Improved NADPH Regeneration for Fungal Cytochrome P450 Monooxygenase by Co-Expressing Bacterial Glucose Dehydrogenase in Resting-Cell Biotransformation of Recombinant Yeast.
Identifieur interne : 000F55 ( Main/Exploration ); précédent : 000F54; suivant : 000F56Improved NADPH Regeneration for Fungal Cytochrome P450 Monooxygenase by Co-Expressing Bacterial Glucose Dehydrogenase in Resting-Cell Biotransformation of Recombinant Yeast.
Auteurs : Hyunwoo Jeon [Corée du Sud] ; Pradeepraj Durairaj [Corée du Sud] ; Dowoo Lee [Corée du Sud] ; Md Murshidul Ahsan [Corée du Sud] ; Hyungdon Yun [Corée du Sud]Source :
- Journal of microbiology and biotechnology [ 1738-8872 ] ; 2016.
Descripteurs français
- KwdFr :
- Bacillus subtilis (enzymologie), Bacillus subtilis (génétique), Biotransformation (MeSH), Cytochrome P-450 enzyme system (génétique), Cytochrome P-450 enzyme system (métabolisme), Expression des gènes (MeSH), Fusarium (enzymologie), Fusarium (génétique), Glucose 1-dehydrogenase (génétique), Glucose 1-dehydrogenase (métabolisme), Génie métabolique (MeSH), Mixed function oxygenases (génétique), Mixed function oxygenases (métabolisme), NADP (métabolisme), Protéines bactériennes (génétique), Protéines bactériennes (métabolisme), Protéines fongiques (génétique), Protéines fongiques (métabolisme), Saccharomyces cerevisiae (croissance et développement), Saccharomyces cerevisiae (génétique), Saccharomyces cerevisiae (métabolisme).
- MESH :
- croissance et développement : Saccharomyces cerevisiae.
- enzymologie : Bacillus subtilis, Fusarium.
- génétique : Bacillus subtilis, Cytochrome P-450 enzyme system, Fusarium, Glucose 1-dehydrogenase, Mixed function oxygenases, Protéines bactériennes, Protéines fongiques, Saccharomyces cerevisiae.
- métabolisme : Cytochrome P-450 enzyme system, Glucose 1-dehydrogenase, Mixed function oxygenases, NADP, Protéines bactériennes, Protéines fongiques, Saccharomyces cerevisiae.
- Biotransformation, Expression des gènes, Génie métabolique.
English descriptors
- KwdEn :
- Bacillus subtilis (enzymology), Bacillus subtilis (genetics), Bacterial Proteins (genetics), Bacterial Proteins (metabolism), Biotransformation (MeSH), Cytochrome P-450 Enzyme System (genetics), Cytochrome P-450 Enzyme System (metabolism), Fungal Proteins (genetics), Fungal Proteins (metabolism), Fusarium (enzymology), Fusarium (genetics), Gene Expression (MeSH), Glucose 1-Dehydrogenase (genetics), Glucose 1-Dehydrogenase (metabolism), Metabolic Engineering (MeSH), Mixed Function Oxygenases (genetics), Mixed Function Oxygenases (metabolism), NADP (metabolism), Saccharomyces cerevisiae (genetics), Saccharomyces cerevisiae (growth & development), Saccharomyces cerevisiae (metabolism).
- MESH :
- chemical , genetics : Bacterial Proteins, Cytochrome P-450 Enzyme System, Fungal Proteins, Glucose 1-Dehydrogenase, Mixed Function Oxygenases.
- enzymology : Bacillus subtilis, Fusarium.
- genetics : Bacillus subtilis, Fusarium, Saccharomyces cerevisiae.
- growth & development : Saccharomyces cerevisiae.
- chemical , metabolism : Bacterial Proteins, Cytochrome P-450 Enzyme System, Fungal Proteins, Glucose 1-Dehydrogenase, Mixed Function Oxygenases, NADP, Saccharomyces cerevisiae.
- Biotransformation, Gene Expression, Metabolic Engineering.
Abstract
Fungal cytochrome P450 (CYP) enzymes catalyze versatile monooxygenase reactions and play a major role in fungal adaptations owing to their essential roles in the production avoid metabolites critical for pathogenesis, detoxification of xenobiotics, and exploitation avoid substrates. Although fungal CYP-dependent biotransformation for the selective oxidation avoid organic compounds in yeast system is advantageous, it often suffers from a shortage avoid intracellular NADPH. In this study, we aimed to investigate the use of bacterial glucose dehydrogenase (GDH) for the intracellular electron regeneration of fungal CYP monooxygenase in a yeast reconstituted system. The benzoate hydroxylase FoCYP53A19 and its homologous redox partner FoCPR from Fusarium oxysporum were co-expressed with the BsGDH from Bacillus subtilis in Saccharomyces cerevisiae for heterologous expression and biotransformations. We attempted to optimize several bottlenecks concerning the efficiency of fungal CYP-mediated whole-cell-biotransformation to enhance the conversion. The catalytic performance of the intracellular NADPH regeneration system facilitated the hydroxylation of benzoic acid to 4-hydroxybenzoic acid with high conversion in the resting-cell reaction. The FoCYP53A19+FoCPR+BsGDH reconstituted system produced 0.47 mM 4-hydroxybenzoic acid (94% conversion) in the resting-cell biotransformations performed in 50 mM phosphate buffer (pH 6.0) containing 0.5 mM benzoic acid and 0.25% glucose for 24 h at 30°C. The "coupled-enzyme" system can certainly improve the overall performance of NADPH-dependent whole-cell biotransformations in a yeast system.
DOI: 10.4014/jmb.1605.05090
PubMed: 27666994
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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(genetics)</term><term>Cytochrome P-450 Enzyme System (metabolism)</term><term>Fungal Proteins (genetics)</term><term>Fungal Proteins (metabolism)</term><term>Fusarium (enzymology)</term><term>Fusarium (genetics)</term><term>Gene Expression (MeSH)</term><term>Glucose 1-Dehydrogenase (genetics)</term><term>Glucose 1-Dehydrogenase (metabolism)</term><term>Metabolic Engineering (MeSH)</term><term>Mixed Function Oxygenases (genetics)</term><term>Mixed Function Oxygenases (metabolism)</term><term>NADP (metabolism)</term><term>Saccharomyces cerevisiae (genetics)</term><term>Saccharomyces cerevisiae (growth & development)</term><term>Saccharomyces cerevisiae (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Bacillus subtilis (enzymologie)</term><term>Bacillus subtilis (génétique)</term><term>Biotransformation (MeSH)</term><term>Cytochrome P-450 enzyme system (génétique)</term><term>Cytochrome P-450 enzyme system (métabolisme)</term><term>Expression des gènes (MeSH)</term><term>Fusarium (enzymologie)</term><term>Fusarium (génétique)</term><term>Glucose 1-dehydrogenase (génétique)</term><term>Glucose 1-dehydrogenase (métabolisme)</term><term>Génie métabolique (MeSH)</term><term>Mixed function oxygenases (génétique)</term><term>Mixed function oxygenases (métabolisme)</term><term>NADP (métabolisme)</term><term>Protéines bactériennes (génétique)</term><term>Protéines bactériennes (métabolisme)</term><term>Protéines fongiques (génétique)</term><term>Protéines fongiques (métabolisme)</term><term>Saccharomyces cerevisiae (croissance et développement)</term><term>Saccharomyces cerevisiae (génétique)</term><term>Saccharomyces cerevisiae (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Bacterial Proteins</term><term>Cytochrome P-450 Enzyme System</term><term>Fungal Proteins</term><term>Glucose 1-Dehydrogenase</term><term>Mixed Function Oxygenases</term></keywords><keywords scheme="MESH" qualifier="croissance et développement" xml:lang="fr"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Bacillus subtilis</term><term>Fusarium</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Bacillus subtilis</term><term>Fusarium</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Bacillus subtilis</term><term>Fusarium</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="growth & development" xml:lang="en"><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Bacillus subtilis</term><term>Cytochrome P-450 enzyme system</term><term>Fusarium</term><term>Glucose 1-dehydrogenase</term><term>Mixed function oxygenases</term><term>Protéines bactériennes</term><term>Protéines fongiques</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Bacterial Proteins</term><term>Cytochrome P-450 Enzyme System</term><term>Fungal Proteins</term><term>Glucose 1-Dehydrogenase</term><term>Mixed Function Oxygenases</term><term>NADP</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cytochrome P-450 enzyme system</term><term>Glucose 1-dehydrogenase</term><term>Mixed function oxygenases</term><term>NADP</term><term>Protéines bactériennes</term><term>Protéines fongiques</term><term>Saccharomyces cerevisiae</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biotransformation</term><term>Gene Expression</term><term>Metabolic Engineering</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Biotransformation</term><term>Expression des gènes</term><term>Génie métabolique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Fungal cytochrome P450 (CYP) enzymes catalyze versatile monooxygenase reactions and play a major role in fungal adaptations owing to their essential roles in the production avoid metabolites critical for pathogenesis, detoxification of xenobiotics, and exploitation avoid substrates. Although fungal CYP-dependent biotransformation for the selective oxidation avoid organic compounds in yeast system is advantageous, it often suffers from a shortage avoid intracellular NADPH. In this study, we aimed to investigate the use of bacterial glucose dehydrogenase (GDH) for the intracellular electron regeneration of fungal CYP monooxygenase in a yeast reconstituted system. The benzoate hydroxylase <i>FoCYP53A19</i> and its homologous redox partner FoCPR from <i>Fusarium oxysporum</i> were co-expressed with the BsGDH from <i>Bacillus subtilis</i> in <i>Saccharomyces cerevisiae</i> for heterologous expression and biotransformations. We attempted to optimize several bottlenecks concerning the efficiency of fungal CYP-mediated whole-cell-biotransformation to enhance the conversion. The catalytic performance of the intracellular NADPH regeneration system facilitated the hydroxylation of benzoic acid to 4-hydroxybenzoic acid with high conversion in the resting-cell reaction. The <i>FoCYP53A19</i>+FoCPR+BsGDH reconstituted system produced 0.47 mM 4-hydroxybenzoic acid (94% conversion) in the resting-cell biotransformations performed in 50 mM phosphate buffer (pH 6.0) containing 0.5 mM benzoic acid and 0.25% glucose for 24 h at 30°C. The "coupled-enzyme" system can certainly improve the overall performance of NADPH-dependent whole-cell biotransformations in a yeast system.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">27666994</PMID><DateCompleted><Year>2017</Year><Month>03</Month><Day>22</Day></DateCompleted><DateRevised><Year>2017</Year><Month>03</Month><Day>22</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1738-8872</ISSN><JournalIssue CitedMedium="Internet"><Volume>26</Volume><Issue>12</Issue><PubDate><Year>2016</Year><Month>Dec</Month><Day>28</Day></PubDate></JournalIssue><Title>Journal of microbiology and biotechnology</Title><ISOAbbreviation>J Microbiol Biotechnol</ISOAbbreviation></Journal><ArticleTitle>Improved NADPH Regeneration for Fungal Cytochrome P450 Monooxygenase by Co-Expressing Bacterial Glucose Dehydrogenase in Resting-Cell Biotransformation of Recombinant Yeast.</ArticleTitle><Pagination><MedlinePgn>2076-2086</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.4014/jmb.1605.05090</ELocationID><Abstract><AbstractText>Fungal cytochrome P450 (CYP) enzymes catalyze versatile monooxygenase reactions and play a major role in fungal adaptations owing to their essential roles in the production avoid metabolites critical for pathogenesis, detoxification of xenobiotics, and exploitation avoid substrates. Although fungal CYP-dependent biotransformation for the selective oxidation avoid organic compounds in yeast system is advantageous, it often suffers from a shortage avoid intracellular NADPH. In this study, we aimed to investigate the use of bacterial glucose dehydrogenase (GDH) for the intracellular electron regeneration of fungal CYP monooxygenase in a yeast reconstituted system. The benzoate hydroxylase <i>FoCYP53A19</i> and its homologous redox partner FoCPR from <i>Fusarium oxysporum</i> were co-expressed with the BsGDH from <i>Bacillus subtilis</i> in <i>Saccharomyces cerevisiae</i> for heterologous expression and biotransformations. We attempted to optimize several bottlenecks concerning the efficiency of fungal CYP-mediated whole-cell-biotransformation to enhance the conversion. The catalytic performance of the intracellular NADPH regeneration system facilitated the hydroxylation of benzoic acid to 4-hydroxybenzoic acid with high conversion in the resting-cell reaction. The <i>FoCYP53A19</i>+FoCPR+BsGDH reconstituted system produced 0.47 mM 4-hydroxybenzoic acid (94% conversion) in the resting-cell biotransformations performed in 50 mM phosphate buffer (pH 6.0) containing 0.5 mM benzoic acid and 0.25% glucose for 24 h at 30°C. The "coupled-enzyme" system can certainly improve the overall performance of NADPH-dependent whole-cell biotransformations in a yeast system.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Jeon</LastName><ForeName>Hyunwoo</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Department of Bioscience and Biotechnology, Konkuk University, Seoul 05029, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Durairaj</LastName><ForeName>Pradeepraj</ForeName><Initials>P</Initials><AffiliationInfo><Affiliation>Korean Lichen Research Institute, Sunchon National University, Suncheon 57922, Republic of Korea.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>School of Biotechnology, Yeungnam University, Gyeongsan 38541, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lee</LastName><ForeName>Dowoo</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Department of Bioscience and Biotechnology, Konkuk University, Seoul 05029, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ahsan</LastName><ForeName>Md Murshidul</ForeName><Initials>MM</Initials><AffiliationInfo><Affiliation>School of Biotechnology, Yeungnam University, Gyeongsan 38541, Republic of Korea.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Yun</LastName><ForeName>Hyungdon</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>Department of Bioscience and Biotechnology, Konkuk University, Seoul 05029, Republic of Korea.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Korea (South)</Country><MedlineTA>J Microbiol Biotechnol</MedlineTA><NlmUniqueID>9431852</NlmUniqueID><ISSNLinking>1017-7825</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001426">Bacterial Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>53-59-8</RegistryNumber><NameOfSubstance UI="D009249">NADP</NameOfSubstance></Chemical><Chemical><RegistryNumber>9035-51-2</RegistryNumber><NameOfSubstance UI="D003577">Cytochrome P-450 Enzyme System</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D006899">Mixed Function Oxygenases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.1.1.47</RegistryNumber><NameOfSubstance UI="D042843">Glucose 1-Dehydrogenase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D001412" MajorTopicYN="N">Bacillus subtilis</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001426" MajorTopicYN="N">Bacterial Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001711" MajorTopicYN="N">Biotransformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003577" MajorTopicYN="N">Cytochrome P-450 Enzyme System</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005656" MajorTopicYN="N">Fungal Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005670" MajorTopicYN="N">Fusarium</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015870" MajorTopicYN="N">Gene Expression</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D042843" MajorTopicYN="N">Glucose 1-Dehydrogenase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D060847" MajorTopicYN="N">Metabolic Engineering</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006899" MajorTopicYN="N">Mixed Function Oxygenases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D009249" MajorTopicYN="N">NADP</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012441" MajorTopicYN="N">Saccharomyces cerevisiae</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000254" MajorTopicYN="N">growth & development</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Cytochrome P450</Keyword><Keyword MajorTopicYN="Y">Saccharomyces cerevisiae</Keyword><Keyword MajorTopicYN="Y">benzoate hydroxylase</Keyword><Keyword MajorTopicYN="Y">biotransformation</Keyword><Keyword MajorTopicYN="Y">glucose dehydrogenase</Keyword><Keyword MajorTopicYN="Y">heterologous expression</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2016</Year><Month>9</Month><Day>27</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2017</Year><Month>3</Month><Day>23</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2016</Year><Month>9</Month><Day>27</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">27666994</ArticleId><ArticleId IdType="pii">10.4014/jmb.1605.05090</ArticleId><ArticleId IdType="doi">10.4014/jmb.1605.05090</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Corée du Sud</li></country><region><li>Région capitale de Séoul</li></region><settlement><li>Séoul</li></settlement></list><tree><country name="Corée du Sud"><region name="Région capitale de Séoul"><name sortKey="Jeon, Hyunwoo" sort="Jeon, Hyunwoo" uniqKey="Jeon H" first="Hyunwoo" last="Jeon">Hyunwoo Jeon</name></region><name sortKey="Ahsan, Md Murshidul" sort="Ahsan, Md Murshidul" uniqKey="Ahsan M" first="Md Murshidul" last="Ahsan">Md Murshidul Ahsan</name><name sortKey="Durairaj, Pradeepraj" sort="Durairaj, Pradeepraj" uniqKey="Durairaj P" first="Pradeepraj" last="Durairaj">Pradeepraj Durairaj</name><name sortKey="Durairaj, Pradeepraj" sort="Durairaj, Pradeepraj" uniqKey="Durairaj P" first="Pradeepraj" last="Durairaj">Pradeepraj Durairaj</name><name sortKey="Lee, Dowoo" sort="Lee, Dowoo" uniqKey="Lee D" first="Dowoo" last="Lee">Dowoo Lee</name><name sortKey="Yun, Hyungdon" sort="Yun, Hyungdon" uniqKey="Yun H" first="Hyungdon" last="Yun">Hyungdon Yun</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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