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BioAssay: AID 273098

Activity of mouse SSAO measured as hydrogen peroxide production at 100 uM relative to benzylamine oxidation

Structure activity relationships for semicarbazide-sensitive amine oxidase/vascular adhesion protein-1 (SSAO/VAP-1) were studied using a library of arylalkylamine substrates, with the aim of contributing to the discovery of more efficient SSAO substrates. Experimental data were contrasted with computational docking studies, thereby allowing us to examine the mechanism and substrate-binding more ..
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 Tested Compounds
 Tested Compounds
All(45)
 
 
Unspecified(45)
 
 
 Tested Substances
 Tested Substances
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Unspecified(45)
 
 
 Related BioAssays
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AID: 273098
Data Source: ChEMBL (415921)
Depositor Category: Literature, Extracted
BioAssay Version:
Deposit Date: 2010-05-25
Modify Date: 2013-11-18

Data Table ( Complete ):           All
Target
Sequence: RecName: Full=Membrane primary amine oxidase; AltName: Full=Copper amine oxidase; AltName: Full=Semicarbazide-sensitive amine oxidase; Short=SSAO; AltName: Full=Vascular adhesion protein 1; Short=VAP-1
Description ..   
Protein Family: Copper amine oxidase, enzyme domain
Comment ..   

Gene:AOC3     Related Protein 3D Structures     More BioActivity Data..
Tested Compounds:
Description:
Title: New efficient substrates for semicarbazide-sensitive amine oxidase/VAP-1 enzyme: analysis by SARs and computational docking.

Abstract: Structure activity relationships for semicarbazide-sensitive amine oxidase/vascular adhesion protein-1 (SSAO/VAP-1) were studied using a library of arylalkylamine substrates, with the aim of contributing to the discovery of more efficient SSAO substrates. Experimental data were contrasted with computational docking studies, thereby allowing us to examine the mechanism and substrate-binding affinity of SSAO and thus contribute to the discovery of more efficient SSAO substrates and provide a structural basis for their interactions. We also built a model of the mouse SSAO structure, which provides several structural rationales for interspecies differences in SSAO substrate selectivity and reveals new trends in SSAO substrate recognition. In this context, we identified novel efficient substrates for human SSAO that can be used as a lead for the discovery of antidiabetic agents.
(PMID: 17034126)
Categorized Comment
ChEMBL Assay Type: Functional

ChEMBL Assay Data Source: Scientific Literature

ChEMBL Target ID: 20006

ChEMBL Target Type: Target is a single protein chain

Result Definitions
TIDNameDescriptionHistogramTypeUnit
OutcomeThe BioAssay activity outcomeOutcome
1Activity activity commentActivity activity commentString
2Activity standard flagActivity standard flagInteger
3Activity qualifierActivity qualifierString
4Activity published valueActivity published valueFloat%
5Activity standard valueActivity standard valueFloat%

Data Table (Concise)
Classification
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