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Literature summary for 4.6.1.2 extracted from
- Tonic and acute nitric oxide signaling through soluble guanylate cyclase is mediated by nonheme nitric oxide, ATP, and GTP (2005), Proc. Natl. Acad. Sci. USA, 102, 13064-13069.
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| NO | NO binds to the heme of soluble guanylate cyclase heme, activating the enzyme. In the presence of physiological concentrations of ATP and GTP, NO dissociation from the heme of soluble guanylate cyclase is about 160 times slower than the rate of enzyme deactivation in vitro. Deactivated enzyme still has NO bound to the heme, and full activation requires additional NO. An activation model is proposed where, in the presence of both ATP and GTP, tonic NO forms a stable heme complex with low activity, acute production of NO transiently and fully activates this NO-bound enzyme | Rattus norvegicus |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Rattus norvegicus | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme | Rattus norvegicus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| lung | - |
Rattus norvegicus | - |
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