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Literature summary extracted from

  • Winger, J.A.; Marletta, M.A.
    Expression and characterization of the catalytic domains of soluble guanylate cyclase: interaction with the heme domain (2005), Biochemistry, 44, 4083-4090.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
4.6.1.2 NO
-
Rattus norvegicus

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.6.1.2 catalytic domains (alphacat and betacat) of alpha1beta1 soluble guanylate cyclase are expressed in Escherichia coli Rattus norvegicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.6.1.2 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]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.6.1.2 0.085
-
GTP Mn2+-GTP Rattus norvegicus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
4.6.1.2 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
4.6.1.2 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

EC Number Organism UniProt Comment Textmining
4.6.1.2 Rattus norvegicus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.6.1.2
-
Rattus norvegicus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
4.6.1.2 lung
-
Rattus norvegicus
-

Subunits

EC Number Subunits Comment Organism
4.6.1.2 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