Biotin synthase of Bacillus subtilis shows less reactivity than that of Escherichia coli in in vitro reaction systems
The biotin synthases of Bacillus subtilis and Escherichia coli were compared in a physiological reduction system using cell-free extracts and in a artificial reduction system using photo-reduced deazariboflavin. The biotin synthase of B. subtilis was less active than that of E. coli in both reaction...
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| Veröffentlicht in: | Archives of microbiology 2002-12, Vol.179 (1), p.26-32 |
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| container_title | Archives of microbiology |
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| creator | KIYASU, Tatsuya ASAKURA, Akira NAGAHASHI, Yoshie HOSHINO, Tatsuo |
| description | The biotin synthases of Bacillus subtilis and Escherichia coli were compared in a physiological reduction system using cell-free extracts and in a artificial reduction system using photo-reduced deazariboflavin. The biotin synthase of B. subtilis was less active than that of E. coli in both reaction systems and showed at least ten-fold less biotin-forming activity than that of E. coli in the artificial reduction system. The physiological reduction system using the biotin synthases and cell-free extracts of B. subtilis and E. coli showed species specificity. The results suggest that the activity of the physiological reduction system of B. subtilisis weaker than that of E. coli. Addition of excess dethiobiotin inhibited biotin formation by growing cells of B. subtilis, but not by E. coli. |
| doi_str_mv | 10.1007/s00203-002-0494-3 |
| format | Article |
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The biotin synthase of B. subtilis was less active than that of E. coli in both reaction systems and showed at least ten-fold less biotin-forming activity than that of E. coli in the artificial reduction system. The physiological reduction system using the biotin synthases and cell-free extracts of B. subtilis and E. coli showed species specificity. The results suggest that the activity of the physiological reduction system of B. subtilisis weaker than that of E. coli. Addition of excess dethiobiotin inhibited biotin formation by growing cells of B. subtilis, but not by E. coli.</description><identifier>ISSN: 0302-8933</identifier><identifier>EISSN: 1432-072X</identifier><identifier>DOI: 10.1007/s00203-002-0494-3</identifier><identifier>PMID: 12471501</identifier><identifier>CODEN: AMICCW</identifier><language>eng</language><publisher>Heidelberg: Springer</publisher><subject>Bacillus subtilis - enzymology ; Bacillus subtilis - metabolism ; Bacterial Proteins - biosynthesis ; Bacterial Proteins - isolation & purification ; Bacteriology ; Biological and medical sciences ; Biotin - analogs & derivatives ; Biotin - metabolism ; Chlorides ; Cloning, Molecular ; Culture Media ; Escherichia coli - enzymology ; Escherichia coli - metabolism ; Escherichia coli Proteins ; Ferric Compounds - metabolism ; Fundamental and applied biological sciences. 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The biotin synthase of B. subtilis was less active than that of E. coli in both reaction systems and showed at least ten-fold less biotin-forming activity than that of E. coli in the artificial reduction system. The physiological reduction system using the biotin synthases and cell-free extracts of B. subtilis and E. coli showed species specificity. The results suggest that the activity of the physiological reduction system of B. subtilisis weaker than that of E. coli. Addition of excess dethiobiotin inhibited biotin formation by growing cells of B. subtilis, but not by E. coli.</description><subject>Bacillus subtilis - enzymology</subject><subject>Bacillus subtilis - metabolism</subject><subject>Bacterial Proteins - biosynthesis</subject><subject>Bacterial Proteins - isolation & purification</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Biotin - analogs & derivatives</subject><subject>Biotin - metabolism</subject><subject>Chlorides</subject><subject>Cloning, Molecular</subject><subject>Culture Media</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli - metabolism</subject><subject>Escherichia coli Proteins</subject><subject>Ferric Compounds - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>In Vitro Techniques</subject><subject>Microbiology</subject><subject>Miscellaneous</subject><subject>Riboflavin - analogs & derivatives</subject><subject>Riboflavin - metabolism</subject><subject>Species Specificity</subject><subject>Sulfides - metabolism</subject><subject>Sulfurtransferases - genetics</subject><subject>Sulfurtransferases - metabolism</subject><issn>0302-8933</issn><issn>1432-072X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2002</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0M9PwyAUB3BiNG5O_wAvhoveqg9oCz3qMn8kS7xo4q2hFDIMa2cf1ey_l8UZjybkAeHzfQQIOWdwzQDkDQJwEFmqGeRVnokDMmW5SDvJ3w7JFEQ6UZUQE3KC-A7AuFLqmEwYzyUrgE3JeOf76DuK2y6uNFraO3qnjQ9hRIpjE33wabHqv5AGi0gHq030nz5uaQp0uxJ3oQWalR28WXlNTR88TU3TSHDo96F-dw1Gu8ZTcuR0QHu2n2fk9X7xMn_Mls8PT_PbZbbhpYqZk6rhpW5cel0FzBrRVMwYp1uhC8clOFeUrKyMsCZXVSutqlzbysStZVCIGbn66bsZ-o_RYqzXHo0NQXe2H7GWXO7y-b-QqZKrZBO82MOxWdu23gx-rYdt_fujCVzugUajgxt0Zzz-ubyQAArEN0TUh4E</recordid><startdate>20021201</startdate><enddate>20021201</enddate><creator>KIYASU, Tatsuya</creator><creator>ASAKURA, Akira</creator><creator>NAGAHASHI, Yoshie</creator><creator>HOSHINO, Tatsuo</creator><general>Springer</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>20021201</creationdate><title>Biotin synthase of Bacillus subtilis shows less reactivity than that of Escherichia coli in in vitro reaction systems</title><author>KIYASU, Tatsuya ; ASAKURA, Akira ; NAGAHASHI, Yoshie ; HOSHINO, Tatsuo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p268t-f78b26abf049901ec3b91ccfad3a5f270ff56169c3ec489d7e89fdd7049ee1053</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2002</creationdate><topic>Bacillus subtilis - enzymology</topic><topic>Bacillus subtilis - metabolism</topic><topic>Bacterial Proteins - biosynthesis</topic><topic>Bacterial Proteins - isolation & purification</topic><topic>Bacteriology</topic><topic>Biological and medical sciences</topic><topic>Biotin - analogs & derivatives</topic><topic>Biotin - metabolism</topic><topic>Chlorides</topic><topic>Cloning, Molecular</topic><topic>Culture Media</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli - metabolism</topic><topic>Escherichia coli Proteins</topic><topic>Ferric Compounds - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>In Vitro Techniques</topic><topic>Microbiology</topic><topic>Miscellaneous</topic><topic>Riboflavin - analogs & derivatives</topic><topic>Riboflavin - metabolism</topic><topic>Species Specificity</topic><topic>Sulfides - metabolism</topic><topic>Sulfurtransferases - genetics</topic><topic>Sulfurtransferases - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>KIYASU, Tatsuya</creatorcontrib><creatorcontrib>ASAKURA, Akira</creatorcontrib><creatorcontrib>NAGAHASHI, Yoshie</creatorcontrib><creatorcontrib>HOSHINO, Tatsuo</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Archives of microbiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>KIYASU, Tatsuya</au><au>ASAKURA, Akira</au><au>NAGAHASHI, Yoshie</au><au>HOSHINO, Tatsuo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Biotin synthase of Bacillus subtilis shows less reactivity than that of Escherichia coli in in vitro reaction systems</atitle><jtitle>Archives of microbiology</jtitle><addtitle>Arch Microbiol</addtitle><date>2002-12-01</date><risdate>2002</risdate><volume>179</volume><issue>1</issue><spage>26</spage><epage>32</epage><pages>26-32</pages><issn>0302-8933</issn><eissn>1432-072X</eissn><coden>AMICCW</coden><abstract>The biotin synthases of Bacillus subtilis and Escherichia coli were compared in a physiological reduction system using cell-free extracts and in a artificial reduction system using photo-reduced deazariboflavin. The biotin synthase of B. subtilis was less active than that of E. coli in both reaction systems and showed at least ten-fold less biotin-forming activity than that of E. coli in the artificial reduction system. The physiological reduction system using the biotin synthases and cell-free extracts of B. subtilis and E. coli showed species specificity. The results suggest that the activity of the physiological reduction system of B. subtilisis weaker than that of E. coli. Addition of excess dethiobiotin inhibited biotin formation by growing cells of B. subtilis, but not by E. coli.</abstract><cop>Heidelberg</cop><cop>Berlin</cop><pub>Springer</pub><pmid>12471501</pmid><doi>10.1007/s00203-002-0494-3</doi><tpages>7</tpages></addata></record> |
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| identifier | ISSN: 0302-8933 |
| ispartof | Archives of microbiology, 2002-12, Vol.179 (1), p.26-32 |
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| language | eng |
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| subjects | Bacillus subtilis - enzymology Bacillus subtilis - metabolism Bacterial Proteins - biosynthesis Bacterial Proteins - isolation & purification Bacteriology Biological and medical sciences Biotin - analogs & derivatives Biotin - metabolism Chlorides Cloning, Molecular Culture Media Escherichia coli - enzymology Escherichia coli - metabolism Escherichia coli Proteins Ferric Compounds - metabolism Fundamental and applied biological sciences. Psychology In Vitro Techniques Microbiology Miscellaneous Riboflavin - analogs & derivatives Riboflavin - metabolism Species Specificity Sulfides - metabolism Sulfurtransferases - genetics Sulfurtransferases - metabolism |
| title | Biotin synthase of Bacillus subtilis shows less reactivity than that of Escherichia coli in in vitro reaction systems |
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