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BioAssay: AID 725671

Ratio of Kinact to Ki for human PAD4 using BAEE as substrate after 30 mins

Protein arginine deiminases (PADs) are involved in a number of cellular pathways, and they catalyze the transformation of peptidyl arginine residue into a citrulline as part of post-translational modifications. To understand ligand preferences, a group of probe molecules were investigated against PAD1, PAD2, and PAD4. These probe molecules carried a well-known covalent modifier of the catalytic more ..
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 Tested Compounds
 Tested Compounds
All(4)
 
 
Unspecified(4)
 
 
 Tested Substances
 Tested Substances
All(4)
 
 
Unspecified(4)
 
 
 Related BioAssays
 Related BioAssays
AID: 725671
Data Source: ChEMBL (938237)
Depositor Category: Literature, Extracted
BioAssay Version:
Deposit Date: 2013-11-07
Modify Date: 2014-08-27

Data Table ( Complete ):           View All Data
Target
Sequence: RecName: Full=Protein-arginine deiminase type-4; AltName: Full=HL-60 PAD; AltName: Full=Peptidylarginine deiminase IV; AltName: Full=Protein-arginine deiminase type IV
Description ..   
Protein Family: Protein-arginine deiminase (PAD)
Comment ..   

Gene:PADI4     Related Protein 3D Structures     More BioActivity Data..
Tested Compounds:
Description:
Title: Interrogation of the Active Sites of Protein Arginine Deiminases (PAD1, -2, and -4) Using Designer Probes.

Abstract: Protein arginine deiminases (PADs) are involved in a number of cellular pathways, and they catalyze the transformation of peptidyl arginine residue into a citrulline as part of post-translational modifications. To understand ligand preferences, a group of probe molecules were investigated against PAD1, PAD2, and PAD4. These probe molecules carried a well-known covalent modifier of the catalytic cysteine residue, 2-chloroacetamidine moiety, which was tethered to an alpha-amino acid via a carbon linker. The chain length for the linker varied from 0 to 4. Time-dependent assays indicated that 2-chloroacetamidine (2CA) with no linker inhibited all PAD enzymes with a similar trend in the second-order rate constants, although with poor affinity. Among the other three probe molecules, compound 3 with a three-carbon linker exhibited the best second-order rate constants for optimal ligand reactivity with the binding site. These analyses provide insights into the relative patterns of covalent inactivation of PAD isozymes and the design of novel inhibitors targeting PAD enzymes as potential therapeutic targets.
(PMID: 24900657)
Categorized Comment - additional comments and annotations
From BioAssay Depositor:
Assay Type: Binding
Target Type: Target is a single protein chain
Assay Data Source: Scientific Literature
Result Definitions
TIDNameDescriptionHistogramTypeUnit
OutcomeThe BioAssay activity outcomeOutcome
1Ratio activity commentRatio activity commentString
2Ratio standard flagRatio standard flagInteger
3Ratio qualifierRatio qualifierString
4Ratio published valueRatio published valueFloat/M/min
5Ratio standard valueRatio standard valueFloat/M/min

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