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Literature summary for 4.6.1.2 extracted from

  • Hu, X.; Murata, L.B.; Weichsel, A.; Brailey, J.L.; Roberts, S.A.; Nighorn, A.; Montfort, W.R.
    Allostery in recombinant soluble guanylyl cyclase from Manduca sexta (2008), J. Biol. Chem., 283, 20968-20977.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
additional information for maximal activity, msGC required both NO and YC-1 Manduca sexta
NO 170fold activation, binding of NO leads to a transient six-coordinate intermediate, followed by release of the proximal histidine to yield a five-coordinate nitrosyl complex. Hallmark of sGC activation by NO is the release of beta1 His105 from the heme, leading to allosteric stimulation of cyclase activity Manduca sexta
YC-1 affects binding of NO and CO to the enzyme, it reduces the NO and CO off-rates for the 100 kDa N-terminal heterodimeric fragment and increases the CO affinity by 50fold, overview Manduca sexta

Cloned(Commentary)

Cloned (Comment) Organism
expression of His-tagged heterodimeric full-length and N-terminal fragments of Manduca sexta sGC in Escherichia coli strains BL21(DE3) Manduca sexta

Protein Variants

Protein Variants Comment Organism
alpha1L211A site-directed mutagenesis of the alpha1 subunit Manduca sexta
alpha1Y223A site-directed mutagenesis Manduca sexta

Inhibitors

Inhibitors Comment Organism Structure
ATP inhibits the enzyme by 70% at 1 mM in presence of stoichiometric concentrations of NO Manduca sexta

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics of ligand binding Manduca sexta

Metals/Ions

Metals/Ions Comment Organism Structure
CO competitive binding, off rates are reduced by YC-1, but YC-1 stimulation of CO binding is unaltered for the heme-intact portion of both mutated proteins, CO release from msGC-NT1-CO is measured in a stopped-flow device by replacement with NO, which binds more quickly and tightly to the enzyme, overview Manduca sexta
Mg2+
-
Manduca sexta

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
GTP Manduca sexta
-
3',5'-cyclic GMP + diphosphate
-
?

Organism

Organism UniProt Comment Textmining
Manduca sexta Q8IT60
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant His-tagged heterodimeric full-length and N-terminal fragments of sGC from Escherichia coli by nickel affinity chromatography and gel filtration Manduca sexta

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP
-
Manduca sexta 3',5'-cyclic GMP + diphosphate
-
?

Subunits

Subunits Comment Organism
More structure molecular modeling of N-terminal domains of GC alpha1 and beta1 subunits Manduca sexta

Synonyms

Synonyms Comment Organism
sGC
-
Manduca sexta
soluble guanylyl cyclase
-
Manduca sexta

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
assay at room temperature Manduca sexta

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4 7.5 assay at Manduca sexta

Cofactor

Cofactor Comment Organism Structure
heme hallmark of sGC activation by NO is the release of beta1 His105 from the heme, leading to allosteric stimulation of cyclase activity Manduca sexta