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Literature summary for 2.7.11.12 extracted from

  • Campbell, J.C.; VanSchouwen, B.; Lorenz, R.; Sankaran, B.; Herberg, F.W.; Melacini, G.; Kim, C.
    Crystal structure of cGMP-dependent protein kinase Ib cyclic nucleotide-binding-B domain Rp-cGMPS complex reveals an apo-like, inactive conformation (2017), FEBS Lett., 591, 221-230 .
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
cGMP activation constant (Ka) of 537 nM Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
cGMP-dependent protein kinase Ib cyclic nucleotide-binding domain, hanging drop vapor diffusion method, using 0.8 M lithium sulfate monohydrate, 0.1 M sodium acetate trihydrate, pH 4.0, 4% (v/v) polyethylene glycol 200 Homo sapiens

Inhibitors

Inhibitors Comment Organism Structure
additional information the R-diastereomer of the phosphorothioate analog of cGMP, Rp-cGMPS, inhibits enzyme isoform PKG I by stabilizing the inactive conformation of cyclic nucleotide-binding domain Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ 10 mM used in assay conditions Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + Kemptide Homo sapiens
-
ADP + Kemptide phosphate
-
?

Organism

Organism UniProt Comment Textmining
Homo sapiens Q13976
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + Kemptide
-
Homo sapiens ADP + Kemptide phosphate
-
?

Synonyms

Synonyms Comment Organism
cGMP-dependent protein kinase Ib
-
Homo sapiens
PKG Ibeta
-
Homo sapiens