@article{mbs:/content/journal/micro/10.1099/mic.0.038174-0, author = "Lin, Penghui and Hu, Tiancen and Hu, Jian and Yu, Wenqi and Han, Cong and Zhang, Jian and Qin, Guangrong and Yu, Kunqian and Götz, Friedrich and Shen, Xu and Jiang, Hualiang and Qu, Di", title = "Characterization of peptide deformylase homologues from Staphylococcus epidermidis", journal= "Microbiology", year = "2010", volume = "156", number = "10", pages = "3194-3202", doi = "https://doi.org/10.1099/mic.0.038174-0", url = "https://www.microbiologyresearch.org/content/journal/micro/10.1099/mic.0.038174-0", publisher = "Microbiology Society", issn = "1465-2080", type = "Journal Article", keywords = "PDF, peptide deformylase", keywords = "RMSD, root-mean-square distance", keywords = "f-MAS, N-formyl-Met-Ala-Ser", keywords = "FDH, formate dehydrogenase", 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. Co2+-substituted SePDF-1 exhibited much higher enzymic activity (k cat/K m 6.3×104 M−1 s−1) than those of Ni2+- and Zn2+-substituted SePDF-1, and SePDF-1 showed much weaker binding ability towards Ni2+ than towards Co2+ and Zn2+, 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.", }