New alpha-L-arabinofuranosidase produced by Streptomyces lividans: cloning and DNA sequence of the abfB gene and characterization of the enzyme
A fully secreted alpha-l-arabinofuranosidase was cloned from the homologous expression system of Streptomyces lividans. The gene, located upstream adjacent to the previously described xylanase A gene, was sequenced. It is divergently transcribed from the xlnA gene and the two genes are separated by...
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| Veröffentlicht in: | Biochemical journal 1997-03, Vol.322 ( Pt 3) (3), p.845-852 |
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| container_title | Biochemical journal |
| container_volume | 322 ( Pt 3) |
| creator | Vincent, P Shareck, F Dupont, C Morosoli, R Kluepfel, D |
| description | A fully secreted alpha-l-arabinofuranosidase was cloned from the homologous expression system of Streptomyces lividans. The gene, located upstream adjacent to the previously described xylanase A gene, was sequenced. It is divergently transcribed from the xlnA gene and the two genes are separated by an intercistronic region of 391nt which contains a palindromic AT-rich sequence. The deduced amino acid sequence of the protein shows that the enzyme contains a distinct catalytic domain which is linked to a specific xylan-binding domain by a linker region. The purified enzyme has a specific arabinofuranose-debranching activity on xylan from Gramineae, acts synergistically with the S. lividans xylanases and binds specifically to xylan. From small arabinoxylo-oligosides, it liberates arabinose and, after prolonged incubation, the purified enzyme exhibits some xylanolytic activity as well. |
| doi_str_mv | 10.1042/bj3220845 |
| format | Article |
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The gene, located upstream adjacent to the previously described xylanase A gene, was sequenced. It is divergently transcribed from the xlnA gene and the two genes are separated by an intercistronic region of 391nt which contains a palindromic AT-rich sequence. The deduced amino acid sequence of the protein shows that the enzyme contains a distinct catalytic domain which is linked to a specific xylan-binding domain by a linker region. The purified enzyme has a specific arabinofuranose-debranching activity on xylan from Gramineae, acts synergistically with the S. lividans xylanases and binds specifically to xylan. 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The gene, located upstream adjacent to the previously described xylanase A gene, was sequenced. It is divergently transcribed from the xlnA gene and the two genes are separated by an intercistronic region of 391nt which contains a palindromic AT-rich sequence. The deduced amino acid sequence of the protein shows that the enzyme contains a distinct catalytic domain which is linked to a specific xylan-binding domain by a linker region. The purified enzyme has a specific arabinofuranose-debranching activity on xylan from Gramineae, acts synergistically with the S. lividans xylanases and binds specifically to xylan. From small arabinoxylo-oligosides, it liberates arabinose and, after prolonged incubation, the purified enzyme exhibits some xylanolytic activity as well.</description><subject>Amino Acid Sequence</subject><subject>Base Sequence</subject><subject>Cloning, Molecular</subject><subject>DNA, Bacterial - genetics</subject><subject>Genes, Bacterial</subject><subject>Glycoside Hydrolases - analysis</subject><subject>Glycoside Hydrolases - genetics</subject><subject>Glycoside Hydrolases - isolation & purification</subject><subject>Molecular Sequence Data</subject><subject>Sequence Analysis, DNA</subject><subject>Streptomyces - genetics</subject><subject>Streptomyces lividans</subject><issn>0264-6021</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkcluFDEQhi0ECpPlwAMg-YTEocFLj9udQ6QQwiKNwgFyttx2ecZRt92xu4MmL8ErY5JhFE7UpaSqT38tP0KvKHlHSc3edzecMSLr5TO0oHVDKtkw-RwtCBN1JQijL9FhzjeE0JrU5AAdtLSWzbJdoF9X8BPrftzoalXppDsfopuTDjF7qzPgMUU7G7C42-LvU4JxisPWQMa9vytEyKfY9DH4sMY6WPzx6hxnuJ0hGMDR4WkDWHfuA15DgAfCbMoYM0Hy93ryMfylINxvBzhGL5zuM5zs8hG6_nT54-JLtfr2-evF-aoyNaFT1YJl3ZIIoaUhpGUcyl3ARMNYqTMpW-u41dZpLjreWAa0bcEZSW35jJP8CJ096o5zN4A1EKakezUmP-i0VVF79W8n-I1axztFGZVMLIvAm51AiuXcPKnBZwN9rwPEOatGlmgl_S9IBeFM8KaAbx9Bk2LOCdx-G0rUH5vV3ubCvn66_p7c-cp_AynPpYU</recordid><startdate>19970315</startdate><enddate>19970315</enddate><creator>Vincent, P</creator><creator>Shareck, F</creator><creator>Dupont, C</creator><creator>Morosoli, R</creator><creator>Kluepfel, D</creator><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>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>P64</scope><scope>RC3</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19970315</creationdate><title>New alpha-L-arabinofuranosidase produced by Streptomyces lividans: cloning and DNA sequence of the abfB gene and characterization of the enzyme</title><author>Vincent, P ; Shareck, F ; Dupont, C ; Morosoli, R ; Kluepfel, D</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c401t-9ed2b5066a8c00923e040e267222b52889df3dadfa36b37d2e199efc81d728f83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Amino Acid Sequence</topic><topic>Base Sequence</topic><topic>Cloning, Molecular</topic><topic>DNA, Bacterial - genetics</topic><topic>Genes, Bacterial</topic><topic>Glycoside Hydrolases - analysis</topic><topic>Glycoside Hydrolases - genetics</topic><topic>Glycoside Hydrolases - isolation & purification</topic><topic>Molecular Sequence Data</topic><topic>Sequence Analysis, DNA</topic><topic>Streptomyces - genetics</topic><topic>Streptomyces lividans</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Vincent, P</creatorcontrib><creatorcontrib>Shareck, F</creatorcontrib><creatorcontrib>Dupont, C</creatorcontrib><creatorcontrib>Morosoli, R</creatorcontrib><creatorcontrib>Kluepfel, D</creatorcontrib><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>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biochemical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Vincent, P</au><au>Shareck, F</au><au>Dupont, C</au><au>Morosoli, R</au><au>Kluepfel, D</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>New alpha-L-arabinofuranosidase produced by Streptomyces lividans: cloning and DNA sequence of the abfB gene and characterization of the enzyme</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>1997-03-15</date><risdate>1997</risdate><volume>322 ( Pt 3)</volume><issue>3</issue><spage>845</spage><epage>852</epage><pages>845-852</pages><issn>0264-6021</issn><eissn>1470-8728</eissn><abstract>A fully secreted alpha-l-arabinofuranosidase was cloned from the homologous expression system of Streptomyces lividans. The gene, located upstream adjacent to the previously described xylanase A gene, was sequenced. It is divergently transcribed from the xlnA gene and the two genes are separated by an intercistronic region of 391nt which contains a palindromic AT-rich sequence. The deduced amino acid sequence of the protein shows that the enzyme contains a distinct catalytic domain which is linked to a specific xylan-binding domain by a linker region. The purified enzyme has a specific arabinofuranose-debranching activity on xylan from Gramineae, acts synergistically with the S. lividans xylanases and binds specifically to xylan. From small arabinoxylo-oligosides, it liberates arabinose and, after prolonged incubation, the purified enzyme exhibits some xylanolytic activity as well.</abstract><cop>England</cop><pmid>9148759</pmid><doi>10.1042/bj3220845</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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| identifier | ISSN: 0264-6021 |
| ispartof | Biochemical journal, 1997-03, Vol.322 ( Pt 3) (3), p.845-852 |
| issn | 0264-6021 1470-8728 |
| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Amino Acid Sequence Base Sequence Cloning, Molecular DNA, Bacterial - genetics Genes, Bacterial Glycoside Hydrolases - analysis Glycoside Hydrolases - genetics Glycoside Hydrolases - isolation & purification Molecular Sequence Data Sequence Analysis, DNA Streptomyces - genetics Streptomyces lividans |
| title | New alpha-L-arabinofuranosidase produced by Streptomyces lividans: cloning and DNA sequence of the abfB gene and characterization of the enzyme |
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