Molecular cloning and functional expression of D-sorbitol dehydrogenase from Gluconobacter suboxydans IF03255, which requires pyrroloquinoline quinone and hydrophobic protein SldB for activity development in E. coli
The sldA gene that encodes the D-sorbitol dehydrogenase (SLDH) from Gluconobacter suboxydans IFO 3255 was cloned and sequenced. It encodes a polypeptide of 740 residues, which contains a signal sequence of 24 residues. SLDH had 35-37% identity to the membrane-bound quinoprotein glucose dehydrogenase...
Gespeichert in:
| Veröffentlicht in: | Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2002-02, Vol.66 (2), p.262-270 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 270 |
|---|---|
| container_issue | 2 |
| container_start_page | 262 |
| container_title | Bioscience, biotechnology, and biochemistry |
| container_volume | 66 |
| creator | Miyazaki, Taro Tomiyama, Noribumi Shinjoh, Masako Hoshino, Tatsuo |
| description | The sldA gene that encodes the D-sorbitol dehydrogenase (SLDH) from Gluconobacter suboxydans IFO 3255 was cloned and sequenced. It encodes a polypeptide of 740 residues, which contains a signal sequence of 24 residues. SLDH had 35-37% identity to the membrane-bound quinoprotein glucose dehydrogenases (GDHs) from E. coli, Gluconobacter oxydans, and Acinetobacter calcoaceticus except the N-terminal hydrophobic region of GDH. Additionally, the sldB gene located just upstream of sldA was found to encode a polypeptide consisting of 126 very hydrophobic residues that is similar in sequence to the one-sixth N-terminal region of the GDH. For the development of the SLDH activity in E. coli, co-expression of the sldA and sldB genes and the presence of pyrrloquinolone quinone as a co-factor were required. |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_pubme</sourceid><recordid>TN_cdi_proquest_miscellaneous_71663333</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>71663333</sourcerecordid><originalsourceid>FETCH-LOGICAL-p547-ee1b28e5188e77336de796caaf1f06d432211c59eb211fdba6bd3fdd3a9b14f23</originalsourceid><addsrcrecordid>eNo1kctOxDAMRbsAMTDwC8grVhQ1zbSdLnkNIIFYMPtRHg4TlMYlaYF-Kb9DeHlzfS3r-EreyfaLltX5clGxWXYQ40tRpEHF9rIZY23b8rbZzz4fyKEanQigHHnrn0F4DWb0arDkhQP86APGmAyQgas8UpB2IAcat5MO9IxeRAQTqIMbNyryJIUaMEAcJX1MWvgId6uCl1V1Cu9bq7YQ8HW0iQr9FAI5Ss6Tsx7hp0v6HeIH329JWgV9oAGthyenL8BQgHTCvtlhSjHe0FHfoR8gLVyfgUqow2zXCBfx6E_n2Xp1vb68ze8fb-4uz-_zvlo0OSKT5RIrtlxi03Bea2zaWglhmClqveBlyZiqWpRJjZailpobrbloJVuYks-zk19syvc6Yhw2nY0KnRMeaYybhtU1_655dvy3OMoO9aYPthNh2vx_gn8Ba8OK2w</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>71663333</pqid></control><display><type>article</type><title>Molecular cloning and functional expression of D-sorbitol dehydrogenase from Gluconobacter suboxydans IF03255, which requires pyrroloquinoline quinone and hydrophobic protein SldB for activity development in E. coli</title><source>MEDLINE</source><source>Oxford University Press Journals All Titles (1996-Current)</source><source>J-STAGE (Japan Science & Technology Information Aggregator, Electronic) Freely Available Titles - Japanese</source><source>Open Access Titles of Japan</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Free Full-Text Journals in Chemistry</source><creator>Miyazaki, Taro ; Tomiyama, Noribumi ; Shinjoh, Masako ; Hoshino, Tatsuo</creator><creatorcontrib>Miyazaki, Taro ; Tomiyama, Noribumi ; Shinjoh, Masako ; Hoshino, Tatsuo</creatorcontrib><description>The sldA gene that encodes the D-sorbitol dehydrogenase (SLDH) from Gluconobacter suboxydans IFO 3255 was cloned and sequenced. It encodes a polypeptide of 740 residues, which contains a signal sequence of 24 residues. SLDH had 35-37% identity to the membrane-bound quinoprotein glucose dehydrogenases (GDHs) from E. coli, Gluconobacter oxydans, and Acinetobacter calcoaceticus except the N-terminal hydrophobic region of GDH. Additionally, the sldB gene located just upstream of sldA was found to encode a polypeptide consisting of 126 very hydrophobic residues that is similar in sequence to the one-sixth N-terminal region of the GDH. For the development of the SLDH activity in E. coli, co-expression of the sldA and sldB genes and the presence of pyrrloquinolone quinone as a co-factor were required.</description><identifier>ISSN: 0916-8451</identifier><identifier>PMID: 11999397</identifier><language>eng</language><publisher>England</publisher><subject>Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; DNA, Bacterial ; Escherichia coli - genetics ; Gluconobacter - enzymology ; L-Iditol 2-Dehydrogenase - genetics ; L-Iditol 2-Dehydrogenase - metabolism ; Molecular Sequence Data ; Polymerase Chain Reaction ; PQQ Cofactor ; Quinolones - metabolism ; Quinones - metabolism ; Sequence Homology, Amino Acid</subject><ispartof>Bioscience, biotechnology, and biochemistry, 2002-02, Vol.66 (2), p.262-270</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11999397$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Miyazaki, Taro</creatorcontrib><creatorcontrib>Tomiyama, Noribumi</creatorcontrib><creatorcontrib>Shinjoh, Masako</creatorcontrib><creatorcontrib>Hoshino, Tatsuo</creatorcontrib><title>Molecular cloning and functional expression of D-sorbitol dehydrogenase from Gluconobacter suboxydans IF03255, which requires pyrroloquinoline quinone and hydrophobic protein SldB for activity development in E. coli</title><title>Bioscience, biotechnology, and biochemistry</title><addtitle>Biosci Biotechnol Biochem</addtitle><description>The sldA gene that encodes the D-sorbitol dehydrogenase (SLDH) from Gluconobacter suboxydans IFO 3255 was cloned and sequenced. It encodes a polypeptide of 740 residues, which contains a signal sequence of 24 residues. SLDH had 35-37% identity to the membrane-bound quinoprotein glucose dehydrogenases (GDHs) from E. coli, Gluconobacter oxydans, and Acinetobacter calcoaceticus except the N-terminal hydrophobic region of GDH. Additionally, the sldB gene located just upstream of sldA was found to encode a polypeptide consisting of 126 very hydrophobic residues that is similar in sequence to the one-sixth N-terminal region of the GDH. For the development of the SLDH activity in E. coli, co-expression of the sldA and sldB genes and the presence of pyrrloquinolone quinone as a co-factor were required.</description><subject>Amino Acid Sequence</subject><subject>Base Sequence</subject><subject>Cloning, Molecular</subject><subject>DNA, Bacterial</subject><subject>Escherichia coli - genetics</subject><subject>Gluconobacter - enzymology</subject><subject>L-Iditol 2-Dehydrogenase - genetics</subject><subject>L-Iditol 2-Dehydrogenase - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Polymerase Chain Reaction</subject><subject>PQQ Cofactor</subject><subject>Quinolones - metabolism</subject><subject>Quinones - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><issn>0916-8451</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo1kctOxDAMRbsAMTDwC8grVhQ1zbSdLnkNIIFYMPtRHg4TlMYlaYF-Kb9DeHlzfS3r-EreyfaLltX5clGxWXYQ40tRpEHF9rIZY23b8rbZzz4fyKEanQigHHnrn0F4DWb0arDkhQP86APGmAyQgas8UpB2IAcat5MO9IxeRAQTqIMbNyryJIUaMEAcJX1MWvgId6uCl1V1Cu9bq7YQ8HW0iQr9FAI5Ss6Tsx7hp0v6HeIH329JWgV9oAGthyenL8BQgHTCvtlhSjHe0FHfoR8gLVyfgUqow2zXCBfx6E_n2Xp1vb68ze8fb-4uz-_zvlo0OSKT5RIrtlxi03Bea2zaWglhmClqveBlyZiqWpRJjZailpobrbloJVuYks-zk19syvc6Yhw2nY0KnRMeaYybhtU1_655dvy3OMoO9aYPthNh2vx_gn8Ba8OK2w</recordid><startdate>200202</startdate><enddate>200202</enddate><creator>Miyazaki, Taro</creator><creator>Tomiyama, Noribumi</creator><creator>Shinjoh, Masako</creator><creator>Hoshino, Tatsuo</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>200202</creationdate><title>Molecular cloning and functional expression of D-sorbitol dehydrogenase from Gluconobacter suboxydans IF03255, which requires pyrroloquinoline quinone and hydrophobic protein SldB for activity development in E. coli</title><author>Miyazaki, Taro ; Tomiyama, Noribumi ; Shinjoh, Masako ; Hoshino, Tatsuo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p547-ee1b28e5188e77336de796caaf1f06d432211c59eb211fdba6bd3fdd3a9b14f23</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Amino Acid Sequence</topic><topic>Base Sequence</topic><topic>Cloning, Molecular</topic><topic>DNA, Bacterial</topic><topic>Escherichia coli - genetics</topic><topic>Gluconobacter - enzymology</topic><topic>L-Iditol 2-Dehydrogenase - genetics</topic><topic>L-Iditol 2-Dehydrogenase - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Polymerase Chain Reaction</topic><topic>PQQ Cofactor</topic><topic>Quinolones - metabolism</topic><topic>Quinones - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Miyazaki, Taro</creatorcontrib><creatorcontrib>Tomiyama, Noribumi</creatorcontrib><creatorcontrib>Shinjoh, Masako</creatorcontrib><creatorcontrib>Hoshino, Tatsuo</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Bioscience, biotechnology, and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Miyazaki, Taro</au><au>Tomiyama, Noribumi</au><au>Shinjoh, Masako</au><au>Hoshino, Tatsuo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular cloning and functional expression of D-sorbitol dehydrogenase from Gluconobacter suboxydans IF03255, which requires pyrroloquinoline quinone and hydrophobic protein SldB for activity development in E. coli</atitle><jtitle>Bioscience, biotechnology, and biochemistry</jtitle><addtitle>Biosci Biotechnol Biochem</addtitle><date>2002-02</date><risdate>2002</risdate><volume>66</volume><issue>2</issue><spage>262</spage><epage>270</epage><pages>262-270</pages><issn>0916-8451</issn><abstract>The sldA gene that encodes the D-sorbitol dehydrogenase (SLDH) from Gluconobacter suboxydans IFO 3255 was cloned and sequenced. It encodes a polypeptide of 740 residues, which contains a signal sequence of 24 residues. SLDH had 35-37% identity to the membrane-bound quinoprotein glucose dehydrogenases (GDHs) from E. coli, Gluconobacter oxydans, and Acinetobacter calcoaceticus except the N-terminal hydrophobic region of GDH. Additionally, the sldB gene located just upstream of sldA was found to encode a polypeptide consisting of 126 very hydrophobic residues that is similar in sequence to the one-sixth N-terminal region of the GDH. For the development of the SLDH activity in E. coli, co-expression of the sldA and sldB genes and the presence of pyrrloquinolone quinone as a co-factor were required.</abstract><cop>England</cop><pmid>11999397</pmid><tpages>9</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0916-8451 |
| ispartof | Bioscience, biotechnology, and biochemistry, 2002-02, Vol.66 (2), p.262-270 |
| issn | 0916-8451 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_71663333 |
| source | MEDLINE; Oxford University Press Journals All Titles (1996-Current); J-STAGE (Japan Science & Technology Information Aggregator, Electronic) Freely Available Titles - Japanese; Open Access Titles of Japan; EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry |
| subjects | Amino Acid Sequence Base Sequence Cloning, Molecular DNA, Bacterial Escherichia coli - genetics Gluconobacter - enzymology L-Iditol 2-Dehydrogenase - genetics L-Iditol 2-Dehydrogenase - metabolism Molecular Sequence Data Polymerase Chain Reaction PQQ Cofactor Quinolones - metabolism Quinones - metabolism Sequence Homology, Amino Acid |
| title | Molecular cloning and functional expression of D-sorbitol dehydrogenase from Gluconobacter suboxydans IF03255, which requires pyrroloquinoline quinone and hydrophobic protein SldB for activity development in E. coli |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-29T20%3A55%3A20IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Molecular%20cloning%20and%20functional%20expression%20of%20D-sorbitol%20dehydrogenase%20from%20Gluconobacter%20suboxydans%20IF03255,%20which%20requires%20pyrroloquinoline%20quinone%20and%20hydrophobic%20protein%20SldB%20for%20activity%20development%20in%20E.%20coli&rft.jtitle=Bioscience,%20biotechnology,%20and%20biochemistry&rft.au=Miyazaki,%20Taro&rft.date=2002-02&rft.volume=66&rft.issue=2&rft.spage=262&rft.epage=270&rft.pages=262-270&rft.issn=0916-8451&rft_id=info:doi/&rft_dat=%3Cproquest_pubme%3E71663333%3C/proquest_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=71663333&rft_id=info:pmid/11999397&rfr_iscdi=true |