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3-phenylpropylamine (CID 16259) - Compound BioActivity Data
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BioActivity Outcomes:
Active(8)
 
 
Unspecified(13)
 
 
Top Targets:
Tryp SPc(6)
 
 
Cu amine oxid(4)
 
 
 
BioAssay Types:
Literature(20)
 
 
 
BioActivity Types:
Ki(3)
 
 
Kd(2)
 
 
Data download

Chemical Probe    Active    Inactive    Inconclusive    Unspecified   

Total Bioassays: 19    Data Row: 21   Total Pages: 2   Display: Page     
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#SubstanceActivityBioAssayTargetLinks
OutcomeTypeValue [μM]
1
[SID103172071]
Kd 11.749Affinity against 5-hydroxytryptamine receptors in rat fundus model [AID6406, Type: Literature]
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2
[SID103172071]
Km 27Binding affinity to mouse SSAO [AID273100, Type: Literature]Membrane primary amine oxidase [gi:5902787]
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3
[SID103172071]
Ki 32.5Binding affinity against bovine trypsin [AID214878, Type: Literature]Cationic trypsin [gi:205371855]
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4
[SID46393334]
Kd 3410Experimentally measured binding affinity data (Kd) for protein-ligand complexes derived from PDB [AID977611, Type: Literature]Chain M, Trypsin Specificity As Elucidated By Lie Calculations, X-Ray Structures And Association Constant Measurements [gi:42543834]
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5
[SID46393247]
Ki 32500Experimentally measured binding affinity data (Ki) for protein-ligand complexes derived from PDB [AID977610, Type: Literature]Chain A, Prediction Of Novel Serine Protease Inhibitors [gi:157833980]
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6
[SID46393247]
Ki 32500Experimentally measured binding affinity data (Ki) for protein-ligand complexes derived from PDB [AID977610, Type: Literature]Chain A, Prediction Of Novel Serine Protease Inhibitors [gi:157833980]
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7
[SID46393247]
Experimentally measured binding affinity data derived from PDB [AID1811, Type: Literature]Chain A, Prediction Of Novel Serine Protease Inhibitors [gi:157833980]
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8
[SID46393334]
Experimentally measured binding affinity data derived from PDB [AID1811, Type: other]Chain M, Trypsin Specificity As Elucidated By Lie Calculations, X-Ray Structures And Association Constant Measurements [gi:42543834]
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9
[SID103172071]
Km 290Compound was evaluated as substrate for monoamine oxidase (MAO) from bovine erythrocyte and the enzymatic kinetic constant was reported as Km [AID125217, Type: Literature]
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10
[SID103172071]
Km 1672Binding affinity to human SSAO [AID273099, Type: Literature]Membrane primary amine oxidase [gi:2501336]
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11
[SID103172071]
Km 20400Compound was evaluated as substrate for Dopamine beta hydroxylase (DBH) from bovine adrenals and the enzymatic kinetic constant was reported as Km [AID62142, Type: Literature]
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12
[SID103172071]
Km 20400Kinetic parameter Km was measured for dopamine beta-monooxygenase [AID62282, Type: Literature]
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13
[SID103172071]
Kcat/Km value of the compound [AID62283, Type: Literature]
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14
[SID103172071]
Kinetic parameter kcat was measured for dopamine beta-monooxygenase [AID62284, Type: Literature]
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15
[SID103172071]
Compound was evaluated as substrate for monoamine oxidase (MAO) from bovine erythrocyte and the enzymatic kinetic constant was reported as Kcat [AID125213, Type: Literature]
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16
[SID103172071]
Binding affinity against trypsin [AID215916, Type: Literature]
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17
[SID103172071]
Ratio of the kinetic parameter Kcat to the Km on substrate dopamine beta-hydrolase from bovine adrenals [AID231141, Type: Literature]
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18
[SID103172071]
Ratio of the kinetic parameter Kcat to the Km on substrate dopamine monoamine oxidase [AID231142, Type: Literature]
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19
[SID103172071]
Activity of human SSAO measured as hydrogen peroxide production at 1 mM relative to benzylamine oxidation [AID273097, Type: Literature]Membrane primary amine oxidase [gi:2501336]
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20
[SID103172071]
Activity of mouse SSAO measured as hydrogen peroxide production at 100 uM relative to benzylamine oxidation [AID273098, Type: Literature]Membrane primary amine oxidase [gi:5902787]
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