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Literature summary for 2.7.11.11 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)

Crystallization (Comment) Organism
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

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

KM Value [mM]

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

Metals/Ions Comment Organism Structure
Mg2+ required Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
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
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
phosphoprotein phosphorylation on Ser10, Ser139, Thr197, and Ser338 Mus musculus

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
PKA
-
Mus musculus
protein kinase A
-
Mus musculus

Turnover Number [1/s]

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

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

Cofactor

Cofactor Comment Organism Structure
ATP
-
Mus musculus

General Information

General Information Comment Organism
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