| Structural highlights
Function
[DEF_MYCTU] 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).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Bacterial peptide deformylase (PDF) belongs to a subfamily of metalloproteases catalyzing the removal of the N-terminal formyl group from newly synthesized proteins. We report the synthesis and biological activity of highly potent inhibitors of Mycobacterium tuberculosis (Mtb) PDF enzyme as well as the first X-ray crystal structure of Mtb PDF. Structure-activity relationship and crystallographic data clarified the structural requirements for high enzyme potency and cell based potency. Activities against single and multi-drug-resistant Mtb strains are also reported.
Peptide deformylase inhibitors of Mycobacterium tuberculosis: synthesis, structural investigations, and biological results.,Pichota A, Duraiswamy J, Yin Z, Keller TH, Alam J, Liung S, Lee G, Ding M, Wang G, Chan WL, Schreiber M, Ma I, Beer D, Ngew X, Mukherjee K, Nanjundappa M, Teo JW, Thayalan P, Yap A, Dick T, Meng W, Xu M, Koehn J, Pan SH, Clark K, Xie X, Shoen C, Cynamon M Bioorg Med Chem Lett. 2008 Dec 15;18(24):6568-72. Epub 2008 Oct 14. PMID:19008098[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Pichota A, Duraiswamy J, Yin Z, Keller TH, Alam J, Liung S, Lee G, Ding M, Wang G, Chan WL, Schreiber M, Ma I, Beer D, Ngew X, Mukherjee K, Nanjundappa M, Teo JW, Thayalan P, Yap A, Dick T, Meng W, Xu M, Koehn J, Pan SH, Clark K, Xie X, Shoen C, Cynamon M. Peptide deformylase inhibitors of Mycobacterium tuberculosis: synthesis, structural investigations, and biological results. Bioorg Med Chem Lett. 2008 Dec 15;18(24):6568-72. Epub 2008 Oct 14. PMID:19008098 doi:10.1016/j.bmcl.2008.10.040
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