and glutathione disulfide (GSSG) | Homo sapiens |
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