A new beta-hydroxyacyl-acyl carrier protein dehydratase (FabZ) from Helicobacter pylori: Molecular cloning, enzymatic characterization, and structural modeling

doi:10.1016/j.bbrc.2005.05.197

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	A new beta-hydroxyacyl-acyl carrier protein dehydratase (FabZ) from Helicobacter pylori: Molecular cloning, enzymatic characterization, and structural modeling
	Liu, WZ ; Luo, C; Han, C ; Peng, SY ; Yang, YM ; Yue, JM; Shen, X; Jiang, HL
刊名	BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
	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
出版者	ACADEMIC PRESS INC ELSEVIER SCIENCE
WOS记录号	WOS:000230538900006
内容类型	期刊论文
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.