Essential role of the small subunit of thermostable glucose dehydrogenase from Burkholderia cepacia
The co-expression in Escherichia coli of the gamma-subunit and the catalytic alpha-subunit of the thermostable glucose dehydrogenase (GDH) from Burkholderia cepacia sp. SM4 produced 12.7 U GDH activity mg(-1) protein. A 47-amino acid, twin-arginine translocase signal peptide was identified at the am...
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| Veröffentlicht in: | Biotechnology letters 2004-11, Vol.26 (22), p.1757-1761 |
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| container_title | Biotechnology letters |
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| creator | YAMAOKA, Hideaki FERRI, Stefano FUJIKAWA, Masako SODE, Koji |
| description | The co-expression in Escherichia coli of the gamma-subunit and the catalytic alpha-subunit of the thermostable glucose dehydrogenase (GDH) from Burkholderia cepacia sp. SM4 produced 12.7 U GDH activity mg(-1) protein. A 47-amino acid, twin-arginine translocase signal peptide was identified at the amino terminus of the gamma-subunit. The expression of the alpha-subunit in the absence of the gamma-subunit or the gamma-subunit signal peptide failed to produce any detectable GDH protein or activity. The gamma-subunit may be a chaperone-like component that assists folding of the alpha-subunit polypeptide to the active form and its translocation to the periplasm. |
| doi_str_mv | 10.1007/s10529-004-4582-0 |
| format | Article |
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SM4 produced 12.7 U GDH activity mg(-1) protein. A 47-amino acid, twin-arginine translocase signal peptide was identified at the amino terminus of the gamma-subunit. The expression of the alpha-subunit in the absence of the gamma-subunit or the gamma-subunit signal peptide failed to produce any detectable GDH protein or activity. The gamma-subunit may be a chaperone-like component that assists folding of the alpha-subunit polypeptide to the active form and its translocation to the periplasm.</description><identifier>ISSN: 0141-5492</identifier><identifier>EISSN: 1573-6776</identifier><identifier>DOI: 10.1007/s10529-004-4582-0</identifier><identifier>PMID: 15604831</identifier><identifier>CODEN: BILED3</identifier><language>eng</language><publisher>Dordrecht: Springer</publisher><subject>Amino Acid Sequence ; Amino acids ; Biological and medical sciences ; Biotechnology ; Burkholderia cepacia ; Burkholderia cepacia - enzymology ; Burkholderia cepacia - genetics ; Dehydrogenase ; E coli ; Enzyme Activation ; Enzyme Stability ; Escherichia coli - enzymology ; Escherichia coli - genetics ; Fundamental and applied biological sciences. Psychology ; Glucose 1-Dehydrogenase - analysis ; Glucose 1-Dehydrogenase - biosynthesis ; Glucose 1-Dehydrogenase - chemistry ; Molecular Sequence Data ; Molecular Weight ; Protein Subunits - chemistry ; Protein Subunits - metabolism ; Proteins ; Recombinant Proteins - chemistry ; Recombinant Proteins - metabolism ; Structure-Activity Relationship ; Temperature ; Translocation</subject><ispartof>Biotechnology letters, 2004-11, Vol.26 (22), p.1757-1761</ispartof><rights>2005 INIST-CNRS</rights><rights>Kluwer Academic Publishers 2004</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c490t-51b5835584215566282ca9706e4a625c889f0669fc1d9ebeb87243c925a2f2b33</citedby><cites>FETCH-LOGICAL-c490t-51b5835584215566282ca9706e4a625c889f0669fc1d9ebeb87243c925a2f2b33</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27923,27924</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=16355930$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15604831$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>YAMAOKA, Hideaki</creatorcontrib><creatorcontrib>FERRI, Stefano</creatorcontrib><creatorcontrib>FUJIKAWA, Masako</creatorcontrib><creatorcontrib>SODE, Koji</creatorcontrib><title>Essential role of the small subunit of thermostable glucose dehydrogenase from Burkholderia cepacia</title><title>Biotechnology letters</title><addtitle>Biotechnol Lett</addtitle><description>The co-expression in Escherichia coli of the gamma-subunit and the catalytic alpha-subunit of the thermostable glucose dehydrogenase (GDH) from Burkholderia cepacia sp. SM4 produced 12.7 U GDH activity mg(-1) protein. A 47-amino acid, twin-arginine translocase signal peptide was identified at the amino terminus of the gamma-subunit. The expression of the alpha-subunit in the absence of the gamma-subunit or the gamma-subunit signal peptide failed to produce any detectable GDH protein or activity. The gamma-subunit may be a chaperone-like component that assists folding of the alpha-subunit polypeptide to the active form and its translocation to the periplasm.</description><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Burkholderia cepacia</subject><subject>Burkholderia cepacia - enzymology</subject><subject>Burkholderia cepacia - genetics</subject><subject>Dehydrogenase</subject><subject>E coli</subject><subject>Enzyme Activation</subject><subject>Enzyme Stability</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Glucose 1-Dehydrogenase - analysis</subject><subject>Glucose 1-Dehydrogenase - biosynthesis</subject><subject>Glucose 1-Dehydrogenase - chemistry</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>Protein Subunits - chemistry</subject><subject>Protein Subunits - metabolism</subject><subject>Proteins</subject><subject>Recombinant Proteins - chemistry</subject><subject>Recombinant Proteins - metabolism</subject><subject>Structure-Activity Relationship</subject><subject>Temperature</subject><subject>Translocation</subject><issn>0141-5492</issn><issn>1573-6776</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</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>eNqFkctu1DAUQC0EaofSD2CDIqSyC1y_7SVUfSBVYgNry3GcTooTD77Jon-PRxOpEhtW1rXOfR5C3lP4TAH0F6QgmW0BRCukYS28IjsqNW-V1uo12QEVtJXCsnPyFvEJAKwGfUbOqVQgDKc7Em4Q47yMPjUlp9jkoVn2scHJp9Tg2q3zuGyfZcq4-K5Cj2kNGWPTx_1zX_JjnH2NhpKn5ttafu9z6mMZfRPiwYfRvyNvBp8wXm7vBfl1e_Pz-r59-HH3_frrQxuEhaWVtJOGS2kEo1IqxQwLvg6sovCKyWCMHUApOwTa29jFzmgmeLBMejawjvML8ulU91DynzXi4qYRQ0zJzzGv6JSmpq7N_gtSLaGeUVbw4z_gU17LXJdwmgujhNXHtvQEhZIRSxzcoYyTL8-Ogjt6cidPrnpyR08Oas6HrfDaTbF_ydjEVOBqAzwGn4bi5zDiC6fqoSwH_hc9H5n7</recordid><startdate>20041101</startdate><enddate>20041101</enddate><creator>YAMAOKA, Hideaki</creator><creator>FERRI, Stefano</creator><creator>FUJIKAWA, Masako</creator><creator>SODE, Koji</creator><general>Springer</general><general>Springer Nature B.V</general><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>7QR</scope><scope>7T7</scope><scope>7TB</scope><scope>7U5</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</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>HCIFZ</scope><scope>K9.</scope><scope>L6V</scope><scope>L7M</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>Q9U</scope><scope>7X8</scope></search><sort><creationdate>20041101</creationdate><title>Essential role of the small subunit of thermostable glucose dehydrogenase from Burkholderia cepacia</title><author>YAMAOKA, Hideaki ; FERRI, Stefano ; FUJIKAWA, Masako ; SODE, Koji</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c490t-51b5835584215566282ca9706e4a625c889f0669fc1d9ebeb87243c925a2f2b33</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Burkholderia cepacia</topic><topic>Burkholderia cepacia - enzymology</topic><topic>Burkholderia cepacia - genetics</topic><topic>Dehydrogenase</topic><topic>E coli</topic><topic>Enzyme Activation</topic><topic>Enzyme Stability</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli - genetics</topic><topic>Fundamental and applied biological sciences. 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Academic</collection><jtitle>Biotechnology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>YAMAOKA, Hideaki</au><au>FERRI, Stefano</au><au>FUJIKAWA, Masako</au><au>SODE, Koji</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Essential role of the small subunit of thermostable glucose dehydrogenase from Burkholderia cepacia</atitle><jtitle>Biotechnology letters</jtitle><addtitle>Biotechnol Lett</addtitle><date>2004-11-01</date><risdate>2004</risdate><volume>26</volume><issue>22</issue><spage>1757</spage><epage>1761</epage><pages>1757-1761</pages><issn>0141-5492</issn><eissn>1573-6776</eissn><coden>BILED3</coden><abstract>The co-expression in Escherichia coli of the gamma-subunit and the catalytic alpha-subunit of the thermostable glucose dehydrogenase (GDH) from Burkholderia cepacia sp. SM4 produced 12.7 U GDH activity mg(-1) protein. A 47-amino acid, twin-arginine translocase signal peptide was identified at the amino terminus of the gamma-subunit. The expression of the alpha-subunit in the absence of the gamma-subunit or the gamma-subunit signal peptide failed to produce any detectable GDH protein or activity. The gamma-subunit may be a chaperone-like component that assists folding of the alpha-subunit polypeptide to the active form and its translocation to the periplasm.</abstract><cop>Dordrecht</cop><pub>Springer</pub><pmid>15604831</pmid><doi>10.1007/s10529-004-4582-0</doi><tpages>5</tpages></addata></record> |
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| ispartof | Biotechnology letters, 2004-11, Vol.26 (22), p.1757-1761 |
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| subjects | Amino Acid Sequence Amino acids Biological and medical sciences Biotechnology Burkholderia cepacia Burkholderia cepacia - enzymology Burkholderia cepacia - genetics Dehydrogenase E coli Enzyme Activation Enzyme Stability Escherichia coli - enzymology Escherichia coli - genetics Fundamental and applied biological sciences. Psychology Glucose 1-Dehydrogenase - analysis Glucose 1-Dehydrogenase - biosynthesis Glucose 1-Dehydrogenase - chemistry Molecular Sequence Data Molecular Weight Protein Subunits - chemistry Protein Subunits - metabolism Proteins Recombinant Proteins - chemistry Recombinant Proteins - metabolism Structure-Activity Relationship Temperature Translocation |
| title | Essential role of the small subunit of thermostable glucose dehydrogenase from Burkholderia cepacia |
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