A new beta-hydroxyacyl-acyl carrier protein dehydratase (FabZ) from Helicobacter pylori: Molecular cloning, enzymatic characterization, and structural modeling
文献类型:期刊论文
作者 | Liu, WZ; Luo, C![]() ![]() ![]() ![]() |
刊名 | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
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出版日期 | 2005-08-12 |
卷号 | 333期号:4页码:1078-1086 |
关键词 | fatty acid biosynthesis Helicobacter pylori beta-hydroxyacyl-acyl carrier protein dehydratase (FabZ) molecular cloning unfolding structural modeling |
ISSN号 | 0006-291X |
DOI | 10.1016/j.bbrc.2005.05.197 |
文献子类 | Article |
英文摘要 | Helicobacter pylori is a gram-negative pathogenic bacterium that causes peptic ulcer disease and gastric cancer, and studies of the related potent enzymes associated with this bacterium are urgent for the discovery of novel drug targets. In bacteria, beta-hydroxyacyl-acyl carrier protein (ACP) dehydratase (FabZ) is a potent enzyme in fatty acid biosynthesis and catalyzes the dehydration of beta-hydroxyacyl-ACP to trans-2-acyl-ACP. In this study, the cloning and enzymatic characterization of FabZ from H. pylori strain SS1 (HpFabZ) were reported, and the gene sequence of HpfabZ was deposited in the GenBank database (Accession No. AY725427). Enzyme dynamic analysis showed that HpFabZ had a K-m of 82.6 +/- 4.3 mu M toward its substrate analog crotonoyl-CoA. Dynamic light scattering and native-PAGE investigations suggested that HpFabZ exists as hexamer in native state. Enzymatic characterization and thermal-induced unfolding analysis based on circular dichroism spectral measurements indicated that HpFabZ is very stable against high temperature (90 degrees C). Such a high stability of HpFabZ was well elucidated by the strong H-bonds and hydrophobic interactions among the HpFabZ hexamer as investigated in the modeled HpFabZ hexamer structure. Our current study is hoped to provide useful information in better understanding the FabZ of H. pylori strain and further supply possible hints in the discovery of anti-bacterial compounds using HpFabZ as target. (c) 2005 Elsevier Inc. All rights reserved. |
WOS关键词 | FATTY-ACID BIOSYNTHESIS ; ESCHERICHIA-COLI ; PLASMODIUM-FALCIPARUM ; TARGETS |
WOS研究方向 | Biochemistry & Molecular Biology ; Biophysics |
语种 | 英语 |
WOS记录号 | WOS:000230538900006 |
出版者 | ACADEMIC PRESS INC ELSEVIER SCIENCE |
源URL | [http://119.78.100.183/handle/2S10ELR8/273818] ![]() |
专题 | 药理学第三研究室 药物发现与设计中心 |
通讯作者 | Shen, X |
作者单位 | 1.E China Univ Sci & Technol, Sch Pharm, Shanghai 200237, Peoples R China 2.Chinese Acad Sci, Shanghai Inst Mat Med, Drug Discovery & Design Ctr,State Key Lab Drug Re, Shanhai Inst Biol Sci,Grad Sch, Shanghai 201203, Peoples R China |
推荐引用方式 GB/T 7714 | Liu, WZ,Luo, C,Han, C,et al. A new beta-hydroxyacyl-acyl carrier protein dehydratase (FabZ) from Helicobacter pylori: Molecular cloning, enzymatic characterization, and structural modeling[J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,2005,333(4):1078-1086. |
APA | Liu, WZ.,Luo, C.,Han, C.,Peng, SY.,Yang, YM.,...&Jiang, HL.(2005).A new beta-hydroxyacyl-acyl carrier protein dehydratase (FabZ) from Helicobacter pylori: Molecular cloning, enzymatic characterization, and structural modeling.BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,333(4),1078-1086. |
MLA | Liu, WZ,et al."A new beta-hydroxyacyl-acyl carrier protein dehydratase (FabZ) from Helicobacter pylori: Molecular cloning, enzymatic characterization, and structural modeling".BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 333.4(2005):1078-1086. |
入库方式: OAI收割
来源:上海药物研究所
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