High substrate specificity and induction characteristics of trimethylamine- N -oxide reductase of Escherichia coli
Identifieur interne : 002894 ( Istex/Corpus ); précédent : 002893; suivant : 002895High substrate specificity and induction characteristics of trimethylamine- N -oxide reductase of Escherichia coli
Auteurs : Chantal Iobbi-Nivol ; Janine Pommier ; Joanne Simala-Grant ; Vincent Méjean ; Gérard GiordanoSource :
- Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology [ 0167-4838 ] ; 1996.
Abstract
Using a wide variety of N- and S-oxide compounds we have shown by kinetic analysis that only two N-oxidestrimethylamine-N-oxide and 4-methylmorpholine-N-oxide, can be considered good substrates for trimethylamine-N-oxide (TMAO) reductase on the basis of their kcat Km ratio. This result demonstrates that TMAO reductase possesses a high substrate specificity. Induction of the torCAD operon using the same S- and N-oxide compounds was also analyzed. We demonstrate that there is no correlation between the ability for a compound to be reduced by TMAO reductase and to induce TMAO reductase synthesis.
Url:
DOI: 10.1016/0167-4838(95)00271-5
Links to Exploration step
ISTEX:DA385A7331C8B4A076EAE6482CC0FDBDD32CCFCCLe document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title>High substrate specificity and induction characteristics of trimethylamine- N -oxide reductase of Escherichia coli</title>
<author><name sortKey="Iobbi Nivol, Chantal" sort="Iobbi Nivol, Chantal" uniqKey="Iobbi Nivol C" first="Chantal" last="Iobbi-Nivol">Chantal Iobbi-Nivol</name>
<affiliation><mods:affiliation>Laboratoire de Chimie Bactérienne, Institut Fédératif Biologie Structurale et Microbiologie (IFRC1), CNRS, 31, Chemin J. Aiguier, 13402 Marseille, France</mods:affiliation>
</affiliation>
</author>
<author><name sortKey="Pommier, Janine" sort="Pommier, Janine" uniqKey="Pommier J" first="Janine" last="Pommier">Janine Pommier</name>
<affiliation><mods:affiliation>Laboratoire de Chimie Bactérienne, Institut Fédératif Biologie Structurale et Microbiologie (IFRC1), CNRS, 31, Chemin J. Aiguier, 13402 Marseille, France</mods:affiliation>
</affiliation>
</author>
<author><name sortKey="Simala Grant, Joanne" sort="Simala Grant, Joanne" uniqKey="Simala Grant J" first="Joanne" last="Simala-Grant">Joanne Simala-Grant</name>
<affiliation><mods:affiliation>Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H, Canada</mods:affiliation>
</affiliation>
</author>
<author><name sortKey="Mejean, Vincent" sort="Mejean, Vincent" uniqKey="Mejean V" first="Vincent" last="Méjean">Vincent Méjean</name>
<affiliation><mods:affiliation>Laboratoire de Chimie Bactérienne, Institut Fédératif Biologie Structurale et Microbiologie (IFRC1), CNRS, 31, Chemin J. Aiguier, 13402 Marseille, France</mods:affiliation>
</affiliation>
</author>
<author><name sortKey="Giordano, Gerard" sort="Giordano, Gerard" uniqKey="Giordano G" first="Gérard" last="Giordano">Gérard Giordano</name>
<affiliation><mods:affiliation>Corresponding author. Fax: +33 91 718914.</mods:affiliation>
</affiliation>
<affiliation><mods:affiliation>Laboratoire de Chimie Bactérienne, Institut Fédératif Biologie Structurale et Microbiologie (IFRC1), CNRS, 31, Chemin J. Aiguier, 13402 Marseille, France</mods:affiliation>
</affiliation>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">ISTEX</idno>
<idno type="RBID">ISTEX:DA385A7331C8B4A076EAE6482CC0FDBDD32CCFCC</idno>
<date when="1996" year="1996">1996</date>
<idno type="doi">10.1016/0167-4838(95)00271-5</idno>
<idno type="url">https://api-v5.istex.fr/document/DA385A7331C8B4A076EAE6482CC0FDBDD32CCFCC/fulltext/pdf</idno>
<idno type="wicri:Area/Istex/Corpus">002894</idno>
<idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">002894</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title level="a">High substrate specificity and induction characteristics of trimethylamine- N -oxide reductase of Escherichia coli</title>
<author><name sortKey="Iobbi Nivol, Chantal" sort="Iobbi Nivol, Chantal" uniqKey="Iobbi Nivol C" first="Chantal" last="Iobbi-Nivol">Chantal Iobbi-Nivol</name>
<affiliation><mods:affiliation>Laboratoire de Chimie Bactérienne, Institut Fédératif Biologie Structurale et Microbiologie (IFRC1), CNRS, 31, Chemin J. Aiguier, 13402 Marseille, France</mods:affiliation>
</affiliation>
</author>
<author><name sortKey="Pommier, Janine" sort="Pommier, Janine" uniqKey="Pommier J" first="Janine" last="Pommier">Janine Pommier</name>
<affiliation><mods:affiliation>Laboratoire de Chimie Bactérienne, Institut Fédératif Biologie Structurale et Microbiologie (IFRC1), CNRS, 31, Chemin J. Aiguier, 13402 Marseille, France</mods:affiliation>
</affiliation>
</author>
<author><name sortKey="Simala Grant, Joanne" sort="Simala Grant, Joanne" uniqKey="Simala Grant J" first="Joanne" last="Simala-Grant">Joanne Simala-Grant</name>
<affiliation><mods:affiliation>Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H, Canada</mods:affiliation>
</affiliation>
</author>
<author><name sortKey="Mejean, Vincent" sort="Mejean, Vincent" uniqKey="Mejean V" first="Vincent" last="Méjean">Vincent Méjean</name>
<affiliation><mods:affiliation>Laboratoire de Chimie Bactérienne, Institut Fédératif Biologie Structurale et Microbiologie (IFRC1), CNRS, 31, Chemin J. Aiguier, 13402 Marseille, France</mods:affiliation>
</affiliation>
</author>
<author><name sortKey="Giordano, Gerard" sort="Giordano, Gerard" uniqKey="Giordano G" first="Gérard" last="Giordano">Gérard Giordano</name>
<affiliation><mods:affiliation>Corresponding author. Fax: +33 91 718914.</mods:affiliation>
</affiliation>
<affiliation><mods:affiliation>Laboratoire de Chimie Bactérienne, Institut Fédératif Biologie Structurale et Microbiologie (IFRC1), CNRS, 31, Chemin J. Aiguier, 13402 Marseille, France</mods:affiliation>
</affiliation>
</author>
</analytic>
<monogr></monogr>
<series><title level="j">Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology</title>
<title level="j" type="abbrev">BBAPRO</title>
<idno type="ISSN">0167-4838</idno>
<imprint><publisher>ELSEVIER</publisher>
<date type="published" when="1996">1996</date>
<biblScope unit="volume">1294</biblScope>
<biblScope unit="issue">1</biblScope>
<biblScope unit="page" from="77">77</biblScope>
<biblScope unit="page" to="82">82</biblScope>
</imprint>
<idno type="ISSN">0167-4838</idno>
</series>
</biblStruct>
</sourceDesc>
<seriesStmt><idno type="ISSN">0167-4838</idno>
</seriesStmt>
</fileDesc>
<profileDesc><textClass></textClass>
<langUsage><language ident="en">en</language>
</langUsage>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Using a wide variety of N- and S-oxide compounds we have shown by kinetic analysis that only two N-oxidestrimethylamine-N-oxide and 4-methylmorpholine-N-oxide, can be considered good substrates for trimethylamine-N-oxide (TMAO) reductase on the basis of their kcat Km ratio. This result demonstrates that TMAO reductase possesses a high substrate specificity. Induction of the torCAD operon using the same S- and N-oxide compounds was also analyzed. We demonstrate that there is no correlation between the ability for a compound to be reduced by TMAO reductase and to induce TMAO reductase synthesis.</div>
</front>
</TEI>
<istex><corpusName>elsevier</corpusName>
<author><json:item><name>Chantal Iobbi-Nivol</name>
<affiliations><json:string>Laboratoire de Chimie Bactérienne, Institut Fédératif Biologie Structurale et Microbiologie (IFRC1), CNRS, 31, Chemin J. Aiguier, 13402 Marseille, France</json:string>
</affiliations>
</json:item>
<json:item><name>Janine Pommier</name>
<affiliations><json:string>Laboratoire de Chimie Bactérienne, Institut Fédératif Biologie Structurale et Microbiologie (IFRC1), CNRS, 31, Chemin J. Aiguier, 13402 Marseille, France</json:string>
</affiliations>
</json:item>
<json:item><name>Joanne Simala-Grant</name>
<affiliations><json:string>Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H, Canada</json:string>
</affiliations>
</json:item>
<json:item><name>Vincent Méjean</name>
<affiliations><json:string>Laboratoire de Chimie Bactérienne, Institut Fédératif Biologie Structurale et Microbiologie (IFRC1), CNRS, 31, Chemin J. Aiguier, 13402 Marseille, France</json:string>
</affiliations>
</json:item>
<json:item><name>Gérard Giordano</name>
<affiliations><json:string>Corresponding author. Fax: +33 91 718914.</json:string>
<json:string>Laboratoire de Chimie Bactérienne, Institut Fédératif Biologie Structurale et Microbiologie (IFRC1), CNRS, 31, Chemin J. Aiguier, 13402 Marseille, France</json:string>
</affiliations>
</json:item>
</author>
<subject><json:item><lang><json:string>eng</json:string>
</lang>
<value>Trimethylamine-N-oxide reductase</value>
</json:item>
<json:item><lang><json:string>eng</json:string>
</lang>
<value>Reductase activity</value>
</json:item>
<json:item><lang><json:string>eng</json:string>
</lang>
<value>Reductase induction</value>
</json:item>
<json:item><lang><json:string>eng</json:string>
</lang>
<value>Molybdoenzyme</value>
</json:item>
<json:item><lang><json:string>eng</json:string>
</lang>
<value>(E. coli)</value>
</json:item>
<json:item><lang><json:string>eng</json:string>
</lang>
<value>DMSO : dimethylsulfoxide</value>
</json:item>
<json:item><lang><json:string>eng</json:string>
</lang>
<value>LDAO : N , N -dimethyldodecylamine- N -oxide</value>
</json:item>
<json:item><lang><json:string>eng</json:string>
</lang>
<value>TMAO : trimethylamine- N -oxide</value>
</json:item>
<json:item><lang><json:string>eng</json:string>
</lang>
<value>TMSO : tetramethylenesulfoxide</value>
</json:item>
</subject>
<language><json:string>eng</json:string>
</language>
<originalGenre><json:string>Full-length article</json:string>
</originalGenre>
<abstract>Using a wide variety of N- and S-oxide compounds we have shown by kinetic analysis that only two N-oxidestrimethylamine-N-oxide and 4-methylmorpholine-N-oxide, can be considered good substrates for trimethylamine-N-oxide (TMAO) reductase on the basis of their kcat Km ratio. This result demonstrates that TMAO reductase possesses a high substrate specificity. Induction of the torCAD operon using the same S- and N-oxide compounds was also analyzed. We demonstrate that there is no correlation between the ability for a compound to be reduced by TMAO reductase and to induce TMAO reductase synthesis.</abstract>
<qualityIndicators><score>4.506</score>
<pdfWordCount>3438</pdfWordCount>
<pdfCharCount>19898</pdfCharCount>
<pdfVersion>1.2</pdfVersion>
<pdfPageCount>6</pdfPageCount>
<pdfPageSize>591 x 807 pts</pdfPageSize>
<refBibsNative>true</refBibsNative>
<abstractWordCount>89</abstractWordCount>
<abstractCharCount>600</abstractCharCount>
<keywordCount>9</keywordCount>
</qualityIndicators>
<title>High substrate specificity and induction characteristics of trimethylamine- N -oxide reductase of Escherichia coli</title>
<pii><json:string>0167-4838(95)00271-5</json:string>
</pii>
<genre><json:string>research-article</json:string>
</genre>
<host><title>Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology</title>
<language><json:string>unknown</json:string>
</language>
<publicationDate>1996</publicationDate>
<issn><json:string>0167-4838</json:string>
</issn>
<pii><json:string>S0167-4838(00)X0003-9</json:string>
</pii>
<volume>1294</volume>
<issue>1</issue>
<pages><first>77</first>
<last>82</last>
</pages>
<genre><json:string>journal</json:string>
</genre>
</host>
<categories><wos></wos>
<scienceMetrix><json:string>health sciences</json:string>
<json:string>biomedical research</json:string>
<json:string>biophysics</json:string>
</scienceMetrix>
<inist><json:string>sciences appliquees, technologies et medecines</json:string>
<json:string>sciences biologiques et medicales</json:string>
<json:string>sciences biologiques fondamentales et appliquees. psychologie</json:string>
</inist>
</categories>
<publicationDate>1996</publicationDate>
<copyrightDate>1996</copyrightDate>
<doi><json:string>10.1016/0167-4838(95)00271-5</json:string>
</doi>
<id>DA385A7331C8B4A076EAE6482CC0FDBDD32CCFCC</id>
<fulltext><json:item><extension>pdf</extension>
<original>true</original>
<mimetype>application/pdf</mimetype>
<uri>https://api-v5.istex.fr/document/DA385A7331C8B4A076EAE6482CC0FDBDD32CCFCC/fulltext/pdf</uri>
</json:item>
<json:item><extension>zip</extension>
<original>false</original>
<mimetype>application/zip</mimetype>
<uri>https://api-v5.istex.fr/document/DA385A7331C8B4A076EAE6482CC0FDBDD32CCFCC/fulltext/zip</uri>
</json:item>
<istex:fulltextTEI uri="https://api-v5.istex.fr/document/DA385A7331C8B4A076EAE6482CC0FDBDD32CCFCC/fulltext/tei"><teiHeader><fileDesc><titleStmt><title level="a">High substrate specificity and induction characteristics of trimethylamine- N -oxide reductase of Escherichia coli</title>
</titleStmt>
<publicationStmt><authority>ISTEX</authority>
<publisher>ELSEVIER</publisher>
<availability><p>ELSEVIER</p>
</availability>
<date>1996</date>
</publicationStmt>
<notesStmt><note type="content">Section title: Regular paper</note>
</notesStmt>
<sourceDesc><biblStruct type="inbook"><analytic><title level="a">High substrate specificity and induction characteristics of trimethylamine- N -oxide reductase of Escherichia coli</title>
<author xml:id="author-0000"><persName><forename type="first">Chantal</forename>
<surname>Iobbi-Nivol</surname>
</persName>
<affiliation>Laboratoire de Chimie Bactérienne, Institut Fédératif Biologie Structurale et Microbiologie (IFRC1), CNRS, 31, Chemin J. Aiguier, 13402 Marseille, France</affiliation>
</author>
<author xml:id="author-0001"><persName><forename type="first">Janine</forename>
<surname>Pommier</surname>
</persName>
<affiliation>Laboratoire de Chimie Bactérienne, Institut Fédératif Biologie Structurale et Microbiologie (IFRC1), CNRS, 31, Chemin J. Aiguier, 13402 Marseille, France</affiliation>
</author>
<author xml:id="author-0002"><persName><forename type="first">Joanne</forename>
<surname>Simala-Grant</surname>
</persName>
<affiliation>Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H, Canada</affiliation>
</author>
<author xml:id="author-0003"><persName><forename type="first">Vincent</forename>
<surname>Méjean</surname>
</persName>
<affiliation>Laboratoire de Chimie Bactérienne, Institut Fédératif Biologie Structurale et Microbiologie (IFRC1), CNRS, 31, Chemin J. Aiguier, 13402 Marseille, France</affiliation>
</author>
<author xml:id="author-0004"><persName><forename type="first">Gérard</forename>
<surname>Giordano</surname>
</persName>
<affiliation>Corresponding author. Fax: +33 91 718914.</affiliation>
<affiliation>Laboratoire de Chimie Bactérienne, Institut Fédératif Biologie Structurale et Microbiologie (IFRC1), CNRS, 31, Chemin J. Aiguier, 13402 Marseille, France</affiliation>
</author>
<idno type="istex">DA385A7331C8B4A076EAE6482CC0FDBDD32CCFCC</idno>
<idno type="DOI">10.1016/0167-4838(95)00271-5</idno>
<idno type="PII">0167-4838(95)00271-5</idno>
</analytic>
<monogr><title level="j">Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology</title>
<title level="j" type="abbrev">BBAPRO</title>
<idno type="pISSN">0167-4838</idno>
<idno type="PII">S0167-4838(00)X0003-9</idno>
<imprint><publisher>ELSEVIER</publisher>
<date type="published" when="1996"></date>
<biblScope unit="volume">1294</biblScope>
<biblScope unit="issue">1</biblScope>
<biblScope unit="page" from="77">77</biblScope>
<biblScope unit="page" to="82">82</biblScope>
</imprint>
</monogr>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><creation><date>1996</date>
</creation>
<langUsage><language ident="en">en</language>
</langUsage>
<abstract xml:lang="en"><p>Using a wide variety of N- and S-oxide compounds we have shown by kinetic analysis that only two N-oxidestrimethylamine-N-oxide and 4-methylmorpholine-N-oxide, can be considered good substrates for trimethylamine-N-oxide (TMAO) reductase on the basis of their kcat Km ratio. This result demonstrates that TMAO reductase possesses a high substrate specificity. Induction of the torCAD operon using the same S- and N-oxide compounds was also analyzed. We demonstrate that there is no correlation between the ability for a compound to be reduced by TMAO reductase and to induce TMAO reductase synthesis.</p>
</abstract>
<textClass><keywords scheme="keyword"><list><head>Keywords</head>
<item><term>Trimethylamine-N-oxide reductase</term>
</item>
<item><term>Reductase activity</term>
</item>
<item><term>Reductase induction</term>
</item>
<item><term>Molybdoenzyme</term>
</item>
<item><term>(E. coli)</term>
</item>
</list>
</keywords>
</textClass>
<textClass><keywords scheme="keyword"><list><head>Abbreviations</head>
<item><term>DMSO</term>
<term>dimethylsulfoxide</term>
</item>
<item><term>LDAO</term>
<term>N , N -dimethyldodecylamine- N -oxide</term>
</item>
<item><term>TMAO</term>
<term>trimethylamine- N -oxide</term>
</item>
<item><term>TMSO</term>
<term>tetramethylenesulfoxide</term>
</item>
</list>
</keywords>
</textClass>
</profileDesc>
<revisionDesc><change when="1996">Published</change>
</revisionDesc>
</teiHeader>
</istex:fulltextTEI>
<json:item><extension>txt</extension>
<original>false</original>
<mimetype>text/plain</mimetype>
<uri>https://api-v5.istex.fr/document/DA385A7331C8B4A076EAE6482CC0FDBDD32CCFCC/fulltext/txt</uri>
</json:item>
</fulltext>
<metadata><istex:metadataXml wicri:clean="Elsevier, elements deleted: tail"><istex:xmlDeclaration>version="1.0" encoding="utf-8"</istex:xmlDeclaration>
<istex:docType PUBLIC="-//ES//DTD journal article DTD version 4.5.2//EN//XML" URI="art452.dtd" name="istex:docType"></istex:docType>
<istex:document><converted-article version="4.5.2" docsubtype="fla"><item-info><jid>BBAPRO</jid>
<aid>95002715</aid>
<ce:pii>0167-4838(95)00271-5</ce:pii>
<ce:doi>10.1016/0167-4838(95)00271-5</ce:doi>
<ce:copyright type="unknown" year="1996"></ce:copyright>
</item-info>
<head><ce:dochead><ce:textfn>Regular paper</ce:textfn>
</ce:dochead>
<ce:title>High substrate specificity and induction characteristics of trimethylamine-<ce:italic>N</ce:italic>
-oxide reductase of <ce:italic>Escherichia coli</ce:italic>
</ce:title>
<ce:author-group><ce:author><ce:given-name>Chantal</ce:given-name>
<ce:surname>Iobbi-Nivol</ce:surname>
<ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup>
</ce:cross-ref>
</ce:author>
<ce:author><ce:given-name>Janine</ce:given-name>
<ce:surname>Pommier</ce:surname>
<ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup>
</ce:cross-ref>
</ce:author>
<ce:author><ce:given-name>Joanne</ce:given-name>
<ce:surname>Simala-Grant</ce:surname>
<ce:cross-ref refid="AFF2"><ce:sup>b</ce:sup>
</ce:cross-ref>
</ce:author>
<ce:author><ce:given-name>Vincent</ce:given-name>
<ce:surname>Méjean</ce:surname>
<ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup>
</ce:cross-ref>
</ce:author>
<ce:author><ce:given-name>Gérard</ce:given-name>
<ce:surname>Giordano</ce:surname>
<ce:cross-ref refid="COR1"><ce:sup>∗</ce:sup>
</ce:cross-ref>
<ce:cross-ref refid="AFF1"><ce:sup>a</ce:sup>
</ce:cross-ref>
</ce:author>
<ce:affiliation id="AFF1"><ce:label>a</ce:label>
<ce:textfn>Laboratoire de Chimie Bactérienne, Institut Fédératif Biologie Structurale et Microbiologie (IFRC1), CNRS, 31, Chemin J. Aiguier, 13402 Marseille, France</ce:textfn>
</ce:affiliation>
<ce:affiliation id="AFF2"><ce:label>b</ce:label>
<ce:textfn>Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H, Canada</ce:textfn>
</ce:affiliation>
<ce:correspondence id="COR1"><ce:label>∗</ce:label>
<ce:text>Corresponding author. Fax: +33 91 718914.</ce:text>
</ce:correspondence>
</ce:author-group>
<ce:date-received day="10" month="10" year="1995"></ce:date-received>
<ce:date-accepted day="20" month="12" year="1995"></ce:date-accepted>
<ce:abstract><ce:section-title>Abstract</ce:section-title>
<ce:abstract-sec><ce:simple-para>Using a wide variety of <ce:italic>N</ce:italic>
- and <ce:italic>S</ce:italic>
-oxide compounds we have shown by kinetic analysis that only two <ce:italic>N</ce:italic>
-oxidestrimethylamine-<ce:italic>N</ce:italic>
-oxide and 4-methylmorpholine-<ce:italic>N</ce:italic>
-oxide, can be considered good substrates for trimethylamine-<ce:italic>N</ce:italic>
-oxide (TMAO) reductase on the basis of their <math altimg="si1.gif"><fr shape="sol"><nu>k<inf><rm>cat</rm>
</inf>
</nu>
<de>K<inf><rm>m</rm>
</inf>
</de>
</fr>
</math>
ratio. This result demonstrates that TMAO reductase possesses a high substrate specificity. Induction of the <ce:italic>torCAD</ce:italic>
operon using the same <ce:italic>S</ce:italic>
- and <ce:italic>N</ce:italic>
-oxide compounds was also analyzed. We demonstrate that there is no correlation between the ability for a compound to be reduced by TMAO reductase and to induce TMAO reductase synthesis.</ce:simple-para>
</ce:abstract-sec>
</ce:abstract>
<ce:keywords><ce:section-title>Keywords</ce:section-title>
<ce:keyword><ce:text>Trimethylamine-<ce:italic>N</ce:italic>
-oxide reductase</ce:text>
</ce:keyword>
<ce:keyword><ce:text>Reductase activity</ce:text>
</ce:keyword>
<ce:keyword><ce:text>Reductase induction</ce:text>
</ce:keyword>
<ce:keyword><ce:text>Molybdoenzyme</ce:text>
</ce:keyword>
<ce:keyword><ce:text>(<ce:italic>E. coli</ce:italic>
)</ce:text>
</ce:keyword>
</ce:keywords>
<ce:keywords class="abr"><ce:section-title>Abbreviations</ce:section-title>
<ce:keyword><ce:text>DMSO</ce:text>
<ce:keyword><ce:text>dimethylsulfoxide</ce:text>
</ce:keyword>
</ce:keyword>
<ce:keyword><ce:text>LDAO</ce:text>
<ce:keyword><ce:text><ce:italic>N</ce:italic>
,<ce:italic>N</ce:italic>
-dimethyldodecylamine-<ce:italic>N</ce:italic>
-oxide</ce:text>
</ce:keyword>
</ce:keyword>
<ce:keyword><ce:text>TMAO</ce:text>
<ce:keyword><ce:text>trimethylamine-<ce:italic>N</ce:italic>
-oxide</ce:text>
</ce:keyword>
</ce:keyword>
<ce:keyword><ce:text>TMSO</ce:text>
<ce:keyword><ce:text>tetramethylenesulfoxide</ce:text>
</ce:keyword>
</ce:keyword>
</ce:keywords>
</head>
</converted-article>
</istex:document>
</istex:metadataXml>
<mods version="3.6"><titleInfo><title>High substrate specificity and induction characteristics of trimethylamine- N -oxide reductase of Escherichia coli</title>
</titleInfo>
<titleInfo type="alternative" contentType="CDATA"><title>High substrate specificity and induction characteristics of trimethylamine-</title>
</titleInfo>
<name type="personal"><namePart type="given">Chantal</namePart>
<namePart type="family">Iobbi-Nivol</namePart>
<affiliation>Laboratoire de Chimie Bactérienne, Institut Fédératif Biologie Structurale et Microbiologie (IFRC1), CNRS, 31, Chemin J. Aiguier, 13402 Marseille, France</affiliation>
<role><roleTerm type="text">author</roleTerm>
</role>
</name>
<name type="personal"><namePart type="given">Janine</namePart>
<namePart type="family">Pommier</namePart>
<affiliation>Laboratoire de Chimie Bactérienne, Institut Fédératif Biologie Structurale et Microbiologie (IFRC1), CNRS, 31, Chemin J. Aiguier, 13402 Marseille, France</affiliation>
<role><roleTerm type="text">author</roleTerm>
</role>
</name>
<name type="personal"><namePart type="given">Joanne</namePart>
<namePart type="family">Simala-Grant</namePart>
<affiliation>Department of Biochemistry, University of Alberta, Edmonton, Alberta T6G 2H, Canada</affiliation>
<role><roleTerm type="text">author</roleTerm>
</role>
</name>
<name type="personal"><namePart type="given">Vincent</namePart>
<namePart type="family">Méjean</namePart>
<affiliation>Laboratoire de Chimie Bactérienne, Institut Fédératif Biologie Structurale et Microbiologie (IFRC1), CNRS, 31, Chemin J. Aiguier, 13402 Marseille, France</affiliation>
<role><roleTerm type="text">author</roleTerm>
</role>
</name>
<name type="personal"><namePart type="given">Gérard</namePart>
<namePart type="family">Giordano</namePart>
<affiliation>Corresponding author. Fax: +33 91 718914.</affiliation>
<affiliation>Laboratoire de Chimie Bactérienne, Institut Fédératif Biologie Structurale et Microbiologie (IFRC1), CNRS, 31, Chemin J. Aiguier, 13402 Marseille, France</affiliation>
<role><roleTerm type="text">author</roleTerm>
</role>
</name>
<typeOfResource>text</typeOfResource>
<genre type="research-article" displayLabel="Full-length article"></genre>
<originInfo><publisher>ELSEVIER</publisher>
<dateIssued encoding="w3cdtf">1996</dateIssued>
<copyrightDate encoding="w3cdtf">1996</copyrightDate>
</originInfo>
<language><languageTerm type="code" authority="iso639-2b">eng</languageTerm>
<languageTerm type="code" authority="rfc3066">en</languageTerm>
</language>
<physicalDescription><internetMediaType>text/html</internetMediaType>
</physicalDescription>
<abstract lang="en">Using a wide variety of N- and S-oxide compounds we have shown by kinetic analysis that only two N-oxidestrimethylamine-N-oxide and 4-methylmorpholine-N-oxide, can be considered good substrates for trimethylamine-N-oxide (TMAO) reductase on the basis of their kcat Km ratio. This result demonstrates that TMAO reductase possesses a high substrate specificity. Induction of the torCAD operon using the same S- and N-oxide compounds was also analyzed. We demonstrate that there is no correlation between the ability for a compound to be reduced by TMAO reductase and to induce TMAO reductase synthesis.</abstract>
<note type="content">Section title: Regular paper</note>
<subject><genre>Keywords</genre>
<topic>Trimethylamine-N-oxide reductase</topic>
<topic>Reductase activity</topic>
<topic>Reductase induction</topic>
<topic>Molybdoenzyme</topic>
<topic>(E. coli)</topic>
</subject>
<subject><genre>Abbreviations</genre>
<topic>DMSO : dimethylsulfoxide</topic>
<topic>LDAO : N , N -dimethyldodecylamine- N -oxide</topic>
<topic>TMAO : trimethylamine- N -oxide</topic>
<topic>TMSO : tetramethylenesulfoxide</topic>
</subject>
<relatedItem type="host"><titleInfo><title>Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology</title>
</titleInfo>
<titleInfo type="abbreviated"><title>BBAPRO</title>
</titleInfo>
<genre type="journal">journal</genre>
<originInfo><dateIssued encoding="w3cdtf">19960502</dateIssued>
</originInfo>
<identifier type="ISSN">0167-4838</identifier>
<identifier type="PII">S0167-4838(00)X0003-9</identifier>
<part><date>19960502</date>
<detail type="volume"><number>1294</number>
<caption>vol.</caption>
</detail>
<detail type="issue"><number>1</number>
<caption>no.</caption>
</detail>
<extent unit="issue pages"><start>1</start>
<end>97</end>
</extent>
<extent unit="pages"><start>77</start>
<end>82</end>
</extent>
</part>
</relatedItem>
<identifier type="istex">DA385A7331C8B4A076EAE6482CC0FDBDD32CCFCC</identifier>
<identifier type="DOI">10.1016/0167-4838(95)00271-5</identifier>
<identifier type="PII">0167-4838(95)00271-5</identifier>
<recordInfo><recordContentSource>ELSEVIER</recordContentSource>
</recordInfo>
</mods>
</metadata>
<serie></serie>
</istex>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Canada/explor/ParkinsonCanadaV1/Data/Istex/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002894 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Istex/Corpus/biblio.hfd -nk 002894 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Wicri/Canada |area= ParkinsonCanadaV1 |flux= Istex |étape= Corpus |type= RBID |clé= ISTEX:DA385A7331C8B4A076EAE6482CC0FDBDD32CCFCC |texte= High substrate specificity and induction characteristics of trimethylamine- N -oxide reductase of Escherichia coli }}
![]() | This area was generated with Dilib version V0.6.29. | ![]() |