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(R)-PFI-2

(R)-PFI-2 : SAM uncompetitive, peptide competitive inhibitor (in the presence of SAM) of SETD7

Structure

Information

  • SETD7
  • SAM uncompetitive inhibitor, Peptide competitive inhibitor (in the presence of SAM)
  • 100 nM - 5 uM

In Vitro Validations

Uniprot ID: Q8WTS6
Target Class: Epigenetic
Target SubClass: Protein methyltransferase
Potency: Ki (app)
Potency Value: 0.33 nM
Potency Assay: IC50 = 2 nM in radioactive methyltransferase assay, transfer of 3H from 3H-SAM to peptide substrate
PDB ID for probe-target interaction (3D structure): 4JLG
Target aliases:
Histone-lysine N-methyltransferase SETD7, SET9, SE ...

DOI Reference: 10.1073/pnas.1407358111

In Cell Validations

In Vivo Data

No in Vivo Validations

Off-Target Selectivity Assesments

Potency assay (off target): 1000-fold selective compared with 18 other protein methyltransferases and DNMT
Probe Selectivity in Vitro:

No notable activity against 134 targets (ion channels, GPCRs, or other enzymes) up to 10 uM.

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SERP ratings and comments

SERP Ratings

In Cell Rating

(last updated: 17 May 2016 )

SERP Ratings

In Cell Rating

SERP Comments:

The enantiomer (S)-PFI-2 is 500-fold less active, making it a useful negative control. Note, the probe also has an unusual cofactor-dependent mechanism of action: (R)-PFI-2 binds to SETD7 only in the presence of SAM; inhibition of SETD7 activity by (R)-PFI-2 is unlikely to be purely substrate-competitive in the classical sense.

(last updated: 18 May 2016 )

SERP Ratings

In Cell Rating

SERP Comments:

This is currently the most potent probe available for this target. The availability of the negative control compound further strengthens the usability of this inhibitor.

(last updated: 6 Jun 2016 )