In:
Microbiology, Microbiology Society, Vol. 156, No. 10 ( 2010-10-01), p. 3194-3202
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.
Type of Medium:
Online Resource
ISSN:
1350-0872
,
1465-2080
DOI:
10.1099/mic.0.038174-0
Language:
English
Publisher:
Microbiology Society
Publication Date:
2010
detail.hit.zdb_id:
2008736-6
SSG:
12
