Characterization of peptide deformylase homologues from Staphylococcus epidermidis

doi:10.1099/mic.0.038174-0

CORC > 上海药物研究所 > 中国科学院上海药物研究所 > 药理学第三研究室

	Characterization of peptide deformylase homologues from Staphylococcus epidermidis
	Lin, Penghui 4,5,6; Hu, Tiancen 1; Hu, Jian 4,5,6; Yu, Wenqi 4,5,6; Han, Cong 4,5,6; Zhang, Jian 3; Qin, Guangrong 1; Yu, Kunqian1 ; Goetz, Friedrich 2; Shen, Xu1
刊名	MICROBIOLOGY-SGM
	2010-10
卷号	156 页码:3194-3202
ISSN号	1350-0872
DOI	10.1099/mic.0.038174-0
文献子类	Article
英文摘要	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 6.3x10(4) 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.
资助项目	Ministry of Science and Technology of China[2009ZX09303-005] ; Ministry of Science and Technology of China[2010DFA32100] ; Ministry of Science and Technology of China[2008ZX10003-016] ; National Natural Science Foundation of China[30800036] ; Scientific Technology Development Foundation of Shanghai[08JC1401600] ; Scientific Technology Development Foundation of Shanghai[10410700600] ; High-Tech Research and Development Program of China[2006AA02A253] ; High-Tech Research and Development Program of China[2006AA01A124] ; High-Tech Research and Development Program of China[2009AA01A137]
WOS关键词	COAGULASE-NEGATIVE STAPHYLOCOCCI ; BACTERIUM LEPTOSPIRA-INTERROGANS ; ESCHERICHIA-COLI ; CRYSTAL-STRUCTURE ; ACTIVE-SITE ; POLYPEPTIDE DEFORMYLASE ; PLASMODIUM-FALCIPARUM ; HELICOBACTER-PYLORI ; METAL-ION ; TARGET
WOS研究方向	Microbiology
语种	英语
出版者	MICROBIOLOGY SOC
WOS记录号	WOS:000283454100029
内容类型	期刊论文
源URL	[http://119.78.100.183/handle/2S10ELR8/278764]
专题	药理学第三研究室药物发现与设计中心
通讯作者	Qu, Di
作者单位	1.Chinese Acad Sci, Shanghai Inst Mat Med, Shanghai Inst Biol Sci, Drug Discovery & Design Ctr,State Key Lab Drug Re, Shanghai 201203, Peoples R China; 2.Univ Tubingen, D-72076 Tubingen, Germany 3.Shanghai Jiao Tong Univ, Key Lab Cell Differentiat & Apoptosis, Minist Educ China, Dept Pathophysiol,Sch Med, Shanghai 200025, Peoples R China; 4.Fudan Univ, Shanghai Med Coll, Inst Med Microbiol, Key Lab Med Mol Virol,Minist Educ, Shanghai 200032, Peoples R China; 5.Fudan Univ, Shanghai Med Coll, Inst Med Microbiol, Key Lab Med Mol Virol,Minist Hlth, Shanghai 200032, Peoples R China; 6.Fudan Univ, Shanghai Med Coll, Inst Biomed Sci, Shanghai 200032, Peoples R China;
推荐引用方式 GB/T 7714	Lin, Penghui,Hu, Tiancen,Hu, Jian,et al. Characterization of peptide deformylase homologues from Staphylococcus epidermidis[J]. MICROBIOLOGY-SGM,2010,156:3194-3202.
APA	Lin, Penghui.,Hu, Tiancen.,Hu, Jian.,Yu, Wenqi.,Han, Cong.,...&Qu, Di.(2010).Characterization of peptide deformylase homologues from Staphylococcus epidermidis.MICROBIOLOGY-SGM,156,3194-3202.
MLA	Lin, Penghui,et al."Characterization of peptide deformylase homologues from Staphylococcus epidermidis".MICROBIOLOGY-SGM 156(2010):3194-3202.