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Literature summary for 4.6.1.2 extracted from

  • Chang, F.J.; Lemme, S.; Sun, Q.; Sunahara, R.K.; Beuve, A.
    Nitric oxide-dependent allosteric inhibitory role of a second nucleotide binding site in soluble guanylyl cyclase (2005), J. Biol. Chem., 280, 11513-11519.
    View publication on PubMed
Search for more literature for 4.6.1.2

Cloned(Commentary)

Cloned (Comment) Organism
wild-type and mutant enzymes expressed in Sf21/baculovirus system Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
D477A mutation in beta subunit, mutant does not show a non-competitive mechanism with Mg2+GTPgammaS and Mg2+ATPgammaS that is observed with wild-type enzyme Rattus norvegicus
E525K/C594D mutation in alpha subunit, mutant does not show a non-competitive mechanism with Mg2+GTPgammaS and Mg2+ATPgammaS that is observed with wild-type enzyme Rattus norvegicus

Inhibitors

Inhibitors Comment Organism Structure
adenosine-5'-tetraphosphate basal activity of wild-type enzyme is considerably less sensitive than NO-stimulated wild-type activity Rattus norvegicus
ADPbetaS basal activity of wild-type enzyme is considerably less sensitive than NO-stimulated wild-type activity Rattus norvegicus
GDPbetaS basal activity of wild-type enzyme is considerably less sensitive than NO-stimulated wild-type activity Rattus norvegicus
guanosine-5'-tetraphosphate basal activity of wild-type enzyme is considerably less sensitive than NO-stimulated wild-type activity Rattus norvegicus
ITP basal activity of wild-type enzyme is considerably less sensitive than NO-stimulated wild-type activity Rattus norvegicus
Mg2+ATPgammaS inhibits cyclase activity through a mixed, non-competitive mechanism, only observable under NO stimulation and not under basal conditions Rattus norvegicus
Mg2+GTPgammaS inhibits cyclase activity through a mixed, non-competitive mechanism, only observable under NO stimulation and not under basal conditions Rattus norvegicus
XDP basal activity of wild-type enzyme is considerably less sensitive than NO-stimulated wild-type activity Rattus norvegicus
XTP basal activity of wild-type enzyme is considerably less sensitive than NO-stimulated wild-type activity Rattus norvegicus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.021
-
 GTP pH 8.0, 30°C, wild-type enzyme, in presence of NO-donor S-nitroso-N-acetylpenicillamine Rattus norvegicus
0.122
-
 GTP pH 8.0, 30°C, wild-type enzyme Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Rattus norvegicus

Synonyms

Synonyms Comment Organism
NO receptor alpha1*beta1 isoform of soluble guanylyl cyclase Rattus norvegicus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.251
-
 Mg2+GTPgammaS pH 8.0, 30°C, wild-type enzyme Rattus norvegicus