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Literature summary extracted from

  • Bastidas, A.C.; Deal, M.S.; Steichen, J.M.; Keshwani, M.M.; Guo, Y.; Taylor, S.S.
    Role of N-terminal myristylation in the structure and regulation of cAMP-dependent protein kinase (2012), J. Mol. Biol., 422, 215-229.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.7.11.11 purified myristylated wild-type PKA and a K7C mutant as binary complex with bound substrate SP20 peptide and as ternary complex with bound substrate SP20 peptide and adenosine-5'-(beta,gamma-imido)triphosphate, hanging drop vapor diffusion method, 8-10 mg/ml protein in 50 mM N,N-bis(2-hydroxyethyl)glycine, 150 mM ammonium acetate, and 10 mM DTT, pH 8.0, is combined in 1:10:20:5 molar ratio of protein:AMP-PNP:Mg2+:SP20 for the ternary complex or 1:5 protein:SP20 for the binary complex, screening and method optimization, mixing of equal volumes of protein and well solution, the latter containing 2-18% 2-methyl-2,4-pentanediol, and mother liquor or buffers ranging from pH 5.35 to pH 8.5, 100 mM 2-[bis(2-hydroxyethyl)amino]-2-(hydroxymethyl) propane-1,3-diol, pH 6.5, and 9% MeOH, 8-10 weeks, 4°C, X-ray diffraction structure determination and analysis at 1.35-2.0 A resolution, modeling Mus musculus

Protein Variants

EC Number Protein Variants Comment Organism
2.7.11.11 K7C site-directed mutagenesis, the mutant exhibits altered kinetics in a myristylated state compared to the wild-type enzyme Mus musculus
2.7.11.11 N2D site-directed mutagenesis, the mutant cannot be myristoylated at Asn2 Mus musculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.11.11 0.019
-
 ATP pH 7.0, temperature not specified in the publication, wild-type enzyme Mus musculus
2.7.11.11 0.023
-
 Leu-Arg-Arg-Ala-Ser-Leu-Gly pH 7.0, temperature not specified in the publication, myristoylated wild-type enzyme Mus musculus
2.7.11.11 0.023
-
 ATP pH 7.0, temperature not specified in the publication, myristoylated wild-type enzyme and enzyme mutant K7C Mus musculus
2.7.11.11 0.027
-
 Leu-Arg-Arg-Ala-Ser-Leu-Gly pH 7.0, temperature not specified in the publication, enzyme mutant K7C Mus musculus
2.7.11.11 0.029
-
 Leu-Arg-Arg-Ala-Ser-Leu-Gly pH 7.0, temperature not specified in the publication, wild-type enzyme Mus musculus
2.7.11.11 0.032
-
 ATP pH 7.0, temperature not specified in the publication, myristoylated enzyme mutant K7C Mus musculus
2.7.11.11 0.043
-
 Leu-Arg-Arg-Ala-Ser-Leu-Gly pH 7.0, temperature not specified in the publication, myristoylated enzyme mutant K7C Mus musculus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.11.11 Mg2+ required Mus musculus

Organism

EC Number Organism UniProt Comment Textmining
2.7.11.11 Mus musculus
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
2.7.11.11 lipoprotein irreversible covalent N-myristylation of PKA or occupancy of the myristyl binding pocket may serve as a site for allosteric regulation in the catalytic C-subunit. And N-myristylation enhances the thermal stability of the enzyme, the myristylated C-subunit has a higher affinity for membranes alone. PKA cannot be myristylated if Asn2 is mutated to Asp Mus musculus
2.7.11.11 additional information the C-subunit of PKA may be regulated by irreversible deamidation of Asn2. With PKA that is purified from tissues, irreversible deamidation of Asn2 to Asp or isoAsp occurs in about 1/3 of the total C-subunit protein. Also, the deamidated form of the protein has a higher cytosolic-to-nuclear ratio than the non-deamidated protein Mus musculus
2.7.11.11 phosphoprotein phosphorylation on Ser10, Ser139, Thr197, and Ser338 Mus musculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.11.11 ATP + Leu-Arg-Arg-Ala-Ser-Leu-Gly commercial artificial heptapeptide substrate kemptide Mus musculus ADP + Leu-Arg-Arg-Ala-phospho-Ser-Leu-Gly
-
 ?
2.7.11.11 ATP + SP20 peptide
-
 Mus musculus ADP + phosphorylated SP20 peptide
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.11.11 PKA
-
 Mus musculus
2.7.11.11 protein kinase A
-
 Mus musculus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.11.11 18
-
 Leu-Arg-Arg-Ala-Ser-Leu-Gly pH 7.0, temperature not specified in the publication, myristoylated wild-type enzyme and enzyme mutant K7C Mus musculus
2.7.11.11 19
-
 Leu-Arg-Arg-Ala-Ser-Leu-Gly pH 7.0, temperature not specified in the publication, wild-type enzyme Mus musculus
2.7.11.11 29
-
 Leu-Arg-Arg-Ala-Ser-Leu-Gly pH 7.0, temperature not specified in the publication, myristoylated enzyme mutant K7C Mus musculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.11.11 7
-
 assay at Mus musculus

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.11.11 ATP
-
 Mus musculus

General Information

EC Number General Information Comment Organism
2.7.11.11 metabolism the catalytic subunit of cAMP-dependent protein kinase is a major target of cAMP signaling, and its regulation is of fundamental importance to biological processes Mus musculus