Phanerochaete chrysosporium NADPH-cytochrome P450 reductase kinetic mechanism.
Identifieur interne : 000982 ( Main/Exploration ); précédent : 000981; suivant : 000983Phanerochaete chrysosporium NADPH-cytochrome P450 reductase kinetic mechanism.
Auteurs : Andrew G S. Warrilow [Royaume-Uni] ; David C. Lamb ; Diane E. Kelly ; Steven L. KellySource :
- Biochemical and biophysical research communications [ 0006-291X ] ; 2002.
Descripteurs français
- KwdFr :
- Cinétique (MeSH), Cytochromes de type c (métabolisme), Escherichia coli (génétique), NADP (métabolisme), NADPH-ferrihemoprotéine reductase (génétique), NADPH-ferrihemoprotéine reductase (isolement et purification), NADPH-ferrihemoprotéine reductase (métabolisme), Phanerochaete (enzymologie), Transport d'électrons (MeSH).
- MESH :
- enzymologie : Phanerochaete.
- génétique : Escherichia coli, NADPH-ferrihemoprotéine reductase.
- isolement et purification : NADPH-ferrihemoprotéine reductase.
- métabolisme : Cytochromes de type c, NADP, NADPH-ferrihemoprotéine reductase.
- Cinétique, Transport d'électrons.
English descriptors
- KwdEn :
- Cytochrome c Group (metabolism), Electron Transport (MeSH), Escherichia coli (genetics), Kinetics (MeSH), NADP (metabolism), NADPH-Ferrihemoprotein Reductase (genetics), NADPH-Ferrihemoprotein Reductase (isolation & purification), NADPH-Ferrihemoprotein Reductase (metabolism), Phanerochaete (enzymology).
- MESH :
- chemical , genetics : NADPH-Ferrihemoprotein Reductase.
- chemical , isolation & purification : NADPH-Ferrihemoprotein Reductase.
- chemical , metabolism : Cytochrome c Group, NADP, NADPH-Ferrihemoprotein Reductase.
- enzymology : Phanerochaete.
- genetics : Escherichia coli.
- Electron Transport, Kinetics.
Abstract
The recently completed genome of the basidiomycete, Phanerochaete chrysosporium, revealed the presence of one NADPH-cytochrome P450 oxidoreductase (CPR; EC 1.6.2.4) gene and >123 cytochrome P450 (CYP) genes. How a single CPR can drive many CYPs is an important area of study. We have investigated this CPR to gain insight into the mechanistic and structural biodiversity of the cytochrome P450 catalytic system. Native CPR and a NH(2)-terminally truncated derivative lacking 23 amino acids have been overexpressed in Escherichia coli and purified to electrophoretic homogeneity. Steady-state kinetics of cytochrome c reductase activity revealed a random sequential bireactant kinetic mechanism in which both products form dead-end complexes reflecting differences in CPR kinetic mechanisms even within a single kingdom of life. Removal of the N-terminal anchor of P. chrysosporium CPR did not alter the kinetic properties displayed by the enzyme in vitro, indicating it was a useful modification for structural studies.
DOI: 10.1016/s0006-291x(02)02600-1
PubMed: 12437968
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Lamb</name></author><author><name sortKey="Kelly, Diane E" sort="Kelly, Diane E" uniqKey="Kelly D" first="Diane E" last="Kelly">Diane E. Kelly</name></author><author><name sortKey="Kelly, Steven L" sort="Kelly, Steven L" uniqKey="Kelly S" first="Steven L" last="Kelly">Steven L. Kelly</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2002">2002</date><idno type="RBID">pubmed:12437968</idno><idno type="pmid">12437968</idno><idno type="doi">10.1016/s0006-291x(02)02600-1</idno><idno type="wicri:Area/Main/Corpus">000978</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000978</idno><idno type="wicri:Area/Main/Curation">000978</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000978</idno><idno type="wicri:Area/Main/Exploration">000978</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Phanerochaete chrysosporium NADPH-cytochrome P450 reductase kinetic mechanism.</title><author><name sortKey="Warrilow, Andrew G S" sort="Warrilow, Andrew G S" uniqKey="Warrilow A" first="Andrew G S" last="Warrilow">Andrew G S. Warrilow</name><affiliation wicri:level="1"><nlm:affiliation>Wolfson Laboratory of P450 Biodiversity, Institute of Biological Sciences, The University of Wales Aberystwyth, SY23 3DA, Aberystwyth, UK.</nlm:affiliation><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Wolfson Laboratory of P450 Biodiversity, Institute of Biological Sciences, The University of Wales Aberystwyth, SY23 3DA, Aberystwyth</wicri:regionArea><wicri:noRegion>Aberystwyth</wicri:noRegion></affiliation></author><author><name sortKey="Lamb, David C" sort="Lamb, David C" uniqKey="Lamb D" first="David C" last="Lamb">David C. Lamb</name></author><author><name sortKey="Kelly, Diane E" sort="Kelly, Diane E" uniqKey="Kelly D" first="Diane E" last="Kelly">Diane E. Kelly</name></author><author><name sortKey="Kelly, Steven L" sort="Kelly, Steven L" uniqKey="Kelly S" first="Steven L" last="Kelly">Steven L. Kelly</name></author></analytic><series><title level="j">Biochemical and biophysical research communications</title><idno type="ISSN">0006-291X</idno><imprint><date when="2002" type="published">2002</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cytochrome c Group (metabolism)</term><term>Electron Transport (MeSH)</term><term>Escherichia coli (genetics)</term><term>Kinetics (MeSH)</term><term>NADP (metabolism)</term><term>NADPH-Ferrihemoprotein Reductase (genetics)</term><term>NADPH-Ferrihemoprotein Reductase (isolation & purification)</term><term>NADPH-Ferrihemoprotein Reductase (metabolism)</term><term>Phanerochaete (enzymology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cinétique (MeSH)</term><term>Cytochromes de type c (métabolisme)</term><term>Escherichia coli (génétique)</term><term>NADP (métabolisme)</term><term>NADPH-ferrihemoprotéine reductase (génétique)</term><term>NADPH-ferrihemoprotéine reductase (isolement et purification)</term><term>NADPH-ferrihemoprotéine reductase (métabolisme)</term><term>Phanerochaete (enzymologie)</term><term>Transport d'électrons (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>NADPH-Ferrihemoprotein Reductase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>NADPH-Ferrihemoprotein Reductase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cytochrome c Group</term><term>NADP</term><term>NADPH-Ferrihemoprotein Reductase</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Escherichia coli</term><term>NADPH-ferrihemoprotéine reductase</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>NADPH-ferrihemoprotéine reductase</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cytochromes de type c</term><term>NADP</term><term>NADPH-ferrihemoprotéine reductase</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Electron Transport</term><term>Kinetics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cinétique</term><term>Transport d'électrons</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The recently completed genome of the basidiomycete, Phanerochaete chrysosporium, revealed the presence of one NADPH-cytochrome P450 oxidoreductase (CPR; EC 1.6.2.4) gene and >123 cytochrome P450 (CYP) genes. How a single CPR can drive many CYPs is an important area of study. We have investigated this CPR to gain insight into the mechanistic and structural biodiversity of the cytochrome P450 catalytic system. Native CPR and a NH(2)-terminally truncated derivative lacking 23 amino acids have been overexpressed in Escherichia coli and purified to electrophoretic homogeneity. Steady-state kinetics of cytochrome c reductase activity revealed a random sequential bireactant kinetic mechanism in which both products form dead-end complexes reflecting differences in CPR kinetic mechanisms even within a single kingdom of life. Removal of the N-terminal anchor of P. chrysosporium CPR did not alter the kinetic properties displayed by the enzyme in vitro, indicating it was a useful modification for structural studies.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12437968</PMID><DateCompleted><Year>2003</Year><Month>01</Month><Day>09</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>12</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-291X</ISSN><JournalIssue CitedMedium="Print"><Volume>299</Volume><Issue>2</Issue><PubDate><Year>2002</Year><Month>Nov</Month><Day>29</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation></Journal><ArticleTitle>Phanerochaete chrysosporium NADPH-cytochrome P450 reductase kinetic mechanism.</ArticleTitle><Pagination><MedlinePgn>189-95</MedlinePgn></Pagination><Abstract><AbstractText>The recently completed genome of the basidiomycete, Phanerochaete chrysosporium, revealed the presence of one NADPH-cytochrome P450 oxidoreductase (CPR; EC 1.6.2.4) gene and >123 cytochrome P450 (CYP) genes. How a single CPR can drive many CYPs is an important area of study. We have investigated this CPR to gain insight into the mechanistic and structural biodiversity of the cytochrome P450 catalytic system. Native CPR and a NH(2)-terminally truncated derivative lacking 23 amino acids have been overexpressed in Escherichia coli and purified to electrophoretic homogeneity. Steady-state kinetics of cytochrome c reductase activity revealed a random sequential bireactant kinetic mechanism in which both products form dead-end complexes reflecting differences in CPR kinetic mechanisms even within a single kingdom of life. Removal of the N-terminal anchor of P. chrysosporium CPR did not alter the kinetic properties displayed by the enzyme in vitro, indicating it was a useful modification for structural studies.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Warrilow</LastName><ForeName>Andrew G S</ForeName><Initials>AG</Initials><AffiliationInfo><Affiliation>Wolfson Laboratory of P450 Biodiversity, Institute of Biological Sciences, The University of Wales Aberystwyth, SY23 3DA, Aberystwyth, UK.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lamb</LastName><ForeName>David C</ForeName><Initials>DC</Initials></Author><Author ValidYN="Y"><LastName>Kelly</LastName><ForeName>Diane E</ForeName><Initials>DE</Initials></Author><Author ValidYN="Y"><LastName>Kelly</LastName><ForeName>Steven L</ForeName><Initials>SL</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochem Biophys Res Commun</MedlineTA><NlmUniqueID>0372516</NlmUniqueID><ISSNLinking>0006-291X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D003574">Cytochrome c Group</NameOfSubstance></Chemical><Chemical><RegistryNumber>53-59-8</RegistryNumber><NameOfSubstance UI="D009249">NADP</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.6.2.4</RegistryNumber><NameOfSubstance UI="D009251">NADPH-Ferrihemoprotein Reductase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D003574" MajorTopicYN="N">Cytochrome c Group</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004579" MajorTopicYN="N">Electron Transport</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004926" MajorTopicYN="N">Escherichia coli</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009249" MajorTopicYN="N">NADP</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009251" MajorTopicYN="N">NADPH-Ferrihemoprotein Reductase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="N">isolation & purification</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020075" MajorTopicYN="N">Phanerochaete</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2002</Year><Month>11</Month><Day>20</Day><Hour>4</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2003</Year><Month>1</Month><Day>10</Day><Hour>4</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2002</Year><Month>11</Month><Day>20</Day><Hour>4</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">12437968</ArticleId><ArticleId IdType="pii">S0006291X02026001</ArticleId><ArticleId IdType="doi">10.1016/s0006-291x(02)02600-1</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Royaume-Uni</li></country></list><tree><noCountry><name sortKey="Kelly, Diane E" sort="Kelly, Diane E" uniqKey="Kelly D" first="Diane E" last="Kelly">Diane E. Kelly</name><name sortKey="Kelly, Steven L" sort="Kelly, Steven L" uniqKey="Kelly S" first="Steven L" last="Kelly">Steven L. Kelly</name><name sortKey="Lamb, David C" sort="Lamb, David C" uniqKey="Lamb D" first="David C" last="Lamb">David C. Lamb</name></noCountry><country name="Royaume-Uni"><noRegion><name sortKey="Warrilow, Andrew G S" sort="Warrilow, Andrew G S" uniqKey="Warrilow A" first="Andrew G S" last="Warrilow">Andrew G S. Warrilow</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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