Cloning and sequencing of a cyclodextrin glycosyltransferase gene from Brevibacillus brevis CD162 and its expression in Escherichia coli
A cyclodextrin glycosyltransferase (CGTase) gene of Brevibacillus brevis CD162 was cloned into Escherichia coli using pUC19 as a vector. Determination of the nucleotide sequence showed the presence of an open reading frame of 2079 bp encoding a polypeptide of 693 amino acid residues, composed of a 2...
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| Veröffentlicht in: | FEMS microbiology letters 1998-07, Vol.164 (2), p.411-418 |
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| creator | Kim, M.H Sohn, C.B Oh, T.K |
| description | A cyclodextrin glycosyltransferase (CGTase) gene of Brevibacillus brevis CD162 was cloned into Escherichia coli using pUC19 as a vector. Determination of the nucleotide sequence showed the presence of an open reading frame of 2079 bp encoding a polypeptide of 693 amino acid residues, composed of a 20-amino acid signal sequence and a 673-amino acid mature enzyme. Neither a TATA- nor a TTGA-like sequence was observed within the cloned DNA fragment. However, the fragment was expressed in Escherichia coli by the lac promoter of pUC19 and 74% of the total activity was secreted into the fermentation medium. The amino acid sequence of the mature CGTase showed the highest homology of 86% to that of Bacillus sp. KC201. The CGTase purified to homogeneity from the recombinant E. coli exhibited the same properties as those of native CGTase from Brevibacillus brevis CD162 in terms of molecular mass, reaction conditions, stability and the production of cyclodextrins. |
| doi_str_mv | 10.1111/j.1574-6968.1998.tb13117.x |
| format | Article |
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Determination of the nucleotide sequence showed the presence of an open reading frame of 2079 bp encoding a polypeptide of 693 amino acid residues, composed of a 20-amino acid signal sequence and a 673-amino acid mature enzyme. Neither a TATA- nor a TTGA-like sequence was observed within the cloned DNA fragment. However, the fragment was expressed in Escherichia coli by the lac promoter of pUC19 and 74% of the total activity was secreted into the fermentation medium. The amino acid sequence of the mature CGTase showed the highest homology of 86% to that of Bacillus sp. KC201. The CGTase purified to homogeneity from the recombinant E. coli exhibited the same properties as those of native CGTase from Brevibacillus brevis CD162 in terms of molecular mass, reaction conditions, stability and the production of cyclodextrins.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.1998.tb13117.x</identifier><identifier>PMID: 9682490</identifier><identifier>CODEN: FMLED7</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Amino Acid Sequence ; Amino acids ; Bacillaceae - enzymology ; Bacillaceae - genetics ; Bacteriology ; Base Sequence ; Biological and medical sciences ; Biological Sciences ; Biology of microorganisms of confirmed or potential industrial interest ; Biotechnology ; Brevibacillus brevis ; Cloning ; Cloning, Molecular ; Cyclodextrin ; Cyclodextrin glycosyltransferase ; Cyclodextrin glycosyltransferase gene ; Cyclodextrins ; Deoxyribonucleic acid ; DNA ; E coli ; Enzyme Stability ; Escherichia coli ; Escherichia coli - enzymology ; Escherichia coli - genetics ; Fermentation ; food microbiology ; food processing ; Fundamental and applied biological sciences. Psychology ; genbank/af011388 ; Gene expression ; Gene sequencing ; Genetics ; Glucosyltransferases - chemistry ; Glucosyltransferases - genetics ; Glucosyltransferases - isolation & purification ; Glucosyltransferases - metabolism ; Glycosyltransferase ; Homology ; Hydrogen-Ion Concentration ; Microbiology ; Mission oriented research ; Molecular Sequence Data ; Molecular Weight ; Nucleotide sequence ; Nucleotides ; Plasmids ; Polypeptides ; Recombinant Proteins - chemistry ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - metabolism ; Restriction Mapping ; Sequence Analysis, DNA</subject><ispartof>FEMS microbiology letters, 1998-07, Vol.164 (2), p.411-418</ispartof><rights>1998 Federation of European Microbiological Societies 1998</rights><rights>1998 INIST-CNRS</rights><rights>1998 Federation of European Microbiological Societies</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4591-7709fd92c1635370bcaeaa466e4b4e2de8d048888e10aa080723f98693db714b3</citedby><cites>FETCH-LOGICAL-c4591-7709fd92c1635370bcaeaa466e4b4e2de8d048888e10aa080723f98693db714b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1574-6968.1998.tb13117.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1574-6968.1998.tb13117.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27903,27904,45553,45554</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=2367712$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9682490$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kim, M.H</creatorcontrib><creatorcontrib>Sohn, C.B</creatorcontrib><creatorcontrib>Oh, T.K</creatorcontrib><title>Cloning and sequencing of a cyclodextrin glycosyltransferase gene from Brevibacillus brevis CD162 and its expression in Escherichia coli</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Lett</addtitle><description>A cyclodextrin glycosyltransferase (CGTase) gene of Brevibacillus brevis CD162 was cloned into Escherichia coli using pUC19 as a vector. Determination of the nucleotide sequence showed the presence of an open reading frame of 2079 bp encoding a polypeptide of 693 amino acid residues, composed of a 20-amino acid signal sequence and a 673-amino acid mature enzyme. Neither a TATA- nor a TTGA-like sequence was observed within the cloned DNA fragment. However, the fragment was expressed in Escherichia coli by the lac promoter of pUC19 and 74% of the total activity was secreted into the fermentation medium. The amino acid sequence of the mature CGTase showed the highest homology of 86% to that of Bacillus sp. KC201. The CGTase purified to homogeneity from the recombinant E. coli exhibited the same properties as those of native CGTase from Brevibacillus brevis CD162 in terms of molecular mass, reaction conditions, stability and the production of cyclodextrins.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Bacillaceae - enzymology</subject><subject>Bacillaceae - genetics</subject><subject>Bacteriology</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Biological Sciences</subject><subject>Biology of microorganisms of confirmed or potential industrial interest</subject><subject>Biotechnology</subject><subject>Brevibacillus brevis</subject><subject>Cloning</subject><subject>Cloning, Molecular</subject><subject>Cyclodextrin</subject><subject>Cyclodextrin glycosyltransferase</subject><subject>Cyclodextrin glycosyltransferase gene</subject><subject>Cyclodextrins</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>E coli</subject><subject>Enzyme Stability</subject><subject>Escherichia coli</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli - genetics</subject><subject>Fermentation</subject><subject>food microbiology</subject><subject>food processing</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>genbank/af011388</subject><subject>Gene expression</subject><subject>Gene sequencing</subject><subject>Genetics</subject><subject>Glucosyltransferases - chemistry</subject><subject>Glucosyltransferases - genetics</subject><subject>Glucosyltransferases - isolation & purification</subject><subject>Glucosyltransferases - metabolism</subject><subject>Glycosyltransferase</subject><subject>Homology</subject><subject>Hydrogen-Ion Concentration</subject><subject>Microbiology</subject><subject>Mission oriented research</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Nucleotide sequence</subject><subject>Nucleotides</subject><subject>Plasmids</subject><subject>Polypeptides</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - metabolism</subject><subject>Restriction Mapping</subject><subject>Sequence Analysis, DNA</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1998</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqVUcuO0zAUjRBoKAOfgLAAsUvxK3bMAgnKDCAVsYBZW45z03Hlxh27mWn-gM_GoVUXCIS4G8s6j3uuTlE8J3hO8rxez0kleSmUqOdEqXq-awgjRM7394rZCbpfzDCTdUmwkg-LRymtMcacYnFWnGWYcoVnxY-FD73rV8j0LUpwM0Bvp2_okEF2tD60sN9F16OVH21Io99F06cOokmAVtAD6mLYoPcRbl1jrPN-SKiZfgktPhBBfzm7XUKw30ZIyYUeZbuLZK8hOnvt8p7g3ePiQWd8gifH97y4urz4vvhULr9-_Lx4tywtrxQppcSqaxW1RLCKSdxYA8ZwIYA3HGgLdYt5nQcINgbXWFLWqVoo1jaS8IadF68OvtsY8rVppzcuWfDe9BCGpGuMGadV9U8iERWvuMCZ-OI34joMsc9HaMoY4YLVnGbWmwPLxpBShE5vo9uYOGqC9dSqXuupOj1Vp6dW9bFVvc_ip8cVQ7OB9iQ91pjxl0fcJGt8lyuyLp1olAkpyZTh7YF25zyM_xFAX35ZckKyQXUwCMP2L_Lyz_mfHXSdCdqsYs529Y1iwjCtFaGVZD8BD9vYgA</recordid><startdate>19980715</startdate><enddate>19980715</enddate><creator>Kim, M.H</creator><creator>Sohn, C.B</creator><creator>Oh, T.K</creator><general>Blackwell Publishing Ltd</general><general>Blackwell</general><general>Oxford University Press</general><scope>FBQ</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>19980715</creationdate><title>Cloning and sequencing of a cyclodextrin glycosyltransferase gene from Brevibacillus brevis CD162 and its expression in Escherichia coli</title><author>Kim, M.H ; Sohn, C.B ; Oh, T.K</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4591-7709fd92c1635370bcaeaa466e4b4e2de8d048888e10aa080723f98693db714b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1998</creationdate><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Bacillaceae - enzymology</topic><topic>Bacillaceae - genetics</topic><topic>Bacteriology</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Biological Sciences</topic><topic>Biology of microorganisms of confirmed or potential industrial interest</topic><topic>Biotechnology</topic><topic>Brevibacillus brevis</topic><topic>Cloning</topic><topic>Cloning, Molecular</topic><topic>Cyclodextrin</topic><topic>Cyclodextrin glycosyltransferase</topic><topic>Cyclodextrin glycosyltransferase gene</topic><topic>Cyclodextrins</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>E coli</topic><topic>Enzyme Stability</topic><topic>Escherichia coli</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli - genetics</topic><topic>Fermentation</topic><topic>food microbiology</topic><topic>food processing</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>genbank/af011388</topic><topic>Gene expression</topic><topic>Gene sequencing</topic><topic>Genetics</topic><topic>Glucosyltransferases - chemistry</topic><topic>Glucosyltransferases - genetics</topic><topic>Glucosyltransferases - isolation & purification</topic><topic>Glucosyltransferases - metabolism</topic><topic>Glycosyltransferase</topic><topic>Homology</topic><topic>Hydrogen-Ion Concentration</topic><topic>Microbiology</topic><topic>Mission oriented research</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>Nucleotide sequence</topic><topic>Nucleotides</topic><topic>Plasmids</topic><topic>Polypeptides</topic><topic>Recombinant Proteins - chemistry</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Recombinant Proteins - metabolism</topic><topic>Restriction Mapping</topic><topic>Sequence Analysis, DNA</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kim, M.H</creatorcontrib><creatorcontrib>Sohn, C.B</creatorcontrib><creatorcontrib>Oh, T.K</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEMS microbiology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kim, M.H</au><au>Sohn, C.B</au><au>Oh, T.K</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cloning and sequencing of a cyclodextrin glycosyltransferase gene from Brevibacillus brevis CD162 and its expression in Escherichia coli</atitle><jtitle>FEMS microbiology letters</jtitle><addtitle>FEMS Microbiol Lett</addtitle><date>1998-07-15</date><risdate>1998</risdate><volume>164</volume><issue>2</issue><spage>411</spage><epage>418</epage><pages>411-418</pages><issn>0378-1097</issn><eissn>1574-6968</eissn><coden>FMLED7</coden><abstract>A cyclodextrin glycosyltransferase (CGTase) gene of Brevibacillus brevis CD162 was cloned into Escherichia coli using pUC19 as a vector. Determination of the nucleotide sequence showed the presence of an open reading frame of 2079 bp encoding a polypeptide of 693 amino acid residues, composed of a 20-amino acid signal sequence and a 673-amino acid mature enzyme. Neither a TATA- nor a TTGA-like sequence was observed within the cloned DNA fragment. However, the fragment was expressed in Escherichia coli by the lac promoter of pUC19 and 74% of the total activity was secreted into the fermentation medium. The amino acid sequence of the mature CGTase showed the highest homology of 86% to that of Bacillus sp. KC201. The CGTase purified to homogeneity from the recombinant E. coli exhibited the same properties as those of native CGTase from Brevibacillus brevis CD162 in terms of molecular mass, reaction conditions, stability and the production of cyclodextrins.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>9682490</pmid><doi>10.1111/j.1574-6968.1998.tb13117.x</doi><tpages>8</tpages></addata></record> |
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| identifier | ISSN: 0378-1097 |
| ispartof | FEMS microbiology letters, 1998-07, Vol.164 (2), p.411-418 |
| issn | 0378-1097 1574-6968 |
| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete; Oxford University Press Journals All Titles (1996-Current); Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Amino acids Bacillaceae - enzymology Bacillaceae - genetics Bacteriology Base Sequence Biological and medical sciences Biological Sciences Biology of microorganisms of confirmed or potential industrial interest Biotechnology Brevibacillus brevis Cloning Cloning, Molecular Cyclodextrin Cyclodextrin glycosyltransferase Cyclodextrin glycosyltransferase gene Cyclodextrins Deoxyribonucleic acid DNA E coli Enzyme Stability Escherichia coli Escherichia coli - enzymology Escherichia coli - genetics Fermentation food microbiology food processing Fundamental and applied biological sciences. Psychology genbank/af011388 Gene expression Gene sequencing Genetics Glucosyltransferases - chemistry Glucosyltransferases - genetics Glucosyltransferases - isolation & purification Glucosyltransferases - metabolism Glycosyltransferase Homology Hydrogen-Ion Concentration Microbiology Mission oriented research Molecular Sequence Data Molecular Weight Nucleotide sequence Nucleotides Plasmids Polypeptides Recombinant Proteins - chemistry Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Restriction Mapping Sequence Analysis, DNA |
| title | Cloning and sequencing of a cyclodextrin glycosyltransferase gene from Brevibacillus brevis CD162 and its expression in Escherichia coli |
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