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Cloning and characterization of a leucine aminopeptidase from Pseudoalteromonas telluritireducens DSM 16098, a strain isolated from hydrothermal vents fluid

文献类型：期刊论文

作者Zhang, Huan1,4; Wang, Hao1,4; Liu, Rui2,4; Wang, Lingling3; Song, Linsheng3
刊名DEEP-SEA RESEARCH PART I-OCEANOGRAPHIC RESEARCH PAPERS
出版日期2018-08-01
卷号138页码:114-121
ISSN号0967-0637
关键词Leucine aminopeptidases Pseudoalteromonas telluritireducens Recombinant protein Enzyme activity Cell proliferation
DOI10.1016/j.dsr.2018.06.006
通讯作者Wang, Hao(haowang@qdio.ac.cn) ; Wang, Lingling(wanglingling@dlou.edu.cn)
英文摘要Microbes living around hydrothermal vents have developed lots of enzymes with specific characteristics that allow them to thrive in the environment. Extracellular enzyme leucine aminopeptidases (LAPs) are all metallopeptidases that catalyze the hydrolysis of leucine residues from N-terminal residues from peptides and proteins. Genomic analysis of Pseudoalteromonas telluritireducens DSM 16098, a strain of deep-sea bacteria isolated from hydrothermal vents fluid, revealed the presence of an LAP gene (designated as PtLAP). The open reading frame of PtLAP encodes a protein of 614 amino acids (GenBank accession no. KY429939), consisting of a signal peptide, a peptidase_M1 domain and a leuk-A4-hydro_C domain. The putative substrate binding site GGMEN, zinc-binding motif HEXXHX18E and the catalytic residues involved in aminopeptidase activity are all conserved, indicating PtLAP is a member of M1 leucine aminopeptidases. The recombinant PtLAP expressed in Escherichia coli Transetta (DE3) (designated as rPtLAP) exhibits a significant LAP activity to hydrolyze L-leucine 7-amido-4-methylcoumarin (MAC-L). The optimal activity of rPtLAP is observed at pH 7.2 and 28 degrees C with half-saturation coefficient (K-m) of 44.56 +/- 5.09 mu mol L-1. rPtLAP activity is relatively stable at 30-40 degrees C and exhibits a relatively wide pH range (6.0-12.5) with the maximal activity ranging at pH 7.2-8.0. It can be inhibited by EDTA, protease inhibitors and some metal ions including Cu2+, Zn2+ and Cd2+, but is relatively tolerant to Mn2+ which is enriched in hydrothermal vent fluids. Furthermore, rPtLAP can significantly promote the proliferation of tumor cells, including the cell lines HCT116, BEL-7402 and Hela, while displays no effect on that of normal cell 3T3. These results together suggest that the extracellular enzyme PtLAP executes the degradation of organic matters, contributes to the adaptive survival of microbe in deep-sea environment and may play important roles in marine biogeochemical cycles.
资助项目Chinese Academy of Sciences[XDA11030202] ; Chinese Ministry of Science and Technology[2014AA093501]
WOS研究方向Oceanography
语种英语
出版者PERGAMON-ELSEVIER SCIENCE LTD
WOS记录号WOS:000445985100010
源URL[http://ir.qdio.ac.cn/handle/337002/160398]  
专题海洋研究所_实验海洋生物学重点实验室
通讯作者Wang, Hao; Wang, Lingling
作者单位1.Chinese Acad Sci, Inst Oceanol, Ctr Deep Sea Res, 7 Nanhai Rd, Qingdao 266071, Peoples R China
2.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, 7 Nanhai Rd, Qingdao 266071, Peoples R China
3.Dalian Ocean Univ, Liaoning Key Lab Marine Anim Immunol, 52 Heishijiao St, Dalian 116023, Peoples R China
4.Chinese Acad Sci, Ctr Ocean Megasci, 7 Nanhai Rd, Qingdao 266071, Peoples R China
推荐引用方式
GB/T 7714		 Zhang, Huan,Wang, Hao,Liu, Rui,et al. Cloning and characterization of a leucine aminopeptidase from Pseudoalteromonas telluritireducens DSM 16098, a strain isolated from hydrothermal vents fluid[J]. DEEP-SEA RESEARCH PART I-OCEANOGRAPHIC RESEARCH PAPERS,2018,138:114-121.
APA Zhang, Huan,Wang, Hao,Liu, Rui,Wang, Lingling,&Song, Linsheng.(2018).Cloning and characterization of a leucine aminopeptidase from Pseudoalteromonas telluritireducens DSM 16098, a strain isolated from hydrothermal vents fluid.DEEP-SEA RESEARCH PART I-OCEANOGRAPHIC RESEARCH PAPERS,138,114-121.
MLA Zhang, Huan,et al."Cloning and characterization of a leucine aminopeptidase from Pseudoalteromonas telluritireducens DSM 16098, a strain isolated from hydrothermal vents fluid".DEEP-SEA RESEARCH PART I-OCEANOGRAPHIC RESEARCH PAPERS 138(2018):114-121.

入库方式： OAI收割

来源：海洋研究所

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