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Literature summary for 2.7.11.11 extracted from

  • Eyers, P.A.; Liu, J.; Hayashi, N.R.; Lewellyn, A.L.; Gautier, J.; Maller, J.L.
    Regulation of the G2/M transition in Xenopus oocytes by the cAMP-dependent protein kinase (2005), J. Biol. Chem., 280, 24339-24346.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
cAMP dependent on Xenopus laevis

Cloned(Commentary)

Cloned (Comment) Organism
expression of N-terminally His6-tagged wild-type and mutant catalytic subunits C in Escherichia coli strain BL21(DE3) Xenopus laevis

Protein Variants

Protein Variants Comment Organism
D328A site-directed mutagenesis of the catalytic subunit, mutant shows decreased interaction with the regulatory RI subunit Xenopus laevis
D328A/K72H site-directed mutagenesis of the catalytic subunit, inactive mutant showing decreased interaction with the regulatory RII subunit Xenopus laevis
K72H site-directed mutagenesis of the catalytic subunit, inactive mutant Xenopus laevis
K72R site-directed mutagenesis of the catalytic subunit, inactive mutant Xenopus laevis
additional information microinjection of mutant subunits C in Xenopus oocytes, overview Xenopus laevis
R133A site-directed mutagenesis of the catalytic subunit, mutant shows decreased interaction with the regulatory RII subunit Xenopus laevis
R133A/K72H site-directed mutagenesis of the catalytic subunit, inactive mutant showing decreased interaction with the regulatory RII subunit Xenopus laevis

Inhibitors

Inhibitors Comment Organism Structure
PKI recombinant His-tagged rabbit PKA inhibitor protein PKI, binding involves Arg133 Xenopus laevis

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+
-
Xenopus laevis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Xenopus laevis the enzyme regulates the G2/M transition in oocytes of Xenopus laevis, it also blocks progesterone-induced germinal vesicle envelope breakdown GVBD, Cdc-25-dependent dephosphorylation of Tyr15 in Cdc2, and synthesis of MEKK Mos ?
-
?

Organism

Organism UniProt Comment Textmining
Xenopus laevis
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant N-terminally His6-tagged wild-type and mutant catalytic subunits C from Escherichia coli strain BL21(DE3) by nickel affinity chromatography Xenopus laevis

Source Tissue

Source Tissue Comment Organism Textmining
oocyte
-
Xenopus laevis
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + Kemptide peptide substrate, activity of catalytic PKA subunit Xenopus laevis ADP + phosphorylated Kemptide
-
?
additional information the enzyme regulates the G2/M transition in oocytes of Xenopus laevis, it also blocks progesterone-induced germinal vesicle envelope breakdown GVBD, Cdc-25-dependent dephosphorylation of Tyr15 in Cdc2, and synthesis of MEKK Mos Xenopus laevis ?
-
?

Subunits

Subunits Comment Organism
More Arg133 is essential for binding of the catalytic subunit C to the regulatory subunit RII Xenopus laevis

Synonyms

Synonyms Comment Organism
PKA
-
Xenopus laevis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
assay at Xenopus laevis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.4
-
assay at Xenopus laevis

Cofactor

Cofactor Comment Organism Structure
ATP
-
Xenopus laevis