Molecular characterization of cytochrome P450 catalyzing hydroxylation of benzoates from the white-rot fungus Phanerochaete chrysosporium.
Identifieur interne : 000823 ( Main/Exploration ); précédent : 000822; suivant : 000824Molecular characterization of cytochrome P450 catalyzing hydroxylation of benzoates from the white-rot fungus Phanerochaete chrysosporium.
Auteurs : Fumiko Matsuzaki [Japon] ; Hiroyuki WariishiSource :
- Biochemical and biophysical research communications [ 0006-291X ] ; 2005.
Descripteurs français
- KwdFr :
- Acide benzoïque (composition chimique), Acide benzoïque (pharmacologie), Catalyse (MeSH), Cytochrome P-450 enzyme system (analyse), Cytochrome P-450 enzyme system (composition chimique), Cytochrome P-450 enzyme system (génétique), Cytochrome P-450 enzyme system (métabolisme), Données de séquences moléculaires (MeSH), Hydroxylation (MeSH), Phanerochaete (effets des médicaments et des substances chimiques), Phanerochaete (enzymologie), Similitude de séquences d'acides aminés (MeSH), Séquence d'acides aminés (MeSH).
- MESH :
- analyse : Cytochrome P-450 enzyme system.
- composition chimique : Acide benzoïque, Cytochrome P-450 enzyme system.
- effets des médicaments et des substances chimiques : Phanerochaete.
- enzymologie : Phanerochaete.
- génétique : Cytochrome P-450 enzyme system.
- métabolisme : Cytochrome P-450 enzyme system.
- pharmacologie : Acide benzoïque.
- Catalyse, Données de séquences moléculaires, Hydroxylation, Similitude de séquences d'acides aminés, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Benzoic Acid (chemistry), Benzoic Acid (pharmacology), Catalysis (MeSH), Cytochrome P-450 Enzyme System (analysis), Cytochrome P-450 Enzyme System (chemistry), Cytochrome P-450 Enzyme System (genetics), Cytochrome P-450 Enzyme System (metabolism), Hydroxylation (MeSH), Molecular Sequence Data (MeSH), Phanerochaete (drug effects), Phanerochaete (enzymology), Sequence Homology, Amino Acid (MeSH).
- MESH :
- chemical , analysis : Cytochrome P-450 Enzyme System.
- chemical , chemistry : Benzoic Acid, Cytochrome P-450 Enzyme System.
- chemical , genetics : Cytochrome P-450 Enzyme System.
- chemical , metabolism : Cytochrome P-450 Enzyme System.
- chemical , pharmacology : Benzoic Acid.
- drug effects : Phanerochaete.
- enzymology : Phanerochaete.
- Amino Acid Sequence, Catalysis, Hydroxylation, Molecular Sequence Data, Sequence Homology, Amino Acid.
Abstract
We cloned full-length cDNA (PcCYP1f) encoding one of the cytochrome P450s in the lignin-degrading basidiomycete Phanerochaete chrysosporium, which showed high homology to P450s in the CYP53 family. PcCYP1f was expressed as an active microsomal protein using the methylotrophic yeast Pichia pastoris expression system. Using the microsomal fraction containing PcCYP1f, a typical P450 CO-difference spectrum was obtained with absorption maximum at 448nm. Recombinant PcCYP1f catalyzed the hydroxylation of benzoic acid into 4-hydroxybenzoic acid in the presence of NADPH and P. chrysosporium cytochrome P450 oxidoreductase. In contrast to other CYP53 P450s, this enzyme was shown to catalyze the hydroxylation of 3-hydroxybenzoate into 3,4-dihydroxybenzoate. Furthermore, 2- and 3-methylbenzoate were also shown to be substrates of PcCYP1f. This is the first report showing the expression of a functionally active Phanerochaete P450. Finally, real-time quantitative PCR analysis revealed that PcCYP1f is induced at a transcriptional level by exogenous addition of benzoic acid.
DOI: 10.1016/j.bbrc.2005.07.013
PubMed: 16039998
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Wariishi</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2005">2005</date><idno type="RBID">pubmed:16039998</idno><idno type="pmid">16039998</idno><idno type="doi">10.1016/j.bbrc.2005.07.013</idno><idno type="wicri:Area/Main/Corpus">000831</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000831</idno><idno type="wicri:Area/Main/Curation">000831</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">000831</idno><idno type="wicri:Area/Main/Exploration">000831</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Molecular characterization of cytochrome P450 catalyzing hydroxylation of benzoates from the white-rot fungus Phanerochaete chrysosporium.</title><author><name sortKey="Matsuzaki, Fumiko" sort="Matsuzaki, Fumiko" uniqKey="Matsuzaki F" first="Fumiko" last="Matsuzaki">Fumiko Matsuzaki</name><affiliation wicri:level="4"><nlm:affiliation>Faculty of Agriculture, Kyushu University, Fukuoka 812-8581, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Faculty of Agriculture, Kyushu University, Fukuoka 812-8581</wicri:regionArea><orgName type="university">Université de Kyūshū</orgName><placeName><settlement type="city">Fukuoka</settlement><region type="province">Kyūshū</region><region type="prefecture">Préfecture de Fukuoka</region></placeName></affiliation></author><author><name sortKey="Wariishi, Hiroyuki" sort="Wariishi, Hiroyuki" uniqKey="Wariishi H" first="Hiroyuki" last="Wariishi">Hiroyuki Wariishi</name></author></analytic><series><title level="j">Biochemical and biophysical research communications</title><idno type="ISSN">0006-291X</idno><imprint><date when="2005" type="published">2005</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Benzoic Acid (chemistry)</term><term>Benzoic Acid (pharmacology)</term><term>Catalysis (MeSH)</term><term>Cytochrome P-450 Enzyme System (analysis)</term><term>Cytochrome P-450 Enzyme System (chemistry)</term><term>Cytochrome P-450 Enzyme System (genetics)</term><term>Cytochrome P-450 Enzyme System (metabolism)</term><term>Hydroxylation (MeSH)</term><term>Molecular Sequence Data (MeSH)</term><term>Phanerochaete (drug effects)</term><term>Phanerochaete (enzymology)</term><term>Sequence Homology, Amino Acid (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acide benzoïque (composition chimique)</term><term>Acide benzoïque (pharmacologie)</term><term>Catalyse (MeSH)</term><term>Cytochrome P-450 enzyme system (analyse)</term><term>Cytochrome P-450 enzyme system (composition chimique)</term><term>Cytochrome P-450 enzyme system (génétique)</term><term>Cytochrome P-450 enzyme system (métabolisme)</term><term>Données de séquences moléculaires (MeSH)</term><term>Hydroxylation (MeSH)</term><term>Phanerochaete (effets des médicaments et des substances chimiques)</term><term>Phanerochaete (enzymologie)</term><term>Similitude de séquences d'acides aminés (MeSH)</term><term>Séquence d'acides aminés (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Cytochrome P-450 Enzyme System</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Benzoic Acid</term><term>Cytochrome P-450 Enzyme System</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cytochrome P-450 Enzyme System</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cytochrome P-450 Enzyme System</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Benzoic Acid</term></keywords><keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Cytochrome P-450 enzyme system</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Acide benzoïque</term><term>Cytochrome P-450 enzyme system</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Phanerochaete</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Phanerochaete</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="génétique" xml:lang="fr"><term>Cytochrome P-450 enzyme system</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cytochrome P-450 enzyme system</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Acide benzoïque</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Catalysis</term><term>Hydroxylation</term><term>Molecular Sequence Data</term><term>Sequence Homology, Amino Acid</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Catalyse</term><term>Données de séquences moléculaires</term><term>Hydroxylation</term><term>Similitude de séquences d'acides aminés</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">We cloned full-length cDNA (PcCYP1f) encoding one of the cytochrome P450s in the lignin-degrading basidiomycete Phanerochaete chrysosporium, which showed high homology to P450s in the CYP53 family. PcCYP1f was expressed as an active microsomal protein using the methylotrophic yeast Pichia pastoris expression system. Using the microsomal fraction containing PcCYP1f, a typical P450 CO-difference spectrum was obtained with absorption maximum at 448nm. Recombinant PcCYP1f catalyzed the hydroxylation of benzoic acid into 4-hydroxybenzoic acid in the presence of NADPH and P. chrysosporium cytochrome P450 oxidoreductase. In contrast to other CYP53 P450s, this enzyme was shown to catalyze the hydroxylation of 3-hydroxybenzoate into 3,4-dihydroxybenzoate. Furthermore, 2- and 3-methylbenzoate were also shown to be substrates of PcCYP1f. This is the first report showing the expression of a functionally active Phanerochaete P450. Finally, real-time quantitative PCR analysis revealed that PcCYP1f is induced at a transcriptional level by exogenous addition of benzoic acid.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16039998</PMID><DateCompleted><Year>2005</Year><Month>09</Month><Day>26</Day></DateCompleted><DateRevised><Year>2015</Year><Month>11</Month><Day>19</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-291X</ISSN><JournalIssue CitedMedium="Print"><Volume>334</Volume><Issue>4</Issue><PubDate><Year>2005</Year><Month>Sep</Month><Day>09</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation></Journal><ArticleTitle>Molecular characterization of cytochrome P450 catalyzing hydroxylation of benzoates from the white-rot fungus Phanerochaete chrysosporium.</ArticleTitle><Pagination><MedlinePgn>1184-90</MedlinePgn></Pagination><Abstract><AbstractText>We cloned full-length cDNA (PcCYP1f) encoding one of the cytochrome P450s in the lignin-degrading basidiomycete Phanerochaete chrysosporium, which showed high homology to P450s in the CYP53 family. PcCYP1f was expressed as an active microsomal protein using the methylotrophic yeast Pichia pastoris expression system. Using the microsomal fraction containing PcCYP1f, a typical P450 CO-difference spectrum was obtained with absorption maximum at 448nm. Recombinant PcCYP1f catalyzed the hydroxylation of benzoic acid into 4-hydroxybenzoic acid in the presence of NADPH and P. chrysosporium cytochrome P450 oxidoreductase. In contrast to other CYP53 P450s, this enzyme was shown to catalyze the hydroxylation of 3-hydroxybenzoate into 3,4-dihydroxybenzoate. Furthermore, 2- and 3-methylbenzoate were also shown to be substrates of PcCYP1f. This is the first report showing the expression of a functionally active Phanerochaete P450. 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