期刊文献+

南极嗜冷假单胞菌7197S-腺苷同型半胱氨酸水解酶(SAHH)基因的克隆与序列分析 被引量:3

Analysis and Gene Cloning of the S-adenosylhomocysteine Hydrolase from Antarctic Psychrotrophilic Pseudomonas sp.7197 Strain
下载PDF
导出
摘要 从南极普利兹湾深海沉积物中筛选到一株耐冷菌株7197,其16S rDNA序列分析表明该菌株属于假单胞菌属(Pseu-domonas)。作者通过设计引物,从该菌的全基因组DNA中克隆到编码S-腺苷-L-高半胱氨酸(SAHH)的完整ORF,全长为1424bp。使用DNAMAN(5.1)软件对全长ORF为1424bp的SAHH基因进行分析,SAHH基因编码一个由474AA残基组成、分子量预计为52523 Da的SAHH蛋白质,与Psychrobacter sp.273-4的SAHH有96.84%的相似性;与Acinetobacter sp.ADP1的SAHH有79%的相似性;与Pseudomonas fluorescens Pf-5的SAHH有75%的相似性。 A strain 7197, which produces S - adenosyl - L - homocysteine hydrolase, was isolated from the deep sea sediment of Prydz Bay, Antarctic. The morphology identification and 16S rDNA sequence analysis showed that it belonged to genus Pseudomonas, The S- adenosylhomocysteine hydrolase gene was cloned by PCR according to the primers. Nucleotide sequence analysis revealed an open reading frame of 1424 bp encoding the SAHH, The amino acid sequence deduced from the nucleotide sequence of the SAHH gene corresponded to a protein of 474 amino acid residues with a molecular weight of 52,523 kDa, The SAHH shows a high sequence similarity to the SAHH gene from Psychrobacter sp, 273 - 4 and Acinetobacter sp. ADP1, with homologies of 96.84% and 79%, respectively, also show some sequence similarity to the SAHH gene from Pseudomonas fluorescens Pf- 5 with 75 % homologies.
出处 《现代生物医学进展》 CAS 2006年第4期5-7,共3页 Progress in Modern Biomedicine
基金 国家自然科学青年基金资助(No.40406029)~~
关键词 嗜冷假单胞菌 S-腺苷同型半胱氨酸水解酶 克隆 序列分析 Psychrotrophilic Pseudomonas S - adenosyl - L- homocysteine hydrolase gene cloning sequence analysis
  • 相关文献

参考文献12

  • 1Cantoni JL.Biological methylation:selected aspects[J].Annu.Rev.Biochem,1975,44:435-451
  • 2沈萍,范秀容,李广武.微生物学实验[M].第三版.北京:高等教育出版社,1996:69-73
  • 3Sambrook J,Frisch EF,Maniatis T.Molecular Cloning:A Laboratory Manual.2nd ed[M].New York:Cold Spring Harbor Laboratory Press,1989
  • 4Fred A,Roger B,Robert EK,et al.Short Protocols in Molecular Biology,3rd ed[M].John Wiley & Sons Inc,1995
  • 5林念炜,张锐,赵晶,曾润颖.南极产低温蛋白酶菌株Marinobacter sp.R2的发酵条件及酶学性质研究[J].厦门大学学报(自然科学版),2004,43(6):865-869. 被引量:24
  • 6张金伟,曾润颖.南极产低温脂肪酶菌株Psychrobacter sp.7195的选育、发酵条件及酶学性质研究[J].生物磁学,2006,6(1):6-10. 被引量:17
  • 7Sganga MW,Aksamit RR,Cantoni GL,et al.Mutational and nucleotide sequence analysis of S-adenosyl-L-homocysteine hydrolase from Rhodobacter capsulatus.Proc.Natl.Acad.Sci.USA,1992,89:6328-6332
  • 8[英]W.费迪南德.酶分子[M].北京:科学出版社,1985:102-127
  • 9De Clercq E.S-Adenosylhomocysteine hydrolase inhibitors as broad-spectrum antiviral agents[J].Biochem.Pharm,1987,36:2567-2575
  • 10Chian PK.Biological effects of inhibitors of S-adenosylhomocysteine hydrolase[J].Pharmacol.Ther,1998,77:115-134

二级参考文献29

  • 1林念炜,张锐,赵晶,曾润颖.南极产低温蛋白酶菌株Marinobacter sp.R2的发酵条件及酶学性质研究[J].厦门大学学报(自然科学版),2004,43(6):865-869. 被引量:24
  • 2邱秀宝,高东,王颖达.短小芽孢杆菌碱性蛋白酶BP的纯化和性质[J].微生物学报,1994,34(4):293-300. 被引量:25
  • 3沈萍.微生物学实验[M].北京:高等教育出版社,1996..
  • 4JP Bowman,SA Mccammon,MV Browm,et al.Diversity and association of psychrophilic bacteria in Antarctic sea ice[J].Appl Environ Microbiol,1997,63:3068-3078
  • 5Russell N,Toward J.A molecular understanding of cold activity of enzymes from psychrophiles[J].Extremophiles,2000,4,83-90
  • 6Choo DW,Kurihara T,Suzuki T,et al.A Cold-adapted lipase of an Alaskan psychrotroph,Pseudomonas sp.strain B11-1:gene cloning and enzyme purification and characterization[J].Appl Environ Microbiol,1998,64:486-491
  • 7Fujita M,Torigoe K,Nakada T.Cloning and nucleotide sequence of the gene(amyP)for maltotetraose-forming amylase from Pseudomonas stutzeri MO-19[J].J Bacterial,1989,171:1333-1339
  • 8Harwood,J.The versatility of lipases for industrial uses[J].Trends Biochem.Sci.,1989,14:125-126
  • 9Inagaki M,Hiratake J,Nishioka T,et al.Lipase-catalyzed stereoselective acylation of[1,1'-binaphthyl]-2,2'-diol and deacylation of its esters in an organic solvent[J].Agric.Biol.Chem.,1989,53:1879-1884
  • 10Rashid N,Shimada Y,Ezaki S,et al.Low-temperature lipase from psychrotrophic Pseudomonas sp.strain KB700A[J].Appl Environ Microbiol,2000,67(9):4064-4069

共引文献39

同被引文献25

引证文献3

二级引证文献2

相关作者

内容加载中请稍等...

相关机构

内容加载中请稍等...

相关主题

内容加载中请稍等...

浏览历史

内容加载中请稍等...
;
使用帮助 返回顶部