Molecular cloning and characterization of a new peptide deformylase from human pathogenic bacterium Helicobacter pylori
文献类型：期刊论文
| 作者 | Han, C; Wang, Q; Dong, L; Sun, HF; Peng, SY; Chen, J ; Yang, YM; Yue, JM; Shen, X; Jiang, HL
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| 刊名 | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
 |
| 出版日期 | 2004-07-09 |
| 卷号 | 319期号:4页码:1292-1298 |
| 关键词 | peptide deformylase Helicobacter pylori enzymatic properties antimicrobial agents drug target |
| ISSN号 | 0006-291X |
| DOI | 10.1016/j.bbrc.2004.05.120 |
| 文献子类 | Article |
| 英文摘要 | Helicobacter pylori is a gram-negative pathogenic bacterium, which is associated with peptic ulcer disease and gastric cancer. It is urgent to discover novel drug targets for appropriate antimicrobial agents against this human pathogen. In bacteria, peptide deformylase (PDF) catalyzes the removal of a formyl group from the N-termini of nascent polypeptides. Due to its essentiality and absence in mammalian cells, PDF has been considered as an attractive target for the discovery of novel antibiotics. In this work, a new PDF gene (def) from H. pylori strain SS1 was cloned, expressed, and purified in Escherichia coli system. Sequence alignment shows that H. pylori PDF (HpPDF) shares about 40% identity to E. coli PDF (EcPDF). The enzymatic properties of HpPDF demonstrate its relatively high activity toward formyl-Met-Ala-Ser, with K-cat of 3.4 s(-1) K-m of 1.7 mM, and K-cat/K-m of 2000 M-1 s(-1). HpPDF enzyme appears to be fully active at pH between 8.0 and 9.0, and temperature 50degreesC. The enzyme activity of Co2+-containing HpPDF is apparently higher than that of Zn2+-containing HpPDF. This present work thereby supplies a potential platform that facilitates the discovery of novel HpPDF inhibitors and further of possible antimicrobial agents against H. pylori. (C) 2004 Elsevier Inc. All rights reserved. |
| WOS关键词 | ESCHERICHIA-COLI ; DRUG DESIGN ; LEPTOSPIRA-INTERROGANS ; PLASMODIUM-FALCIPARUM ; ANTIMICROBIAL AGENTS ; ENZYMATIC-PROPERTIES ; CRYSTAL-STRUCTURE ; ACTIVE-SITE ; METAL-ION ; IDENTIFICATION |
| WOS研究方向 | Biochemistry & Molecular Biology ; Biophysics |
| 语种 | 英语 |
| WOS记录号 | WOS:000222318700033 |
| 出版者 | ACADEMIC PRESS INC ELSEVIER SCIENCE |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/274048]  |
| 专题 | 药理学第三研究室 中科院受体结构与功能重点实验室 新药研究国家重点实验室 药物发现与设计中心 |
| 通讯作者 | Shen, X |
| 作者单位 | Chinese Acad Sci, Grad Sch,Drug Discovery & Design Ctr, Shanghai Inst Biol Sci, Shanghai Inst Mat Med,State Key Lab Drug Res, Shanghai 201203, Peoples R China |
| 推荐引用方式 GB/T 7714 | Han, C,Wang, Q,Dong, L,et al. Molecular cloning and characterization of a new peptide deformylase from human pathogenic bacterium Helicobacter pylori[J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,2004,319(4):1292-1298. |
| APA | Han, C.,Wang, Q.,Dong, L.,Sun, HF.,Peng, SY.,...&Jiang, HL.(2004).Molecular cloning and characterization of a new peptide deformylase from human pathogenic bacterium Helicobacter pylori.BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,319(4),1292-1298. |
| MLA | Han, C,et al."Molecular cloning and characterization of a new peptide deformylase from human pathogenic bacterium Helicobacter pylori".BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 319.4(2004):1292-1298. |
入库方式： OAI收割
来源：上海药物研究所
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