Links to Exploration step
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Direct Sulfhydrylation for Methionine Biosynthesis in <italic>Leptospira meyeri</italic></title><author><name sortKey="Belfaiza, J" sort="Belfaiza, J" uniqKey="Belfaiza J" first="J." last="Belfaiza">J. Belfaiza</name><affiliation><nlm:aff id="N0x9b80980.0x9e1eca0"></nlm:aff></affiliation></author><author><name sortKey="Martel, A" sort="Martel, A" uniqKey="Martel A" first="A." last="Martel">A. Martel</name><affiliation><nlm:aff id="N0x9b80980.0x9e1eca0"></nlm:aff></affiliation></author><author><name sortKey="Margarita, D" sort="Margarita, D" uniqKey="Margarita D" first="D." last="Margarita">D. Margarita</name><affiliation><nlm:aff id="N0x9b80980.0x9e1eca0"></nlm:aff></affiliation></author><author><name sortKey="Saint Girons, I" sort="Saint Girons, I" uniqKey="Saint Girons I" first="I." last="Saint Girons">I. Saint Girons</name><affiliation><nlm:aff id="N0x9b80980.0x9e1eca0"></nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">9440513</idno><idno type="pmc">106879</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC106879</idno><idno type="RBID">PMC:106879</idno><date when="1998">1998</date><idno type="wicri:Area/Pmc/Corpus">000023</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000023</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Direct Sulfhydrylation for Methionine Biosynthesis in <italic>Leptospira meyeri</italic></title><author><name sortKey="Belfaiza, J" sort="Belfaiza, J" uniqKey="Belfaiza J" first="J." last="Belfaiza">J. Belfaiza</name><affiliation><nlm:aff id="N0x9b80980.0x9e1eca0"></nlm:aff></affiliation></author><author><name sortKey="Martel, A" sort="Martel, A" uniqKey="Martel A" first="A." last="Martel">A. Martel</name><affiliation><nlm:aff id="N0x9b80980.0x9e1eca0"></nlm:aff></affiliation></author><author><name sortKey="Margarita, D" sort="Margarita, D" uniqKey="Margarita D" first="D." last="Margarita">D. Margarita</name><affiliation><nlm:aff id="N0x9b80980.0x9e1eca0"></nlm:aff></affiliation></author><author><name sortKey="Saint Girons, I" sort="Saint Girons, I" uniqKey="Saint Girons I" first="I." last="Saint Girons">I. Saint Girons</name><affiliation><nlm:aff id="N0x9b80980.0x9e1eca0"></nlm:aff></affiliation></author></analytic><series><title level="j">Journal of Bacteriology</title><idno type="ISSN">0021-9193</idno><idno type="eISSN">1098-5530</idno><imprint><date when="1998">1998</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>A gene library of the <italic>Leptospira meyeri</italic> serovar semaranga strain Veldrat S.173 DNA has been constructed in a mobilizable cosmid with inserts of up to 40 kb. It was demonstrated that a <italic>Leptospira</italic> DNA fragment carrying <italic>metY</italic> complemented <italic>Escherichia coli</italic> strains carrying mutations in <italic>metB</italic>. The latter gene encodes cystathionine γ-synthase, an enzyme which catalyzes the second step of the methionine biosynthetic pathway. The <italic>metY</italic> gene is 1,304 bp long and encodes a 443-amino-acid protein with a molecular mass of 45 kDa as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The deduced amino acid sequence of the <italic>Leptospira metY</italic> product has a high degree of similarity to those of <italic>O</italic>-acetylhomoserine sulfhydrylases from <italic>Aspergillus nidulans</italic> and <italic>Saccharomyces cerevisiae</italic>. A lower degree of sequence similarity was also found with bacterial cystathionine γ-synthase. The <italic>L. meyeri metY</italic> gene was overexpressed under the control of the T7 promoter. MetY exhibits an <italic>O</italic>-acetylhomoserine sulfhydrylase activity. Genetic, enzymatic, and physiological studies reveal that the transsulfuration pathway via cystathionine does not exist in <italic>L. meyeri</italic>, in contrast to the situation found for fungi and some bacteria. Our results indicate, therefore, that the <italic>L. meyeri</italic> MetY enzyme is able to perform direct sulfhydrylation for methionine biosynthesis by using <italic>O</italic>-acetylhomoserine as a substrate.</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 Bacteriol</journal-id><journal-id journal-id-type="publisher-id">J BACTERIOL</journal-id><journal-title>Journal of Bacteriology</journal-title><issn pub-type="ppub">0021-9193</issn><issn pub-type="epub">1098-5530</issn><publisher><publisher-name>American Society for Microbiology</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">9440513</article-id><article-id pub-id-type="pmc">106879</article-id><article-id pub-id-type="publisher-id">1052</article-id><article-categories><subj-group subj-group-type="heading"><subject>Enzymes and Proteins</subject></subj-group></article-categories><title-group><article-title>Direct Sulfhydrylation for Methionine Biosynthesis in <italic>Leptospira meyeri</italic></article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Belfaiza</surname><given-names>J.</given-names></name><xref ref-type="aff" rid="N0x9b80980.0x9e1eca0">1</xref></contrib><contrib contrib-type="author"><name><surname>Martel</surname><given-names>A.</given-names></name><xref ref-type="aff" rid="N0x9b80980.0x9e1eca0">2</xref></contrib><contrib contrib-type="author"><name><surname>Margarita</surname><given-names>D.</given-names></name><xref ref-type="aff" rid="N0x9b80980.0x9e1eca0">3</xref></contrib><contrib contrib-type="author"><name><surname>Saint Girons</surname><given-names>I.</given-names></name><xref ref-type="aff" rid="N0x9b80980.0x9e1eca0">3</xref><xref ref-type="author-notes" rid="FN150">*</xref></contrib></contrib-group><aff id="N0x9b80980.0x9e1eca0"> Faculté des Sciences d’El-Jadida, Université Chouaib Doukkali, El-Jadida, Morocco,<sup>1</sup> and Laboratoire de Bioorganique et Biotechnologies, Ecole Nationale Supérieure de Chimie de Paris, 75005 Paris,<sup>2</sup> and Unité de Bactériologie Moléculaire et Médicale, Institut Pasteur, 75724 Paris Cedex 15,<sup>3</sup> France</aff><author-notes><fn id="FN150"><label>*</label><p>Corresponding author. Mailing address: Unité de Bactériologie Moléculaire et Médicale, 25, rue du docteur Roux, Institut Pasteur, 75724 Paris Cedex 15, France. Phone: 33 (0)1 45 68 83 66. Fax: 33 (0)1 40 61 30 01. E-mail: <email>isgirons@pasteur.fr</email>.</p></fn></author-notes><pub-date pub-type="ppub"><month>1</month><year>1998</year></pub-date><volume>180</volume><issue>2</issue><fpage>250</fpage><lpage>255</lpage><history><date date-type="received"><day>30</day><month>7</month><year>1997</year></date><date date-type="accepted"><day>13</day><month>11</month><year>1997</year></date></history><copyright-statement>Copyright © 1998, American Society for Microbiology</copyright-statement><copyright-year>1998</copyright-year><abstract><p>A gene library of the <italic>Leptospira meyeri</italic> serovar semaranga strain Veldrat S.173 DNA has been constructed in a mobilizable cosmid with inserts of up to 40 kb. It was demonstrated that a <italic>Leptospira</italic> DNA fragment carrying <italic>metY</italic> complemented <italic>Escherichia coli</italic> strains carrying mutations in <italic>metB</italic>. The latter gene encodes cystathionine γ-synthase, an enzyme which catalyzes the second step of the methionine biosynthetic pathway. The <italic>metY</italic> gene is 1,304 bp long and encodes a 443-amino-acid protein with a molecular mass of 45 kDa as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The deduced amino acid sequence of the <italic>Leptospira metY</italic> product has a high degree of similarity to those of <italic>O</italic>-acetylhomoserine sulfhydrylases from <italic>Aspergillus nidulans</italic> and <italic>Saccharomyces cerevisiae</italic>. A lower degree of sequence similarity was also found with bacterial cystathionine γ-synthase. The <italic>L. meyeri metY</italic> gene was overexpressed under the control of the T7 promoter. MetY exhibits an <italic>O</italic>-acetylhomoserine sulfhydrylase activity. Genetic, enzymatic, and physiological studies reveal that the transsulfuration pathway via cystathionine does not exist in <italic>L. meyeri</italic>, in contrast to the situation found for fungi and some bacteria. Our results indicate, therefore, that the <italic>L. meyeri</italic> MetY enzyme is able to perform direct sulfhydrylation for methionine biosynthesis by using <italic>O</italic>-acetylhomoserine as a substrate.</p></abstract></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Sante/explor/MaghrebDataLibMedV2/Data/Pmc/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 0000230 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Pmc/Corpus/biblio.hfd -nk 0000230 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Wicri/Sante
|area= MaghrebDataLibMedV2
|flux= Pmc
|étape= Corpus
|type= RBID
|clé=
|texte=
}}
| This area was generated with Dilib version V0.6.38. |  |