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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Novel Isonitrile Hydratase Involved in Isonitrile Metabolism<xref ref-type="fn" rid="FN1">*</xref></title><author><name sortKey="Sato, Hiroyoshi" sort="Sato, Hiroyoshi" uniqKey="Sato H" first="Hiroyoshi" last="Sato">Hiroyoshi Sato</name><affiliation><nlm:aff id="aff1">From the Institute of Applied Biochemistry and Graduate School of Life and Environmental Sciences, The University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8572, Japan</nlm:aff></affiliation></author><author><name sortKey="Hashimoto, Yoshiteru" sort="Hashimoto, Yoshiteru" uniqKey="Hashimoto Y" first="Yoshiteru" last="Hashimoto">Yoshiteru Hashimoto</name><affiliation><nlm:aff id="aff1">From the Institute of Applied Biochemistry and Graduate School of Life and Environmental Sciences, The University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8572, Japan</nlm:aff></affiliation></author><author><name sortKey="Fukatsu, Hiroshi" sort="Fukatsu, Hiroshi" uniqKey="Fukatsu H" first="Hiroshi" last="Fukatsu">Hiroshi Fukatsu</name><affiliation><nlm:aff id="aff1">From the Institute of Applied Biochemistry and Graduate School of Life and Environmental Sciences, The University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8572, Japan</nlm:aff></affiliation></author><author><name sortKey="Kobayashi, Michihiko" sort="Kobayashi, Michihiko" uniqKey="Kobayashi M" first="Michihiko" last="Kobayashi">Michihiko Kobayashi</name><affiliation><nlm:aff id="aff1">From the Institute of Applied Biochemistry and Graduate School of Life and Environmental Sciences, The University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8572, Japan</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">20826798</idno><idno type="pmc">2966095</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2966095</idno><idno type="RBID">PMC:2966095</idno><idno type="doi">10.1074/jbc.M110.150227</idno><date when="2010">2010</date><idno type="wicri:Area/Pmc/Corpus">000276</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000276</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Novel Isonitrile Hydratase Involved in Isonitrile Metabolism<xref ref-type="fn" rid="FN1">*</xref></title><author><name sortKey="Sato, Hiroyoshi" sort="Sato, Hiroyoshi" uniqKey="Sato H" first="Hiroyoshi" last="Sato">Hiroyoshi Sato</name><affiliation><nlm:aff id="aff1">From the Institute of Applied Biochemistry and Graduate School of Life and Environmental Sciences, The University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8572, Japan</nlm:aff></affiliation></author><author><name sortKey="Hashimoto, Yoshiteru" sort="Hashimoto, Yoshiteru" uniqKey="Hashimoto Y" first="Yoshiteru" last="Hashimoto">Yoshiteru Hashimoto</name><affiliation><nlm:aff id="aff1">From the Institute of Applied Biochemistry and Graduate School of Life and Environmental Sciences, The University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8572, Japan</nlm:aff></affiliation></author><author><name sortKey="Fukatsu, Hiroshi" sort="Fukatsu, Hiroshi" uniqKey="Fukatsu H" first="Hiroshi" last="Fukatsu">Hiroshi Fukatsu</name><affiliation><nlm:aff id="aff1">From the Institute of Applied Biochemistry and Graduate School of Life and Environmental Sciences, The University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8572, Japan</nlm:aff></affiliation></author><author><name sortKey="Kobayashi, Michihiko" sort="Kobayashi, Michihiko" uniqKey="Kobayashi M" first="Michihiko" last="Kobayashi">Michihiko Kobayashi</name><affiliation><nlm:aff id="aff1">From the Institute of Applied Biochemistry and Graduate School of Life and Environmental Sciences, The University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8572, Japan</nlm:aff></affiliation></author></analytic><series><title level="j">The Journal of Biological Chemistry</title><idno type="ISSN">0021-9258</idno><idno type="eISSN">1083-351X</idno><imprint><date when="2010">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>We previously discovered <italic>N</italic>-substituted formamide deformylase (NfdA) in <italic>Arthrobacter pascens</italic> F164, which degrades <italic>N</italic>-substituted formamide (Fukatsu, H., Hashimoto, Y., Goda, M., Higashibata, H., and Kobayashi, M. (2004) <italic>Proc. Natl. Acad. Sci. U.S.A.</italic> 101, 13726–13731). In this study, we found an enzyme involved in the first step of isonitrile metabolism, isonitrile hydratase, that hydrates isonitrile to the corresponding <italic>N</italic>-substituted formamide. First, we investigated the optimum culture conditions for the production of isonitrile hydratase. The highest enzyme activity was obtained when <italic>A. pascens</italic> F164 was cultured in a nutrient medium containing <italic>N</italic>-benzylformamide. This <italic>Arthrobacter</italic> isonitrile hydratase was purified, characterized, and compared with <italic>Pseudomonas putida</italic> N19-2 isonitrile hydratase (InhA), which is the sole one reported at present. <italic>Arthrobacter</italic> isonitrile hydratase was found to have a molecular mass of about 530 kDa and to consist of 12 identical subunits. The apparent <italic>K<sub>m</sub></italic> value for cyclohexyl isocyanide was 0.95 ± 0.05 m<sc>m</sc>. <italic>A. pascens</italic> F164 grew and exhibited the isonitrile hydratase and <italic>N</italic>-substituted formamide deformylase activities when cultured in a medium containing an isonitrile as the sole carbon and nitrogen sources. However, both enzyme activities were not observed on culture in a medium containing glycerol and (NH<sub>4</sub>)<sub>2</sub>SO<sub>4</sub> as the sole carbon and nitrogen sources, respectively. These findings suggested that the <italic>Arthrobacter</italic> enzyme is an inducible enzyme, possibly involved in assimilation and/or detoxification of isonitrile. Moreover, gene cloning of the <italic>Arthrobacter</italic> enzyme revealed no sequence similarity between this enzyme and InhA. Comparison of their properties and features demonstrated that the two enzymes are biochemically, immunologically, and structurally different from each other. Thus, we discovered a new isonitrile hydratase named InhB.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">J Biol Chem</journal-id><journal-id journal-id-type="hwp">jbc</journal-id><journal-id journal-id-type="pmc">jbc</journal-id><journal-id journal-id-type="publisher-id">JBC</journal-id><journal-title-group><journal-title>The Journal of Biological Chemistry</journal-title></journal-title-group><issn pub-type="ppub">0021-9258</issn><issn pub-type="epub">1083-351X</issn><publisher><publisher-name>American Society for Biochemistry and Molecular Biology</publisher-name><publisher-loc>9650 Rockville Pike, Bethesda, MD 20814, U.S.A.</publisher-loc></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">20826798</article-id><article-id pub-id-type="pmc">2966095</article-id><article-id pub-id-type="publisher-id">M110.150227</article-id><article-id pub-id-type="doi">10.1074/jbc.M110.150227</article-id><article-categories><subj-group subj-group-type="heading"><subject>Enzymology</subject></subj-group><subj-group><subject>Metabolism</subject></subj-group></article-categories><title-group><article-title>Novel Isonitrile Hydratase Involved in Isonitrile Metabolism<xref ref-type="fn" rid="FN1">*</xref></article-title><alt-title alt-title-type="short">A New Type of Isonitrile Hydratase</alt-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Sato</surname><given-names>Hiroyoshi</given-names></name><xref ref-type="aff" rid="aff1"></xref><xref ref-type="author-notes" rid="FN2"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>Hashimoto</surname><given-names>Yoshiteru</given-names></name><xref ref-type="aff" rid="aff1"></xref><xref ref-type="author-notes" rid="FN2"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>Fukatsu</surname><given-names>Hiroshi</given-names></name><xref ref-type="aff" rid="aff1"></xref></contrib><contrib contrib-type="author"><name><surname>Kobayashi</surname><given-names>Michihiko</given-names></name><xref ref-type="aff" rid="aff1"></xref><xref ref-type="corresp" rid="cor1"><sup>2</sup></xref></contrib><aff id="aff1">From the Institute of Applied Biochemistry and Graduate School of Life and Environmental Sciences, The University of Tsukuba, 1-1-1 Tennodai, Tsukuba, Ibaraki 305-8572, Japan</aff></contrib-group><author-notes><corresp id="cor1"><label>2</label> To whom correspondence should be addressed. Fax: <fax>81-29-853-4605</fax>.</corresp><fn fn-type="equal" id="FN2"><label>1</label><p>Both authors contributed equally to this work.</p></fn></author-notes><pub-date pub-type="ppub"><day>5</day><month>11</month><year>2010</year></pub-date><pub-date pub-type="epub"><day>7</day><month>9</month><year>2010</year></pub-date><volume>285</volume><issue>45</issue><fpage>34793</fpage><lpage>34802</lpage><history><date date-type="received"><day>1</day><month>6</month><year>2010</year></date><date date-type="rev-recd"><day>3</day><month>9</month><year>2010</year></date></history><permissions><copyright-statement>© 2010 by The American Society for Biochemistry and Molecular Biology, Inc.</copyright-statement></permissions><self-uri xlink:title="pdf" xlink:type="simple" xlink:href="zbc04510034793.pdf"></self-uri><abstract><p>We previously discovered <italic>N</italic>-substituted formamide deformylase (NfdA) in <italic>Arthrobacter pascens</italic> F164, which degrades <italic>N</italic>-substituted formamide (Fukatsu, H., Hashimoto, Y., Goda, M., Higashibata, H., and Kobayashi, M. (2004) <italic>Proc. Natl. Acad. Sci. U.S.A.</italic> 101, 13726–13731). In this study, we found an enzyme involved in the first step of isonitrile metabolism, isonitrile hydratase, that hydrates isonitrile to the corresponding <italic>N</italic>-substituted formamide. First, we investigated the optimum culture conditions for the production of isonitrile hydratase. The highest enzyme activity was obtained when <italic>A. pascens</italic> F164 was cultured in a nutrient medium containing <italic>N</italic>-benzylformamide. This <italic>Arthrobacter</italic> isonitrile hydratase was purified, characterized, and compared with <italic>Pseudomonas putida</italic> N19-2 isonitrile hydratase (InhA), which is the sole one reported at present. <italic>Arthrobacter</italic> isonitrile hydratase was found to have a molecular mass of about 530 kDa and to consist of 12 identical subunits. The apparent <italic>K<sub>m</sub></italic> value for cyclohexyl isocyanide was 0.95 ± 0.05 m<sc>m</sc>. <italic>A. pascens</italic> F164 grew and exhibited the isonitrile hydratase and <italic>N</italic>-substituted formamide deformylase activities when cultured in a medium containing an isonitrile as the sole carbon and nitrogen sources. However, both enzyme activities were not observed on culture in a medium containing glycerol and (NH<sub>4</sub>)<sub>2</sub>SO<sub>4</sub> as the sole carbon and nitrogen sources, respectively. These findings suggested that the <italic>Arthrobacter</italic> enzyme is an inducible enzyme, possibly involved in assimilation and/or detoxification of isonitrile. Moreover, gene cloning of the <italic>Arthrobacter</italic> enzyme revealed no sequence similarity between this enzyme and InhA. Comparison of their properties and features demonstrated that the two enzymes are biochemically, immunologically, and structurally different from each other. Thus, we discovered a new isonitrile hydratase named InhB.</p></abstract><kwd-group><kwd>Enzyme Kinetics</kwd><kwd>Enzyme Purification</kwd><kwd>Enzyme Structure</kwd><kwd>Enzymes</kwd><kwd>Metabolism</kwd><kwd>N-Substituted Formamide</kwd><kwd>Isonitrile Hydratase</kwd></kwd-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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