Rational engineering of the fungal P450 monooxygenase CYP5136A3 to improve its oxidizing activity toward polycyclic aromatic hydrocarbons.
Identifieur interne : 000358 ( Main/Corpus ); précédent : 000357; suivant : 000359Rational engineering of the fungal P450 monooxygenase CYP5136A3 to improve its oxidizing activity toward polycyclic aromatic hydrocarbons.
Auteurs : Khajamohiddin Syed ; Aleksey Porollo ; David Miller ; Jagjit S. YadavSource :
- Protein engineering, design & selection : PEDS [ 1741-0134 ] ; 2013.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Amino Acid Substitution (MeSH), Animals (MeSH), Cytochrome P-450 Enzyme System (chemistry), Cytochrome P-450 Enzyme System (genetics), Fungal Proteins (chemistry), Fungal Proteins (genetics), Humans (MeSH), Kinetics (MeSH), Mixed Function Oxygenases (chemistry), Mixed Function Oxygenases (genetics), Molecular Sequence Data (MeSH), Mutagenesis, Site-Directed (MeSH), Oxidation-Reduction (MeSH), Phanerochaete (chemistry), Phanerochaete (enzymology), Phenanthrenes (chemistry), Pichia (genetics), Pichia (metabolism), Protein Engineering (MeSH), Pyrenes (chemistry), Rats (MeSH), Sequence Alignment (MeSH), Substrate Specificity (MeSH).
- MESH :
- chemical , chemistry : Cytochrome P-450 Enzyme System, Fungal Proteins, Mixed Function Oxygenases, Phenanthrenes, Pyrenes.
- chemical , genetics : Cytochrome P-450 Enzyme System, Fungal Proteins, Mixed Function Oxygenases.
- chemistry : Phanerochaete.
- enzymology : Phanerochaete.
- genetics : Pichia.
- metabolism : Pichia.
- Amino Acid Sequence, Amino Acid Substitution, Animals, Humans, Kinetics, Molecular Sequence Data, Mutagenesis, Site-Directed, Oxidation-Reduction, Protein Engineering, Rats, Sequence Alignment, Substrate Specificity.
Abstract
A promising polycyclic aromatic hydrocarbon-oxidizing P450 CYP5136A3 from Phanerochaete chrysosporium was rationally engineered to enhance its catalytic activity. The residues W129 and L324 found to be critical in substrate recognition were transformed by single (L324F) and double (W129L/L324G, W129L/L324F, W129A/L324G, W129F/L324G and W129F/L324F) mutations, and the engineered enzyme forms were expressed in Pichia pastoris. L324F and W129F/L324F mutations enhanced the oxidation activity toward pyrene and phenanthrene. L324F also altered the regio-selectivity favoring C position 4 over 9 for hydroxylation of phenanthrene. This is the first instance of engineering a eukaryotic P450 for enhanced oxidation of these fused-ring hydrocarbons.
DOI: 10.1093/protein/gzt036
PubMed: 23904501
PubMed Central: PMC3751181
Links to Exploration step
pubmed:23904501Le document en format XML
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Yadav</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2013">2013</date><idno type="RBID">pubmed:23904501</idno><idno type="pmid">23904501</idno><idno type="doi">10.1093/protein/gzt036</idno><idno type="pmc">PMC3751181</idno><idno type="wicri:Area/Main/Corpus">000358</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000358</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Rational engineering of the fungal P450 monooxygenase CYP5136A3 to improve its oxidizing activity toward polycyclic aromatic hydrocarbons.</title><author><name sortKey="Syed, Khajamohiddin" sort="Syed, Khajamohiddin" uniqKey="Syed K" first="Khajamohiddin" last="Syed">Khajamohiddin Syed</name><affiliation><nlm:affiliation>Department of Environmental Health, University of Cincinnati College of Medicine, Cincinnati, OH 45267-0056, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Porollo, Aleksey" sort="Porollo, Aleksey" uniqKey="Porollo A" first="Aleksey" last="Porollo">Aleksey Porollo</name></author><author><name sortKey="Miller, David" sort="Miller, David" uniqKey="Miller D" first="David" last="Miller">David Miller</name></author><author><name sortKey="Yadav, Jagjit S" sort="Yadav, Jagjit S" uniqKey="Yadav J" first="Jagjit S" last="Yadav">Jagjit S. Yadav</name></author></analytic><series><title level="j">Protein engineering, design & selection : PEDS</title><idno type="eISSN">1741-0134</idno><imprint><date when="2013" type="published">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Amino Acid Substitution (MeSH)</term><term>Animals (MeSH)</term><term>Cytochrome P-450 Enzyme System (chemistry)</term><term>Cytochrome P-450 Enzyme System (genetics)</term><term>Fungal Proteins (chemistry)</term><term>Fungal Proteins (genetics)</term><term>Humans (MeSH)</term><term>Kinetics (MeSH)</term><term>Mixed Function Oxygenases (chemistry)</term><term>Mixed Function Oxygenases (genetics)</term><term>Molecular Sequence Data (MeSH)</term><term>Mutagenesis, Site-Directed (MeSH)</term><term>Oxidation-Reduction (MeSH)</term><term>Phanerochaete (chemistry)</term><term>Phanerochaete (enzymology)</term><term>Phenanthrenes (chemistry)</term><term>Pichia (genetics)</term><term>Pichia (metabolism)</term><term>Protein Engineering (MeSH)</term><term>Pyrenes (chemistry)</term><term>Rats (MeSH)</term><term>Sequence Alignment (MeSH)</term><term>Substrate Specificity (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cytochrome P-450 Enzyme System</term><term>Fungal Proteins</term><term>Mixed Function Oxygenases</term><term>Phenanthrenes</term><term>Pyrenes</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cytochrome P-450 Enzyme System</term><term>Fungal Proteins</term><term>Mixed Function Oxygenases</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><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>Pichia</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Pichia</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Amino Acid Substitution</term><term>Animals</term><term>Humans</term><term>Kinetics</term><term>Molecular Sequence Data</term><term>Mutagenesis, Site-Directed</term><term>Oxidation-Reduction</term><term>Protein Engineering</term><term>Rats</term><term>Sequence Alignment</term><term>Substrate Specificity</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">A promising polycyclic aromatic hydrocarbon-oxidizing P450 CYP5136A3 from Phanerochaete chrysosporium was rationally engineered to enhance its catalytic activity. The residues W129 and L324 found to be critical in substrate recognition were transformed by single (L324F) and double (W129L/L324G, W129L/L324F, W129A/L324G, W129F/L324G and W129F/L324F) mutations, and the engineered enzyme forms were expressed in Pichia pastoris. L324F and W129F/L324F mutations enhanced the oxidation activity toward pyrene and phenanthrene. L324F also altered the regio-selectivity favoring C position 4 over 9 for hydroxylation of phenanthrene. This is the first instance of engineering a eukaryotic P450 for enhanced oxidation of these fused-ring hydrocarbons. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">23904501</PMID><DateCompleted><Year>2014</Year><Month>03</Month><Day>03</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1741-0134</ISSN><JournalIssue CitedMedium="Internet"><Volume>26</Volume><Issue>9</Issue><PubDate><Year>2013</Year><Month>Sep</Month></PubDate></JournalIssue><Title>Protein engineering, design & selection : PEDS</Title><ISOAbbreviation>Protein Eng Des Sel</ISOAbbreviation></Journal><ArticleTitle>Rational engineering of the fungal P450 monooxygenase CYP5136A3 to improve its oxidizing activity toward polycyclic aromatic hydrocarbons.</ArticleTitle><Pagination><MedlinePgn>553-7</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1093/protein/gzt036</ELocationID><Abstract><AbstractText>A promising polycyclic aromatic hydrocarbon-oxidizing P450 CYP5136A3 from Phanerochaete chrysosporium was rationally engineered to enhance its catalytic activity. The residues W129 and L324 found to be critical in substrate recognition were transformed by single (L324F) and double (W129L/L324G, W129L/L324F, W129A/L324G, W129F/L324G and W129F/L324F) mutations, and the engineered enzyme forms were expressed in Pichia pastoris. L324F and W129F/L324F mutations enhanced the oxidation activity toward pyrene and phenanthrene. L324F also altered the regio-selectivity favoring C position 4 over 9 for hydroxylation of phenanthrene. This is the first instance of engineering a eukaryotic P450 for enhanced oxidation of these fused-ring hydrocarbons. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Syed</LastName><ForeName>Khajamohiddin</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Environmental Health, University of Cincinnati College of Medicine, Cincinnati, OH 45267-0056, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Porollo</LastName><ForeName>Aleksey</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Miller</LastName><ForeName>David</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Yadav</LastName><ForeName>Jagjit S</ForeName><Initials>JS</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 ES010210</GrantID><Acronym>ES</Acronym><Agency>NIEHS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01ES015543</GrantID><Acronym>ES</Acronym><Agency>NIEHS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>P30 ES006096</GrantID><Acronym>ES</Acronym><Agency>NIEHS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>P30-ES006096</GrantID><Acronym>ES</Acronym><Agency>NIEHS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01 ES015543</GrantID><Acronym>ES</Acronym><Agency>NIEHS NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>R01ES10210</GrantID><Acronym>ES</Acronym><Agency>NIEHS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2013</Year><Month>07</Month><Day>31</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Protein Eng Des Sel</MedlineTA><NlmUniqueID>101186484</NlmUniqueID><ISSNLinking>1741-0126</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D005656">Fungal Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010616">Phenanthrenes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011721">Pyrenes</NameOfSubstance></Chemical><Chemical><RegistryNumber>448J8E5BST</RegistryNumber><NameOfSubstance UI="C031181">phenanthrene</NameOfSubstance></Chemical><Chemical><RegistryNumber>9035-51-2</RegistryNumber><NameOfSubstance UI="D003577">Cytochrome P-450 Enzyme System</NameOfSubstance></Chemical><Chemical><RegistryNumber>9E0T7WFW93</RegistryNumber><NameOfSubstance 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PubStatus="medline"><Year>2014</Year><Month>3</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">23904501</ArticleId><ArticleId IdType="pii">gzt036</ArticleId><ArticleId IdType="doi">10.1093/protein/gzt036</ArticleId><ArticleId IdType="pmc">PMC3751181</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>Expert Opin Drug Metab Toxicol. 2010 Feb;6(2):115-31</Citation><ArticleIdList><ArticleId IdType="pubmed">20064075</ArticleId></ArticleIdList></Reference><Reference><Citation>SAR QSAR Environ Res. 2012 Jan;23(1-2):87-109</Citation><ArticleIdList><ArticleId IdType="pubmed">22150106</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Protoc. 2009;4(3):363-71</Citation><ArticleIdList><ArticleId IdType="pubmed">19247286</ArticleId></ArticleIdList></Reference><Reference><Citation>Anal Bioanal Chem. 2008 Nov;392(6):1059-73</Citation><ArticleIdList><ArticleId IdType="pubmed">18622752</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem Biophys Res Commun. 2010 Sep 3;399(4):492-7</Citation><ArticleIdList><ArticleId IdType="pubmed">20674550</ArticleId></ArticleIdList></Reference><Reference><Citation>Trends Biotechnol. 2012 Jan;30(1):26-36</Citation><ArticleIdList><ArticleId IdType="pubmed">21782265</ArticleId></ArticleIdList></Reference><Reference><Citation>J Hazard Mater. 2009 Sep 30;169(1-3):1-15</Citation><ArticleIdList><ArticleId IdType="pubmed">19442441</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Recognit. 1996 Jan-Feb;9(1):1-5</Citation><ArticleIdList><ArticleId IdType="pubmed">8723313</ArticleId></ArticleIdList></Reference><Reference><Citation>Eur J Biochem. 2001 May;268(10):3117-25</Citation><ArticleIdList><ArticleId IdType="pubmed">11358532</ArticleId></ArticleIdList></Reference><Reference><Citation>PLoS One. 2011;6(12):e28286</Citation><ArticleIdList><ArticleId IdType="pubmed">22164262</ArticleId></ArticleIdList></Reference><Reference><Citation>Genome Res. 2004 Jun;14(6):1188-90</Citation><ArticleIdList><ArticleId IdType="pubmed">15173120</ArticleId></ArticleIdList></Reference><Reference><Citation>Drug Discov Today. 2004 Jun 15;9(12):530-7</Citation><ArticleIdList><ArticleId IdType="pubmed">15183161</ArticleId></ArticleIdList></Reference><Reference><Citation>Crit Rev Microbiol. 2012 Nov;38(4):339-63</Citation><ArticleIdList><ArticleId IdType="pubmed">22624627</ArticleId></ArticleIdList></Reference><Reference><Citation>Appl Biochem Biotechnol. 1995 Jul-Sep;54(1-3):291-302</Citation><ArticleIdList><ArticleId IdType="pubmed">7486983</ArticleId></ArticleIdList></Reference><Reference><Citation>Electrophoresis. 1997 Dec;18(15):2714-23</Citation><ArticleIdList><ArticleId IdType="pubmed">9504803</ArticleId></ArticleIdList></Reference><Reference><Citation>Drug Metab Pharmacokinet. 2006 Aug;21(4):257-76</Citation><ArticleIdList><ArticleId IdType="pubmed">16946553</ArticleId></ArticleIdList></Reference><Reference><Citation>Arch Biochem Biophys. 1999 Sep 1;369(1):24-9</Citation><ArticleIdList><ArticleId IdType="pubmed">10462437</ArticleId></ArticleIdList></Reference><Reference><Citation>Curr Opin Biotechnol. 2011 Dec;22(6):809-17</Citation><ArticleIdList><ArticleId IdType="pubmed">21411308</ArticleId></ArticleIdList></Reference><Reference><Citation>J Pet Environ Biotechnol. 2012;3(5):null</Citation><ArticleIdList><ArticleId IdType="pubmed">25298920</ArticleId></ArticleIdList></Reference><Reference><Citation>Bioinformatics. 2007 Nov 1;23(21):2947-8</Citation><ArticleIdList><ArticleId IdType="pubmed">17846036</ArticleId></ArticleIdList></Reference><Reference><Citation>Protein Eng. 2000 Feb;13(2):121-8</Citation><ArticleIdList><ArticleId IdType="pubmed">10708651</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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