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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Characterization of an Inducible Chlorophenol <italic>O</italic>-Methyltransferase from <italic>Trichoderma longibrachiatum</italic> Involved in the Formation of Chloroanisoles and Determination of Its Role in Cork Taint of Wines</title><author><name sortKey="Coque, Juan Jose R" sort="Coque, Juan Jose R" uniqKey="Coque J" first="Juan-José R." last="Coque">Juan-José R. Coque</name><affiliation><nlm:aff id="aff0">Departamento de Microbiología, Facultad de Ciencias, Universidad de Extremadura, 06071 Badajoz, Spain</nlm:aff></affiliation></author><author><name sortKey="Alvarez Rodriguez, Maria Luisa" sort="Alvarez Rodriguez, Maria Luisa" uniqKey="Alvarez Rodriguez M" first="María Luisa" last="Álvarez-Rodríguez">María Luisa Álvarez-Rodríguez</name><affiliation><nlm:aff id="aff0">Departamento de Microbiología, Facultad de Ciencias, Universidad de Extremadura, 06071 Badajoz, Spain</nlm:aff></affiliation></author><author><name sortKey="Larriba, German" sort="Larriba, German" uniqKey="Larriba G" first="Germán" last="Larriba">Germán Larriba</name><affiliation><nlm:aff id="aff0">Departamento de Microbiología, Facultad de Ciencias, Universidad de Extremadura, 06071 Badajoz, Spain</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">12957890</idno><idno type="pmc">194934</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC194934</idno><idno type="RBID">PMC:194934</idno><idno type="doi">10.1128/AEM.69.9.5089-5095.2003</idno><date when="2003">2003</date><idno type="wicri:Area/Pmc/Corpus">000084</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000084</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Characterization of an Inducible Chlorophenol <italic>O</italic>-Methyltransferase from <italic>Trichoderma longibrachiatum</italic> Involved in the Formation of Chloroanisoles and Determination of Its Role in Cork Taint of Wines</title><author><name sortKey="Coque, Juan Jose R" sort="Coque, Juan Jose R" uniqKey="Coque J" first="Juan-José R." last="Coque">Juan-José R. Coque</name><affiliation><nlm:aff id="aff0">Departamento de Microbiología, Facultad de Ciencias, Universidad de Extremadura, 06071 Badajoz, Spain</nlm:aff></affiliation></author><author><name sortKey="Alvarez Rodriguez, Maria Luisa" sort="Alvarez Rodriguez, Maria Luisa" uniqKey="Alvarez Rodriguez M" first="María Luisa" last="Álvarez-Rodríguez">María Luisa Álvarez-Rodríguez</name><affiliation><nlm:aff id="aff0">Departamento de Microbiología, Facultad de Ciencias, Universidad de Extremadura, 06071 Badajoz, Spain</nlm:aff></affiliation></author><author><name sortKey="Larriba, German" sort="Larriba, German" uniqKey="Larriba G" first="Germán" last="Larriba">Germán Larriba</name><affiliation><nlm:aff id="aff0">Departamento de Microbiología, Facultad de Ciencias, Universidad de Extremadura, 06071 Badajoz, Spain</nlm:aff></affiliation></author></analytic><series><title level="j">Applied and Environmental Microbiology</title><idno type="ISSN">0099-2240</idno><idno type="eISSN">1098-5336</idno><imprint><date when="2003">2003</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>A novel <italic>S</italic>-adenosyl-<sc>l</sc>-methionine (SAM)-dependent methyltransferase catalyzing the O methylation of several chlorophenols and other halogenated phenols was purified 220-fold to apparent homogeneity from mycelia of <italic>Trichoderma longibrachiatum</italic> CECT 20431. The enzyme could be identified in partially purified protein preparations by direct photolabeling with [<italic>methyl</italic>-<sup>3</sup>H]SAM, and this reaction was prevented by previous incubation with <italic>S</italic>-adenosylhomocysteine. Gel filtration indicated that the <italic>M</italic><sub>r</sub> was 112,000, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed that the enzyme was composed of two subunits with molecular weights of approximately 52,500. The enzyme had a pH optimum between 8.2 and 8.5 and an optimum temperature of 28°C, with a pI of 4.9. The <italic>K<sub>m</sub></italic> values for 2,4,6-trichlorophenol and SAM were 135.9 ± 12.8 and 284.1 ± 35.1 μM, respectively. <italic>S</italic>-Adenosylhomocysteine acted as a competitive inhibitor, with a <italic>K<sub>i</sub></italic> of 378.9 ± 45.4 μM. The methyltransferase was also strongly inhibited by low concentrations of several metal ions, such as Cu<sup>2+</sup>, Hg<sup>2+</sup>, Zn<sup>2+</sup>, and Ag<sup>+</sup>, and to a lesser extent by <italic>p</italic>-chloromercuribenzoic acid, but it was not significantly affected by several thiols or other thiol reagents. The methyltransferase was specifically induced by several chlorophenols, especially if they contained three or more chlorine atoms in their structures. Substrate specificity studies showed that the activity was also specific for halogenated phenols containing fluoro, chloro, or bromo substituents, whereas other hydroxylated compounds, such as hydroxylated benzoic acids, hydroxybenzaldehydes, phenol, 2-metoxyphenol, and dihydroxybenzene, were not methylated.</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">Appl Environ Microbiol</journal-id><journal-id journal-id-type="publisher-id">aem</journal-id><journal-title>Applied and Environmental Microbiology</journal-title><issn pub-type="ppub">0099-2240</issn><issn pub-type="epub">1098-5336</issn><publisher><publisher-name>American Society for Microbiology</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">12957890</article-id><article-id pub-id-type="pmc">194934</article-id><article-id pub-id-type="publisher-id">0278</article-id><article-id pub-id-type="doi">10.1128/AEM.69.9.5089-5095.2003</article-id><article-categories><subj-group subj-group-type="heading"><subject>Food Microbiology</subject></subj-group></article-categories><title-group><article-title>Characterization of an Inducible Chlorophenol <italic>O</italic>-Methyltransferase from <italic>Trichoderma longibrachiatum</italic> Involved in the Formation of Chloroanisoles and Determination of Its Role in Cork Taint of Wines</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Coque</surname><given-names>Juan-José R.</given-names></name><xref ref-type="aff" rid="aff0"></xref><xref ref-type="corresp" rid="cor1">*</xref></contrib><contrib contrib-type="author"><name><surname>Álvarez-Rodríguez</surname><given-names>María Luisa</given-names></name><xref ref-type="aff" rid="aff0"></xref></contrib><contrib contrib-type="author"><name><surname>Larriba</surname><given-names>Germán</given-names></name><xref ref-type="aff" rid="aff0"></xref></contrib></contrib-group><aff id="aff0">Departamento de Microbiología, Facultad de Ciencias, Universidad de Extremadura, 06071 Badajoz, Spain</aff><author-notes><fn id="cor1"><label>*</label><p>Corresponding author. Mailing address: Departamento de Microbiología, Facultad de Ciencias, Universidad de Extremadura, Avenida de Elvas s/n, 06071 Badajoz, Spain. Phone and fax: 34-924-289424. E-mail: <email>jjrubio@unex.es</email>.</p></fn></author-notes><pub-date pub-type="ppub"><month>9</month><year>2003</year></pub-date><volume>69</volume><issue>9</issue><fpage>5089</fpage><lpage>5095</lpage><history><date date-type="received"><day>21</day><month>2</month><year>2003</year></date><date date-type="accepted"><day>6</day><month>6</month><year>2003</year></date></history><copyright-statement>Copyright © 2003, American Society for Microbiology</copyright-statement><copyright-year>2003</copyright-year><abstract><p>A novel <italic>S</italic>-adenosyl-<sc>l</sc>-methionine (SAM)-dependent methyltransferase catalyzing the O methylation of several chlorophenols and other halogenated phenols was purified 220-fold to apparent homogeneity from mycelia of <italic>Trichoderma longibrachiatum</italic> CECT 20431. The enzyme could be identified in partially purified protein preparations by direct photolabeling with [<italic>methyl</italic>-<sup>3</sup>H]SAM, and this reaction was prevented by previous incubation with <italic>S</italic>-adenosylhomocysteine. Gel filtration indicated that the <italic>M</italic><sub>r</sub> was 112,000, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed that the enzyme was composed of two subunits with molecular weights of approximately 52,500. The enzyme had a pH optimum between 8.2 and 8.5 and an optimum temperature of 28°C, with a pI of 4.9. The <italic>K<sub>m</sub></italic> values for 2,4,6-trichlorophenol and SAM were 135.9 ± 12.8 and 284.1 ± 35.1 μM, respectively. <italic>S</italic>-Adenosylhomocysteine acted as a competitive inhibitor, with a <italic>K<sub>i</sub></italic> of 378.9 ± 45.4 μM. The methyltransferase was also strongly inhibited by low concentrations of several metal ions, such as Cu<sup>2+</sup>, Hg<sup>2+</sup>, Zn<sup>2+</sup>, and Ag<sup>+</sup>, and to a lesser extent by <italic>p</italic>-chloromercuribenzoic acid, but it was not significantly affected by several thiols or other thiol reagents. The methyltransferase was specifically induced by several chlorophenols, especially if they contained three or more chlorine atoms in their structures. Substrate specificity studies showed that the activity was also specific for halogenated phenols containing fluoro, chloro, or bromo substituents, whereas other hydroxylated compounds, such as hydroxylated benzoic acids, hydroxybenzaldehydes, phenol, 2-metoxyphenol, and dihydroxybenzene, were not methylated.</p></abstract></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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