Molecular properties of membrane-bound FAD-containing D-sorbitol dehydrogenase from thermotolerant Gluconobacter frateurii isolated from Thailand
There are two types of membrane-bound D-sorbitol dehydrogenase (SLDH) reported: PQQ-SLDH, having pyrroloquinoline quinone (PQQ), and FAD-SLDH, containing FAD and heme c as the prosthetic groups. FAD-SLDH was purified and characterized from the PQQ-SLDH mutant strain of a thermotolerant Gluco-nobacte...
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| Veröffentlicht in: | Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 2005-06, Vol.69 (6), p.1120-1129 |
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| creator | Toyama, H. (Yamaguchi Univ. (Japan). Faculty of Agriculture) Soemphol, W Moonmangmee, D Adachi, O Matsushita, K |
| description | There are two types of membrane-bound D-sorbitol dehydrogenase (SLDH) reported: PQQ-SLDH, having pyrroloquinoline quinone (PQQ), and FAD-SLDH, containing FAD and heme c as the prosthetic groups. FAD-SLDH was purified and characterized from the PQQ-SLDH mutant strain of a thermotolerant Gluco-nobacter frateurii, having molecular mass of 61.5kDa, 52kDa, and 22kDa. The enzyme properties were quite similar to those of the enzyme from mesophilic G. oxydans IFO 3254. This enzyme was shown to be inducible by D-sorbitol, but not PQQ-SLDH. The oxidation product of FAD-SLDH from D-sorbitol was identified as L-sorbose. The cloned gene of FAD-SLDH had three open reading frames (sldSLC) corresponding to the small, the large, and cytochrome c sub-units of FAD-SLDH respectively. The deduced amino acid sequences showed high identity to those from G. oxydans IFO 3254: SldL showed to other FAD-enzymes, and SldC having three heme c binding motives to cytochrome c sub-units of other membrane-bound dehydrogenases. |
| doi_str_mv | 10.1271/bbb.69.1120 |
| format | Article |
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(Yamaguchi Univ. (Japan). Faculty of Agriculture) ; Soemphol, W ; Moonmangmee, D ; Adachi, O ; Matsushita, K</creator><creatorcontrib>Toyama, H. (Yamaguchi Univ. (Japan). Faculty of Agriculture) ; Soemphol, W ; Moonmangmee, D ; Adachi, O ; Matsushita, K</creatorcontrib><description>There are two types of membrane-bound D-sorbitol dehydrogenase (SLDH) reported: PQQ-SLDH, having pyrroloquinoline quinone (PQQ), and FAD-SLDH, containing FAD and heme c as the prosthetic groups. FAD-SLDH was purified and characterized from the PQQ-SLDH mutant strain of a thermotolerant Gluco-nobacter frateurii, having molecular mass of 61.5kDa, 52kDa, and 22kDa. The enzyme properties were quite similar to those of the enzyme from mesophilic G. oxydans IFO 3254. This enzyme was shown to be inducible by D-sorbitol, but not PQQ-SLDH. The oxidation product of FAD-SLDH from D-sorbitol was identified as L-sorbose. The cloned gene of FAD-SLDH had three open reading frames (sldSLC) corresponding to the small, the large, and cytochrome c sub-units of FAD-SLDH respectively. The deduced amino acid sequences showed high identity to those from G. oxydans IFO 3254: SldL showed to other FAD-enzymes, and SldC having three heme c binding motives to cytochrome c sub-units of other membrane-bound dehydrogenases.</description><identifier>ISSN: 0916-8451</identifier><identifier>EISSN: 1347-6947</identifier><identifier>DOI: 10.1271/bbb.69.1120</identifier><identifier>PMID: 15973043</identifier><language>eng</language><publisher>Tokyo: Japan Society for Bioscience, Biotechnology, and Agrochemistry</publisher><subject>acetic acid bacteria ; Amino Acid Sequence ; AMINO ACID SEQUENCES ; Bacterial Proteins - chemistry ; Bacterial Proteins - metabolism ; Base Sequence ; Biological and medical sciences ; Conserved Sequence ; CYTOCHROME C ; FAD ; Flavin-Adenine Dinucleotide - chemistry ; Fundamental and applied biological sciences. Psychology ; Gluconobacter ; Gluconobacter - enzymology ; Gluconobacter frateurii ; HEAT TOLERANCE ; L-Iditol 2-Dehydrogenase - chemistry ; L-Iditol 2-Dehydrogenase - metabolism ; Membrane Proteins - chemistry ; Membrane Proteins - metabolism ; MOLECULAR CLONING ; Molecular Sequence Data ; Oxidation-Reduction ; OXIDOREDUCTASES ; PSEUDOMONACEAE ; PURIFICATION ; QUINOLINES ; QUINONES ; Sequence Alignment ; Sequence Homology, Amino Acid ; SORBITOL ; Sorbitol - metabolism ; sorbitol dehydrogenase ; Thailand</subject><ispartof>Bioscience, biotechnology, and biochemistry, 2005-06, Vol.69 (6), p.1120-1129</ispartof><rights>2005 by Japan Society for Bioscience, Biotechnology, and Agrochemistry 2005</rights><rights>2005 INIST-CNRS</rights><rights>Copyright Japan Science and Technology Agency 2005</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c637t-13dc5bcd760d3c7acdcf642d2fe1fb94a10ea5b9d9c871f8c3355b805db5e8333</citedby><cites>FETCH-LOGICAL-c637t-13dc5bcd760d3c7acdcf642d2fe1fb94a10ea5b9d9c871f8c3355b805db5e8333</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27922,27923</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=17039330$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15973043$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Toyama, H. (Yamaguchi Univ. (Japan). Faculty of Agriculture)</creatorcontrib><creatorcontrib>Soemphol, W</creatorcontrib><creatorcontrib>Moonmangmee, D</creatorcontrib><creatorcontrib>Adachi, O</creatorcontrib><creatorcontrib>Matsushita, K</creatorcontrib><title>Molecular properties of membrane-bound FAD-containing D-sorbitol dehydrogenase from thermotolerant Gluconobacter frateurii isolated from Thailand</title><title>Bioscience, biotechnology, and biochemistry</title><addtitle>Biosci Biotechnol Biochem</addtitle><description>There are two types of membrane-bound D-sorbitol dehydrogenase (SLDH) reported: PQQ-SLDH, having pyrroloquinoline quinone (PQQ), and FAD-SLDH, containing FAD and heme c as the prosthetic groups. FAD-SLDH was purified and characterized from the PQQ-SLDH mutant strain of a thermotolerant Gluco-nobacter frateurii, having molecular mass of 61.5kDa, 52kDa, and 22kDa. The enzyme properties were quite similar to those of the enzyme from mesophilic G. oxydans IFO 3254. This enzyme was shown to be inducible by D-sorbitol, but not PQQ-SLDH. The oxidation product of FAD-SLDH from D-sorbitol was identified as L-sorbose. The cloned gene of FAD-SLDH had three open reading frames (sldSLC) corresponding to the small, the large, and cytochrome c sub-units of FAD-SLDH respectively. The deduced amino acid sequences showed high identity to those from G. oxydans IFO 3254: SldL showed to other FAD-enzymes, and SldC having three heme c binding motives to cytochrome c sub-units of other membrane-bound dehydrogenases.</description><subject>acetic acid bacteria</subject><subject>Amino Acid Sequence</subject><subject>AMINO ACID SEQUENCES</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - metabolism</subject><subject>Base Sequence</subject><subject>Biological and medical sciences</subject><subject>Conserved Sequence</subject><subject>CYTOCHROME C</subject><subject>FAD</subject><subject>Flavin-Adenine Dinucleotide - chemistry</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gluconobacter</subject><subject>Gluconobacter - enzymology</subject><subject>Gluconobacter frateurii</subject><subject>HEAT TOLERANCE</subject><subject>L-Iditol 2-Dehydrogenase - chemistry</subject><subject>L-Iditol 2-Dehydrogenase - metabolism</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - metabolism</subject><subject>MOLECULAR CLONING</subject><subject>Molecular Sequence Data</subject><subject>Oxidation-Reduction</subject><subject>OXIDOREDUCTASES</subject><subject>PSEUDOMONACEAE</subject><subject>PURIFICATION</subject><subject>QUINOLINES</subject><subject>QUINONES</subject><subject>Sequence Alignment</subject><subject>Sequence Homology, Amino Acid</subject><subject>SORBITOL</subject><subject>Sorbitol - metabolism</subject><subject>sorbitol dehydrogenase</subject><subject>Thailand</subject><issn>0916-8451</issn><issn>1347-6947</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2005</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkU9v1DAQxSMEotvCiTMoEioXlMWOYzs-Vi0toCI4lLPlP5NdV0682I7Qfgy-MV6yqBJC4uSR5_eeZuZV1QuM1rjl-J3Wes3EGuMWPapWmHS8YaLjj6sVEpg1fUfxSXWa0j1C5YPip9UJpoIT1JFV9fNz8GBmr2K9i2EHMTtIdRjqEUYd1QSNDvNk6-uLq8aEKSs3uWlTXzUpRO1y8LWF7d7GsIFJJaiHGMY6byGOoTShOOT6xs9FGrQyGWIhVIY5Ole7FHyp7SK62yrn1WSfVU8G5RM8P75n1bfr93eXH5rbLzcfLy9uG8MIzw0m1lBtLGfIEsOVsWZgXWvbAfCgRacwAkW1sML0HA-9IYRS3SNqNYWeEHJWvVl8y97fZ0hZji4Z8GUGCHOSjAuGBcf_BTEnrCe_wdd_gfdhjlNZQuKuE31JqGOFertQJoaUIgxyF92o4l5iJA-ByhKoZEIeAi30q6PnrEewD-wxwQKcHwGVjPLlupNx6YHjiAhCDkZs4dw0hDiqHyF6K7Pa-xD_iMi_J3i5CAcVpNrEwn362iJEEeICI_ILgprHKQ</recordid><startdate>20050601</startdate><enddate>20050601</enddate><creator>Toyama, H. (Yamaguchi Univ. (Japan). Faculty of Agriculture)</creator><creator>Soemphol, W</creator><creator>Moonmangmee, D</creator><creator>Adachi, O</creator><creator>Matsushita, K</creator><general>Japan Society for Bioscience, Biotechnology, and Agrochemistry</general><general>Japan Society for Bioscience Biotechnology and Agrochemistry</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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>20050601</creationdate><title>Molecular properties of membrane-bound FAD-containing D-sorbitol dehydrogenase from thermotolerant Gluconobacter frateurii isolated from Thailand</title><author>Toyama, H. (Yamaguchi Univ. (Japan). Faculty of Agriculture) ; Soemphol, W ; Moonmangmee, D ; Adachi, O ; Matsushita, K</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c637t-13dc5bcd760d3c7acdcf642d2fe1fb94a10ea5b9d9c871f8c3355b805db5e8333</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2005</creationdate><topic>acetic acid bacteria</topic><topic>Amino Acid Sequence</topic><topic>AMINO ACID SEQUENCES</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - metabolism</topic><topic>Base Sequence</topic><topic>Biological and medical sciences</topic><topic>Conserved Sequence</topic><topic>CYTOCHROME C</topic><topic>FAD</topic><topic>Flavin-Adenine Dinucleotide - chemistry</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gluconobacter</topic><topic>Gluconobacter - enzymology</topic><topic>Gluconobacter frateurii</topic><topic>HEAT TOLERANCE</topic><topic>L-Iditol 2-Dehydrogenase - chemistry</topic><topic>L-Iditol 2-Dehydrogenase - metabolism</topic><topic>Membrane Proteins - chemistry</topic><topic>Membrane Proteins - metabolism</topic><topic>MOLECULAR CLONING</topic><topic>Molecular Sequence Data</topic><topic>Oxidation-Reduction</topic><topic>OXIDOREDUCTASES</topic><topic>PSEUDOMONACEAE</topic><topic>PURIFICATION</topic><topic>QUINOLINES</topic><topic>QUINONES</topic><topic>Sequence Alignment</topic><topic>Sequence Homology, Amino Acid</topic><topic>SORBITOL</topic><topic>Sorbitol - metabolism</topic><topic>sorbitol dehydrogenase</topic><topic>Thailand</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Toyama, H. (Yamaguchi Univ. (Japan). Faculty of Agriculture)</creatorcontrib><creatorcontrib>Soemphol, W</creatorcontrib><creatorcontrib>Moonmangmee, D</creatorcontrib><creatorcontrib>Adachi, O</creatorcontrib><creatorcontrib>Matsushita, 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>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Bioscience, biotechnology, and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Toyama, H. (Yamaguchi Univ. (Japan). Faculty of Agriculture)</au><au>Soemphol, W</au><au>Moonmangmee, D</au><au>Adachi, O</au><au>Matsushita, K</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Molecular properties of membrane-bound FAD-containing D-sorbitol dehydrogenase from thermotolerant Gluconobacter frateurii isolated from Thailand</atitle><jtitle>Bioscience, biotechnology, and biochemistry</jtitle><addtitle>Biosci Biotechnol Biochem</addtitle><date>2005-06-01</date><risdate>2005</risdate><volume>69</volume><issue>6</issue><spage>1120</spage><epage>1129</epage><pages>1120-1129</pages><issn>0916-8451</issn><eissn>1347-6947</eissn><abstract>There are two types of membrane-bound D-sorbitol dehydrogenase (SLDH) reported: PQQ-SLDH, having pyrroloquinoline quinone (PQQ), and FAD-SLDH, containing FAD and heme c as the prosthetic groups. FAD-SLDH was purified and characterized from the PQQ-SLDH mutant strain of a thermotolerant Gluco-nobacter frateurii, having molecular mass of 61.5kDa, 52kDa, and 22kDa. The enzyme properties were quite similar to those of the enzyme from mesophilic G. oxydans IFO 3254. This enzyme was shown to be inducible by D-sorbitol, but not PQQ-SLDH. The oxidation product of FAD-SLDH from D-sorbitol was identified as L-sorbose. The cloned gene of FAD-SLDH had three open reading frames (sldSLC) corresponding to the small, the large, and cytochrome c sub-units of FAD-SLDH respectively. The deduced amino acid sequences showed high identity to those from G. oxydans IFO 3254: SldL showed to other FAD-enzymes, and SldC having three heme c binding motives to cytochrome c sub-units of other membrane-bound dehydrogenases.</abstract><cop>Tokyo</cop><pub>Japan Society for Bioscience, Biotechnology, and Agrochemistry</pub><pmid>15973043</pmid><doi>10.1271/bbb.69.1120</doi><tpages>10</tpages></addata></record> |
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| identifier | ISSN: 0916-8451 |
| ispartof | Bioscience, biotechnology, and biochemistry, 2005-06, Vol.69 (6), p.1120-1129 |
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| language | eng |
| recordid | cdi_fao_agris_JP2005007910 |
| source | J-STAGE Free; MEDLINE; Oxford University Press Journals All Titles (1996-Current); Freely Accessible Japanese Titles; EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry |
| subjects | acetic acid bacteria Amino Acid Sequence AMINO ACID SEQUENCES Bacterial Proteins - chemistry Bacterial Proteins - metabolism Base Sequence Biological and medical sciences Conserved Sequence CYTOCHROME C FAD Flavin-Adenine Dinucleotide - chemistry Fundamental and applied biological sciences. Psychology Gluconobacter Gluconobacter - enzymology Gluconobacter frateurii HEAT TOLERANCE L-Iditol 2-Dehydrogenase - chemistry L-Iditol 2-Dehydrogenase - metabolism Membrane Proteins - chemistry Membrane Proteins - metabolism MOLECULAR CLONING Molecular Sequence Data Oxidation-Reduction OXIDOREDUCTASES PSEUDOMONACEAE PURIFICATION QUINOLINES QUINONES Sequence Alignment Sequence Homology, Amino Acid SORBITOL Sorbitol - metabolism sorbitol dehydrogenase Thailand |
| title | Molecular properties of membrane-bound FAD-containing D-sorbitol dehydrogenase from thermotolerant Gluconobacter frateurii isolated from Thailand |
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