Characterization of peptide deformylase homologues from Staphylococcus epidermidis

Microbiology
Penghui LinDi Qu

Abstract

The emergence of multi-drug-resistant strains of Staphylococcus epidermidis emphasizes the need to develop new antibiotics. The unique and essential role of the peptide deformylase (PDF) in catalysing the removal of the N-terminal formyl group from newly synthesized polypeptides in eubacteria makes it an attractive antibacterial drug target. In the present study, both deformylase homologues from S. epidermidis (SePDF-1 and SePDF-2) were cloned and expressed, and their enzymic activities were characterized. Co(2+)-substituted SePDF-1 exhibited much higher enzymic activity (k(cat)/K(m) 6.3 × 10(4) M(-1) s(-1)) than those of Ni(2+)- and Zn(2+)-substituted SePDF-1, and SePDF-1 showed much weaker binding ability towards Ni(2+) than towards Co(2+) and Zn(2+), which is different from PDF in Staphylococcus aureus (SaPDF), although they share 80 % amino-acid sequence identity. The determined crystal structure of SePDF-1 was similar to that of (SaPDF), except for differences in the metal-binding sites. The other deformylase homologue, SePDF-2, was shown to have no peptide deformylase activity; the function of SePDF-2 needs to be further investigated.

References

May 14, 1968·Journal of Molecular Biology·J M Adams
Nov 24, 1995·Journal of Molecular Biology·T MeinnelS Blanquet
Aug 1, 1994·Clinical Infectious Diseases : an Official Publication of the Infectious Diseases Society of America·M E Rupp, G L Archer
Jan 1, 1997·Analytical Biochemistry·C Lazennec, T Meinnel
Dec 31, 1997·Biochemistry·M K ChanD Pei
Jun 13, 1998·The Journal of Biological Chemistry·A BeckerA F Wagner
Jul 17, 1998·Journal of Molecular Biology·S RagusaT Meinnel
Aug 11, 1998·Trends in Biochemical Sciences·R A BradshawK W Walker
Oct 3, 1998·Acta Crystallographica. Section D, Biological Crystallography·A T BrüngerG L Warren
Mar 21, 2001·Antimicrobial Agents and Chemotherapy·C M ApfelW Keck
Dec 19, 2001·Archives of Biochemistry and Biophysics·V Bracchi-RicardD Pei
Apr 16, 2002·Molecular Microbiology·Friedrich Götz
Jun 6, 2002·The Journal of Biological Chemistry·Eric T BaldwinMartin R Deibel
Jul 20, 2002·Biochemical and Biophysical Research Communications·Yikun LiWeimin Gong
Nov 1, 2002·The Lancet Infectious Diseases·Christof von EiffChristine Heilmann
Jan 23, 2003·Protein Science : a Publication of the Protein Society·Kathrine J SmithSiegfried B Christensen
Oct 9, 2003·The Journal of Biological Chemistry·Alexandre SereroThierry Meinnel
Mar 11, 2004·Protein Science : a Publication of the Protein Society·Mark A RobienWim G J Hol
Jun 15, 2004·Biochemical and Biophysical Research Communications·Cong HanHualiang Jiang
May 1, 1997·Acta Crystallographica. Section D, Biological Crystallography·G N MurshudovE J Dodson
Dec 2, 2004·Acta Crystallographica. Section D, Biological Crystallography·Paul Emsley, Kevin Cowtan
Sep 12, 2006·Molecular & Cellular Proteomics : MCP·Frédéric FrottinThierry Meinnel
Oct 31, 2007·Antimicrobial Agents and Chemotherapy·Mrinalini SharmaPietro Speziale
Nov 6, 2007·Archives of Biochemistry and Biophysics·Kiet T NguyenDehua Pei
Feb 25, 2009·Journal of Molecular Biology·Sindy Escobar-AlvarezDavid A Scheinberg
Jun 18, 2009·Expert Opinion on Therapeutic Targets·Anshika SharmaSadhna Sharma

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