Activating Compound | Comment | Organism | Structure |
---|---|---|---|
NO | - |
Rattus norvegicus |
Cloned (Comment) | Organism |
---|---|
catalytic domains (alphacat and betacat) of alpha1beta1 soluble guanylate cyclase are expressed in Escherichia coli | Rattus norvegicus |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | the N-terminal heme-bound regulatory domain of the beta1 subunit of soluble guanylate cyclase inhibits the activity of the alphacatbetacat complex in trans, suggesting a domain-scale mechanism of regulation by NO | Rattus norvegicus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.085 | - |
GTP | Mn2+-GTP | Rattus norvegicus |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Mg2+ | physiological cofactor. Like the full-length enzyme, the alphacatbetacat complex is more active in presence of Mn2+ as compared to the physiological cofactor | Rattus norvegicus | |
Mn2+ | like the full-length enzyme, the alphacatbetacat complex is more active in presence of Mn2+ as compared to the physiological cofactor | Rattus norvegicus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | - |
- |
- |
Purification (Comment) | Organism |
---|---|
- |
Rattus norvegicus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
lung | - |
Rattus norvegicus | - |
Subunits | Comment | Organism |
---|---|---|
More | each of the catalytic domains alphacat and betacat (expressed in Escherichia coli), form homodimers. Heterodimers are formed when alphacat and betacat are combined | Rattus norvegicus |