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. |  |