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BioAssay: AID 220154

Activation of cAMP-dependent protein kinase type II

A series of novel adenosine 3',5'-cyclic monophosphate (cAMP) analogues, as well as their 6-deamino and 6-nitro derivatives, were synthesized where the purine ring was replaced by indazole, benzotriazole, and benzimidazole. The 3',5'-cyclic monophosphates of indazole and benzotriazole ribofuranosides, where the sugar-phosphate moiety is attached to the N-2 nitrogen atoms of the heterocycles, were more ..
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 Tested Compounds
 Tested Compounds
All(12)
 
 
Unspecified(12)
 
 
 Tested Substances
 Tested Substances
All(12)
 
 
Unspecified(12)
 
 
 Related BioAssays
 Related BioAssays
AID: 220154
Data Source: ChEMBL (217494)
Depositor Category: Literature, Extracted
BioAssay Version:
Deposit Date: 2010-05-21
Modify Date: 2014-08-23

Data Table ( Complete ):           View All Data
Targets
Sequence: RecName: Full=cAMP-dependent protein kinase catalytic subunit beta; Short=PKA C-beta
Description ..   
Protein Family: Catalytic domain of the Protein Serine/Threonine Kinase, cAMP-dependent protein kinase
Comment ..   

Gene:PRKACB     Related Protein 3D Structures     More BioActivity Data..


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Tested Compounds:
Description:
Title: Synthesis and enzymatic activity of some new purine ring system analogues of adenosine 3',5'-cyclic monophosphate.

Abstract: A series of novel adenosine 3',5'-cyclic monophosphate (cAMP) analogues, as well as their 6-deamino and 6-nitro derivatives, were synthesized where the purine ring was replaced by indazole, benzotriazole, and benzimidazole. The 3',5'-cyclic monophosphates of indazole and benzotriazole ribofuranosides, where the sugar-phosphate moiety is attached to the N-2 nitrogen atoms of the heterocycles, were also prepared. The biological efficiency of the analogues was tested by their ability to activate purified cAMP-dependent protein kinase I (PK-I) from rabbit skeletal muscle and cAMP-dependent protein kinase II (PK-II) from bovine heart. Each cyclic nucleotide is capable of activating both PK isozymes in half-maximum concentrations (Ka) ranging from 2.0 x 10(-8) to 4.8 x 10(-6) M. The cyclic phosphate of N-1-beta-D-ribofuranosylindazole (13) proved to be a very poor activator for both PK-I and PK-II, but when indazole binds by N-2 to ribose or when the hydrogen atom at C-4 is substituted by a nitro or amino group, activities of the analogues increase considerably. The activating potencies of benzotriazole derivatives are similar to that of cAMP, irrespective of the C-4 substituents. The Ka' values of cyclic nucleotides containing benzimidazole were found to be higher for PK-II than for PK-I; e.g. the activity of 4-nitro-1-beta-D-ribofuranosylbenzimidazole 3',5'-cyclic monophosphate (32) is nearly 20 times as high for PK-II than for PK-I.
(PMID: 1335076)
Categorized Comment - additional comments and annotations
From BioAssay Depositor:
Assay Type: Binding
Assay Data Source: Scientific Literature
Result Definitions
TIDNameDescriptionHistogramTypeUnit
OutcomeThe BioAssay activity outcomeOutcome
1K'a activity commentK'a activity commentString
2K'a standard flagK'a standard flagInteger
3K'a qualifierK'a qualifierString
4K'a published valueK'a published valueFloat
5K'a standard valueK'a standard valueFloat

Data Table (Concise)
Data Table ( Complete ):     View All Data
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