Structural highlights
Function
[DEF_STRR6] Removes the formyl group from the N-terminal Met of newly synthesized proteins. Requires at least a dipeptide for an efficient rate of reaction. N-terminal L-methionine is a prerequisite for activity but the enzyme has broad specificity at other positions (By similarity).
Publication Abstract from PubMed
A new class of PDF inhibitor with potent, broad spectrum antibacterial activity is described. Optimization of blood stability and potency provided compounds with improved pharmacokinetics that were suitable for in vivo experiments. Compound 5c, which has robust antibacterial activity, demonstrated efficacy in two respiratory tract infection models.
Acylprolinamides: A new class of peptide deformylase inhibitors with in vivo antibacterial activity.,Axten JM, Medina JR, Blackledge CW, Duquenne C, Grant SW, Bobko MA, Peng T, Miller WH, Pinckney T, Gallagher TF, Kulkarni S, Lewandowski T, Van Aller GS, Zonis R, Ward P, Campobasso N Bioorg Med Chem Lett. 2012 Jun 15;22(12):4028-32. Epub 2012 Apr 25. PMID:22579486[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Axten JM, Medina JR, Blackledge CW, Duquenne C, Grant SW, Bobko MA, Peng T, Miller WH, Pinckney T, Gallagher TF, Kulkarni S, Lewandowski T, Van Aller GS, Zonis R, Ward P, Campobasso N. Acylprolinamides: A new class of peptide deformylase inhibitors with in vivo antibacterial activity. Bioorg Med Chem Lett. 2012 Jun 15;22(12):4028-32. Epub 2012 Apr 25. PMID:22579486 doi:10.1016/j.bmcl.2012.04.086
