Characterization of peptide deformylase homologues from Staphylococcus epidermidis | |
Lin, Penghui4,5,6; Hu, Tiancen1; Hu, Jian4,5,6; Yu, Wenqi4,5,6; Han, Cong4,5,6; Zhang, Jian3; Qin, Guangrong1; Yu, Kunqian1![]() ![]() | |
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. |
个性服务 |
查看访问统计 |
相关权益政策 |
暂无数据 |
收藏/分享 |
除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。
修改评论