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Literature summary for 4.6.1.2 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
Search for more literature for 4.6.1.2

Activating Compound

Activating Compound Comment Organism Structure
NO
-
 Rattus norvegicus

Cloned(Commentary)

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

Inhibitors

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

Metals/Ions

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

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Rattus norvegicus

Source Tissue

Source Tissue Comment Organism Textmining
lung
-
 Rattus norvegicus
-

Subunits

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