Isolation and Characterization of a Novel Lysine Racemase from a Soil Metagenomic Library
A lysine racemase (lyr) gene was isolated from a soil metagenome by functional complementation for the first time by using Escherichia coli BCRC 51734 cells as the host and D-lysine as the selection agent. The lyr gene consisted of a 1,182-bp nucleotide sequence encoding a protein of 393 amino acids...
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| Veröffentlicht in: | Applied and Environmental Microbiology 2009-08, Vol.75 (15), p.5161-5166 |
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| container_title | Applied and Environmental Microbiology |
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| creator | Chen, I. Chien Lin, Wei-De Hsu, Shin-Kuang Thiruvengadam, Venkatesan Hsu, Wen-Hwei |
| description | A lysine racemase (lyr) gene was isolated from a soil metagenome by functional complementation for the first time by using Escherichia coli BCRC 51734 cells as the host and D-lysine as the selection agent. The lyr gene consisted of a 1,182-bp nucleotide sequence encoding a protein of 393 amino acids with a molecular mass of about 42.7 kDa. The enzyme exhibited higher specific activity toward lysine in the L-lysine-to-D-lysine direction than in the reverse reaction. |
| doi_str_mv | 10.1128/AEM.00074-09 |
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Chien ; Lin, Wei-De ; Hsu, Shin-Kuang ; Thiruvengadam, Venkatesan ; Hsu, Wen-Hwei</creator><creatorcontrib>Chen, I. Chien ; Lin, Wei-De ; Hsu, Shin-Kuang ; Thiruvengadam, Venkatesan ; Hsu, Wen-Hwei</creatorcontrib><description>A lysine racemase (lyr) gene was isolated from a soil metagenome by functional complementation for the first time by using Escherichia coli BCRC 51734 cells as the host and D-lysine as the selection agent. The lyr gene consisted of a 1,182-bp nucleotide sequence encoding a protein of 393 amino acids with a molecular mass of about 42.7 kDa. The enzyme exhibited higher specific activity toward lysine in the L-lysine-to-D-lysine direction than in the reverse reaction.</description><identifier>ISSN: 0099-2240</identifier><identifier>EISSN: 1098-5336</identifier><identifier>EISSN: 1098-6596</identifier><identifier>DOI: 10.1128/AEM.00074-09</identifier><identifier>PMID: 19502445</identifier><identifier>CODEN: AEMIDF</identifier><language>eng</language><publisher>Washington, DC: American Society for Microbiology</publisher><subject>Amino Acid Isomerases - chemistry ; Amino Acid Isomerases - genetics ; Amino Acid Isomerases - metabolism ; Amino Acid Sequence ; Amino acids ; Base Sequence ; Biological and medical sciences ; Cations, Divalent - pharmacology ; Cells ; Cloning, Molecular ; Coenzymes - pharmacology ; DNA, Bacterial - chemistry ; DNA, Bacterial - genetics ; E coli ; Enzymology and Protein Engineering ; Escherichia coli ; Escherichia coli - genetics ; Fundamental and applied biological sciences. Psychology ; Gene expression ; Gene Library ; Genetic Complementation Test ; Lysine - metabolism ; Microbiology ; Molecular Sequence Data ; Molecular Weight ; Proteins ; Sequence Analysis, DNA ; Soil Microbiology</subject><ispartof>Applied and Environmental Microbiology, 2009-08, Vol.75 (15), p.5161-5166</ispartof><rights>2009 INIST-CNRS</rights><rights>Copyright American Society for Microbiology Aug 2009</rights><rights>Copyright © 2009, American Society for Microbiology</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c587t-ab17bac65dc546b548f77476e75024ca384d45b65cd672509bcc69f7cfcfe28f3</citedby><cites>FETCH-LOGICAL-c587t-ab17bac65dc546b548f77476e75024ca384d45b65cd672509bcc69f7cfcfe28f3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2725492/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2725492/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,3188,3189,27924,27925,53791,53793</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=21798126$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19502445$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Chen, I. Chien</creatorcontrib><creatorcontrib>Lin, Wei-De</creatorcontrib><creatorcontrib>Hsu, Shin-Kuang</creatorcontrib><creatorcontrib>Thiruvengadam, Venkatesan</creatorcontrib><creatorcontrib>Hsu, Wen-Hwei</creatorcontrib><title>Isolation and Characterization of a Novel Lysine Racemase from a Soil Metagenomic Library</title><title>Applied and Environmental Microbiology</title><addtitle>Appl Environ Microbiol</addtitle><description>A lysine racemase (lyr) gene was isolated from a soil metagenome by functional complementation for the first time by using Escherichia coli BCRC 51734 cells as the host and D-lysine as the selection agent. The lyr gene consisted of a 1,182-bp nucleotide sequence encoding a protein of 393 amino acids with a molecular mass of about 42.7 kDa. The enzyme exhibited higher specific activity toward lysine in the L-lysine-to-D-lysine direction than in the reverse reaction.</description><subject>Amino Acid Isomerases - chemistry</subject><subject>Amino Acid Isomerases - genetics</subject><subject>Amino Acid Isomerases - metabolism</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Cations, Divalent - pharmacology</subject><subject>Cells</subject><subject>Cloning, Molecular</subject><subject>Coenzymes - pharmacology</subject><subject>DNA, Bacterial - chemistry</subject><subject>DNA, Bacterial - genetics</subject><subject>E coli</subject><subject>Enzymology and Protein Engineering</subject><subject>Escherichia coli</subject><subject>Escherichia coli - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gene expression</subject><subject>Gene Library</subject><subject>Genetic Complementation Test</subject><subject>Lysine - metabolism</subject><subject>Microbiology</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Proteins</subject><subject>Sequence Analysis, DNA</subject><subject>Soil Microbiology</subject><issn>0099-2240</issn><issn>1098-5336</issn><issn>1098-6596</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkc9rFDEUxwdR7Fq9edZB0JNTXzL5eRHKUrWwVbD24Cm8ySa7KTOTNpmt1L_erLu06sVTIO_Dh-9736p6TuCIEKreHZ-cHQGAZA3oB9WMgFYNb1vxsJoBaN1QyuCgepLzZaEYCPW4OiCaA2WMz6rvpzn2OIU41jgu6_kaE9rJpfBz9xl9jfXneOP6enGbw-jqr2jdgNnVPsWhDM9j6OszN-HKjXEItl6ELmG6fVo98thn92z_HlYXH06-zT81iy8fT-fHi8ZyJacGOyI7tIIvLWei40x5KZkUTm4jWmwVWzLeCW6XQlIOurNWaC-tt95R5dvD6v3Oe7XpBre0bpwS9uYqhaGkMBGD-XsyhrVZxRtDi45pWgRv9oIUrzcuT2YI2bq-x9HFTTZCcgog4L8gJUxxBW0BX_0DXsZNGssVDAWuuVR0a3u7g2yKOSfn7yITMNtmTWnW_G7WgC74iz_XvIf3VRbg9R7AbLH3CUcb8h1HidSKUHEfbh1W6x8hOYN5MOgGI7kh3HAiSIFe7iCP0eAqFdHFOQXSAhFcsbLkLxfuv80</recordid><startdate>20090801</startdate><enddate>20090801</enddate><creator>Chen, I. 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Chien ; Lin, Wei-De ; Hsu, Shin-Kuang ; Thiruvengadam, Venkatesan ; Hsu, Wen-Hwei</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c587t-ab17bac65dc546b548f77476e75024ca384d45b65cd672509bcc69f7cfcfe28f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Amino Acid Isomerases - chemistry</topic><topic>Amino Acid Isomerases - genetics</topic><topic>Amino Acid Isomerases - metabolism</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Cations, Divalent - pharmacology</topic><topic>Cells</topic><topic>Cloning, Molecular</topic><topic>Coenzymes - pharmacology</topic><topic>DNA, Bacterial - chemistry</topic><topic>DNA, Bacterial - genetics</topic><topic>E coli</topic><topic>Enzymology and Protein Engineering</topic><topic>Escherichia coli</topic><topic>Escherichia coli - genetics</topic><topic>Fundamental and applied biological sciences. 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Chien</au><au>Lin, Wei-De</au><au>Hsu, Shin-Kuang</au><au>Thiruvengadam, Venkatesan</au><au>Hsu, Wen-Hwei</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Isolation and Characterization of a Novel Lysine Racemase from a Soil Metagenomic Library</atitle><jtitle>Applied and Environmental Microbiology</jtitle><addtitle>Appl Environ Microbiol</addtitle><date>2009-08-01</date><risdate>2009</risdate><volume>75</volume><issue>15</issue><spage>5161</spage><epage>5166</epage><pages>5161-5166</pages><issn>0099-2240</issn><eissn>1098-5336</eissn><eissn>1098-6596</eissn><coden>AEMIDF</coden><abstract>A lysine racemase (lyr) gene was isolated from a soil metagenome by functional complementation for the first time by using Escherichia coli BCRC 51734 cells as the host and D-lysine as the selection agent. The lyr gene consisted of a 1,182-bp nucleotide sequence encoding a protein of 393 amino acids with a molecular mass of about 42.7 kDa. 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| source | MEDLINE; American Society for Microbiology Journals; EZB-FREE-00999 freely available EZB journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Amino Acid Isomerases - chemistry Amino Acid Isomerases - genetics Amino Acid Isomerases - metabolism Amino Acid Sequence Amino acids Base Sequence Biological and medical sciences Cations, Divalent - pharmacology Cells Cloning, Molecular Coenzymes - pharmacology DNA, Bacterial - chemistry DNA, Bacterial - genetics E coli Enzymology and Protein Engineering Escherichia coli Escherichia coli - genetics Fundamental and applied biological sciences. Psychology Gene expression Gene Library Genetic Complementation Test Lysine - metabolism Microbiology Molecular Sequence Data Molecular Weight Proteins Sequence Analysis, DNA Soil Microbiology |
| title | Isolation and Characterization of a Novel Lysine Racemase from a Soil Metagenomic Library |
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