Structural highlights
Function
[DEF_PSEAE] 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
Screening of our compound collection using Staphylococcus aureus Ni-Peptide deformylase (PDF) afforded a very potent PDF inhibitor with an IC(50) in the low nanomolar range but with poor antibacterial activity (MIC). Three-dimensional structural information obtained from Pseudomonas aeruginosa Ni-PDF complexed with the inhibitor suggested the synthesis of a variety of analogues that would maintain high binding affinity while attempting to improve antibacterial activity. Many of the compounds synthesized proved to be excellent PDF-Ni inhibitors and some showed increased antibacterial activity in selected strains.
Identification of novel potent bicyclic peptide deformylase inhibitors.,Molteni V, He X, Nabakka J, Yang K, Kreusch A, Gordon P, Bursulaya B, Warner I, Shin T, Biorac T, Ryder NS, Goldberg R, Doughty J, He Y Bioorg Med Chem Lett. 2004 Mar 22;14(6):1477-81. PMID:15006385[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Molteni V, He X, Nabakka J, Yang K, Kreusch A, Gordon P, Bursulaya B, Warner I, Shin T, Biorac T, Ryder NS, Goldberg R, Doughty J, He Y. Identification of novel potent bicyclic peptide deformylase inhibitors. Bioorg Med Chem Lett. 2004 Mar 22;14(6):1477-81. PMID:15006385 doi:10.1016/j.bmcl.2004.01.014
