Reaction Details |
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Target | cAMP-dependent protein kinase catalytic subunit alpha |
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Ligand | BDBM11824 |
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Substrate/Competitor | Peptide Substrate |
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Meas. Tech. | Fluorescence Polarization-based Assay |
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pH | 7.2±n/a |
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Temperature | 295.15±n/a K |
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IC50 | 39±n/a nM |
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Citation | Breitenlechner, CB; Wegge, T; Berillon, L; Graul, K; Marzenell, K; Friebe, WG; Thomas, U; Schumacher, R; Huber, R; Engh, RA; Masjost, B Structure-based optimization of novel azepane derivatives as PKB inhibitors. J Med Chem47:1375-90 (2004) [PubMed] Article |
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More Info.: | Get all data from this article, Inhibition_Run data, Solution Info, Assay Method |
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cAMP-dependent protein kinase catalytic subunit alpha |
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Name: | cAMP-dependent protein kinase catalytic subunit alpha |
Synonyms: | KAPCA_BOVIN | PKA C-alpha | PKC | PRKACA | Protein Kinase C | Protein Kinase C, bovine brain | cAMP-Dependent Protein Kinase (PKA) | cAMP-dependent Protein Kinase, bovine heart | cAMP-dependent protein kinase A | cAMP-dependent protein kinase alpha-catalytic subunit | cAMP-dependent protein kinase, alpha-catalytic subunit |
Type: | Enzyme Complex |
Mol. Mass.: | 40627.77 |
Organism: | Bos taurus (bovine) |
Description: | The PKA holoenzyme purified from bovine heart, exists as an inactive tetrameric complex, which consists of a regulatory dimer associated with two catalytic subunits. It requires cAMP to activate the enzymatic reaction. |
Residue: | 351 |
Sequence: | MGNAAAAKKGSEQESVKEFLAKAKEDFLKKWENPAQNTAHLDQFERIKTLGTGSFGRVML
VKHMETGNHYAMKILDKQKVVKLKQIEHTLNEKRILQAVNFPFLVKLEFSFKDNSNLYMV
MEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLTFEYLHSLDLIYRDLKPENLLIDQQGY
IQVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKGYNKAVDWWALGVLIYEMAAGYPPFF
ADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGVNDIKNHKWFAT
TDWIAIYQRKVEAPFIPKFKGPGDTSNFDDYEEEEIRVSINEKCGKEFSEF
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BDBM11824 |
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Peptide Substrate |
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Name: | Peptide Substrate |
Synonyms: | biotinylated tridecapeptide substrate |
Type: | Peptide |
Mol. Mass.: | 1564.86 |
Organism: | n/a |
Description: | n/a |
Residue: | 13 |
Sequence: | |