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Literature summary for 2.7.11.11 extracted from

  • Kivi, R.; Loog, M.; Jemth, P.; Jaerv, J.
    Kinetics of acrylodan-labelled cAMP-dependent protein kinase catalytic subunit denaturation (2013), Protein J., 32, 519-525.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli BL21 cells Mus musculus

Protein Variants

Protein Variants Comment Organism
N326C the mutant shows increased Km values compared to the wild type enzyme Mus musculus

Inhibitors

Inhibitors Comment Organism Structure
PKI(5-24)
-
Mus musculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.027
-
peptide RRYSV wild type enzyme, at pH 7.0 and 25°C Mus musculus
0.029
-
peptide RRYSV mutant enzyme N326C, at pH 7.0 and 25°C Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Mus musculus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + peptide RRYSV
-
Mus musculus ADP + phosphorylated peptide RRYSV
-
?

Synonyms

Synonyms Comment Organism
PKAc catalytic subunit Mus musculus