Unprocessed barley aleurone endo-β-1,4-xylanase X-I is an active enzyme
Endo-β-1,4-xylanase X-I is a major hydrolase produced by the aleurone tissue of germinating barley grain. It was previously reported that this cytosolic enzyme is synthesized as an inactive precursor which is proteolytically processed to active forms upon its programmed cell death dependent release....
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| Veröffentlicht in: | Biochemical and biophysical research communications 2007-05, Vol.356 (3), p.799-804 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Van Campenhout, Steven Pollet, Annick Bourgois, Tine M. Rombouts, Sigrid Beaugrand, Johnny Gebruers, Kurt De Backer, Evelien Courtin, Christophe M. Delcour, Jan A. Volckaert, Guido |
| description | Endo-β-1,4-xylanase X-I is a major hydrolase produced by the aleurone tissue of germinating barley grain. It was previously reported that this cytosolic enzyme is synthesized as an inactive precursor which is proteolytically processed to active forms upon its programmed cell death dependent release. We here demonstrate, however, that the precursor form of X-I is an active enzyme. Purified recombinant precursor X-I was characterised with respect to its molecular weight, iso-electric point and temperature and pH activity and stability. Analysis of the hydrolysis products showed that it is an endo-acting enzyme which has the striking ability to release xylose from both polymeric xylan as well as from small xylo-oligosaccharides. The implications of these findings in relation to the putative role of the N-terminal propeptide as a carbohydrate binding module and the possible consequences for the way X-I fulfils its role in the germination process, are discussed. |
| doi_str_mv | 10.1016/j.bbrc.2007.03.066 |
| format | Article |
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It was previously reported that this cytosolic enzyme is synthesized as an inactive precursor which is proteolytically processed to active forms upon its programmed cell death dependent release. We here demonstrate, however, that the precursor form of X-I is an active enzyme. Purified recombinant precursor X-I was characterised with respect to its molecular weight, iso-electric point and temperature and pH activity and stability. Analysis of the hydrolysis products showed that it is an endo-acting enzyme which has the striking ability to release xylose from both polymeric xylan as well as from small xylo-oligosaccharides. The implications of these findings in relation to the putative role of the N-terminal propeptide as a carbohydrate binding module and the possible consequences for the way X-I fulfils its role in the germination process, are discussed.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2007.03.066</identifier><identifier>PMID: 17383610</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Cloning, Molecular ; Cytoplasmic xylanase ; Endo-1,4-beta Xylanases - chemistry ; Endo-1,4-beta Xylanases - metabolism ; Enzyme Stability ; Escherichia coli ; Escherichia coli - metabolism ; Germination - physiology ; Germination enzyme ; Heteroxylan hydrolysis ; Hordeum - enzymology ; Hordeum vulgare ; Hydrogen-Ion Concentration ; Isoelectric Point ; Kinetics ; Molecular Weight ; Temperature ; Xylans - metabolism</subject><ispartof>Biochemical and biophysical research communications, 2007-05, Vol.356 (3), p.799-804</ispartof><rights>2007 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c354t-7f22030adb4e0b3b17c941299eb8fe6603e38b1efc1f3baa3bdb27ae9d079843</citedby><cites>FETCH-LOGICAL-c354t-7f22030adb4e0b3b17c941299eb8fe6603e38b1efc1f3baa3bdb27ae9d079843</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006291X07005359$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/17383610$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Van Campenhout, Steven</creatorcontrib><creatorcontrib>Pollet, Annick</creatorcontrib><creatorcontrib>Bourgois, Tine M.</creatorcontrib><creatorcontrib>Rombouts, Sigrid</creatorcontrib><creatorcontrib>Beaugrand, Johnny</creatorcontrib><creatorcontrib>Gebruers, Kurt</creatorcontrib><creatorcontrib>De Backer, Evelien</creatorcontrib><creatorcontrib>Courtin, Christophe M.</creatorcontrib><creatorcontrib>Delcour, Jan A.</creatorcontrib><creatorcontrib>Volckaert, Guido</creatorcontrib><title>Unprocessed barley aleurone endo-β-1,4-xylanase X-I is an active enzyme</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Endo-β-1,4-xylanase X-I is a major hydrolase produced by the aleurone tissue of germinating barley grain. It was previously reported that this cytosolic enzyme is synthesized as an inactive precursor which is proteolytically processed to active forms upon its programmed cell death dependent release. We here demonstrate, however, that the precursor form of X-I is an active enzyme. Purified recombinant precursor X-I was characterised with respect to its molecular weight, iso-electric point and temperature and pH activity and stability. Analysis of the hydrolysis products showed that it is an endo-acting enzyme which has the striking ability to release xylose from both polymeric xylan as well as from small xylo-oligosaccharides. The implications of these findings in relation to the putative role of the N-terminal propeptide as a carbohydrate binding module and the possible consequences for the way X-I fulfils its role in the germination process, are discussed.</description><subject>Cloning, Molecular</subject><subject>Cytoplasmic xylanase</subject><subject>Endo-1,4-beta Xylanases - chemistry</subject><subject>Endo-1,4-beta Xylanases - metabolism</subject><subject>Enzyme Stability</subject><subject>Escherichia coli</subject><subject>Escherichia coli - metabolism</subject><subject>Germination - physiology</subject><subject>Germination enzyme</subject><subject>Heteroxylan hydrolysis</subject><subject>Hordeum - enzymology</subject><subject>Hordeum vulgare</subject><subject>Hydrogen-Ion Concentration</subject><subject>Isoelectric Point</subject><subject>Kinetics</subject><subject>Molecular Weight</subject><subject>Temperature</subject><subject>Xylans - metabolism</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kM1KAzEUhYMotlZfwIXMypUZbyZxfsCNFLWFgpsK3YUkcwdS5qcmM8XxsXwQn8kZWnDn6m6-czj3I-SaQciAxffbUGtnwgggCYGHEMcnZMogAxoxEKdkCgAxjTK2mZAL77cAjIk4OycTlvCUxwymZPFe71xj0HvMA61ciX2gSuxcU2OAdd7Qn2_K7gT97EtVK4_Bhi4D6wNVB8q0dj9SX32Fl-SsUKXHq-OdkfXL83q-oKu31-X8aUUNfxAtTYooAg4q1wJBc80SkwkWZRnqtMA4Bo481QwLwwquleI611GiMMshyVLBZ-T2UDus_ujQt7Ky3mA5jMOm8zIBLpI0hQGMDqBxjfcOC7lztlKulwzkqE9u5ahPjvokcDnoG0I3x_ZOV5j_RY6-BuDxAODw4t6ik95YrA3m1qFpZd7Y__p_AUT8gQU</recordid><startdate>20070511</startdate><enddate>20070511</enddate><creator>Van Campenhout, Steven</creator><creator>Pollet, Annick</creator><creator>Bourgois, Tine M.</creator><creator>Rombouts, Sigrid</creator><creator>Beaugrand, Johnny</creator><creator>Gebruers, Kurt</creator><creator>De Backer, Evelien</creator><creator>Courtin, Christophe M.</creator><creator>Delcour, Jan A.</creator><creator>Volckaert, Guido</creator><general>Elsevier Inc</general><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>7X8</scope></search><sort><creationdate>20070511</creationdate><title>Unprocessed barley aleurone endo-β-1,4-xylanase X-I is an active enzyme</title><author>Van Campenhout, Steven ; Pollet, Annick ; Bourgois, Tine M. ; Rombouts, Sigrid ; Beaugrand, Johnny ; Gebruers, Kurt ; De Backer, Evelien ; Courtin, Christophe M. ; Delcour, Jan A. ; Volckaert, Guido</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c354t-7f22030adb4e0b3b17c941299eb8fe6603e38b1efc1f3baa3bdb27ae9d079843</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Cloning, Molecular</topic><topic>Cytoplasmic xylanase</topic><topic>Endo-1,4-beta Xylanases - chemistry</topic><topic>Endo-1,4-beta Xylanases - metabolism</topic><topic>Enzyme Stability</topic><topic>Escherichia coli</topic><topic>Escherichia coli - metabolism</topic><topic>Germination - physiology</topic><topic>Germination enzyme</topic><topic>Heteroxylan hydrolysis</topic><topic>Hordeum - enzymology</topic><topic>Hordeum vulgare</topic><topic>Hydrogen-Ion Concentration</topic><topic>Isoelectric Point</topic><topic>Kinetics</topic><topic>Molecular Weight</topic><topic>Temperature</topic><topic>Xylans - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Van Campenhout, Steven</creatorcontrib><creatorcontrib>Pollet, Annick</creatorcontrib><creatorcontrib>Bourgois, Tine M.</creatorcontrib><creatorcontrib>Rombouts, Sigrid</creatorcontrib><creatorcontrib>Beaugrand, Johnny</creatorcontrib><creatorcontrib>Gebruers, Kurt</creatorcontrib><creatorcontrib>De Backer, Evelien</creatorcontrib><creatorcontrib>Courtin, Christophe M.</creatorcontrib><creatorcontrib>Delcour, Jan A.</creatorcontrib><creatorcontrib>Volckaert, Guido</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Van Campenhout, Steven</au><au>Pollet, Annick</au><au>Bourgois, Tine M.</au><au>Rombouts, Sigrid</au><au>Beaugrand, Johnny</au><au>Gebruers, Kurt</au><au>De Backer, Evelien</au><au>Courtin, Christophe M.</au><au>Delcour, Jan A.</au><au>Volckaert, Guido</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Unprocessed barley aleurone endo-β-1,4-xylanase X-I is an active enzyme</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2007-05-11</date><risdate>2007</risdate><volume>356</volume><issue>3</issue><spage>799</spage><epage>804</epage><pages>799-804</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Endo-β-1,4-xylanase X-I is a major hydrolase produced by the aleurone tissue of germinating barley grain. It was previously reported that this cytosolic enzyme is synthesized as an inactive precursor which is proteolytically processed to active forms upon its programmed cell death dependent release. We here demonstrate, however, that the precursor form of X-I is an active enzyme. Purified recombinant precursor X-I was characterised with respect to its molecular weight, iso-electric point and temperature and pH activity and stability. Analysis of the hydrolysis products showed that it is an endo-acting enzyme which has the striking ability to release xylose from both polymeric xylan as well as from small xylo-oligosaccharides. The implications of these findings in relation to the putative role of the N-terminal propeptide as a carbohydrate binding module and the possible consequences for the way X-I fulfils its role in the germination process, are discussed.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>17383610</pmid><doi>10.1016/j.bbrc.2007.03.066</doi><tpages>6</tpages></addata></record> |
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| subjects | Cloning, Molecular Cytoplasmic xylanase Endo-1,4-beta Xylanases - chemistry Endo-1,4-beta Xylanases - metabolism Enzyme Stability Escherichia coli Escherichia coli - metabolism Germination - physiology Germination enzyme Heteroxylan hydrolysis Hordeum - enzymology Hordeum vulgare Hydrogen-Ion Concentration Isoelectric Point Kinetics Molecular Weight Temperature Xylans - metabolism |
| title | Unprocessed barley aleurone endo-β-1,4-xylanase X-I is an active enzyme |
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