{"@context":{"@vocab":"https://cir.nii.ac.jp/schema/1.0/","rdfs":"http://www.w3.org/2000/01/rdf-schema#","dc":"http://purl.org/dc/elements/1.1/","dcterms":"http://purl.org/dc/terms/","foaf":"http://xmlns.com/foaf/0.1/","prism":"http://prismstandard.org/namespaces/basic/2.0/","cinii":"http://ci.nii.ac.jp/ns/1.0/","datacite":"https://schema.datacite.org/meta/kernel-4/","ndl":"http://ndl.go.jp/dcndl/terms/","jpcoar":"https://github.com/JPCOAR/schema/blob/master/2.0/"},"@id":"https://cir.nii.ac.jp/crid/1363670318354094336.json","@type":"Article","productIdentifier":[{"identifier":{"@type":"DOI","@value":"10.1128/aac.06063-11"}},{"identifier":{"@type":"URI","@value":"https://journals.asm.org/doi/pdf/10.1128/AAC.06063-11"}},{"identifier":{"@type":"PMID","@value":"22547618"}}],"dc:title":[{"@value":"Function of Cytochrome P450 Enzymes MycCI and MycG in Micromonospora griseorubida, a Producer of the Macrolide Antibiotic Mycinamicin"}],"description":[{"type":"abstract","notation":[{"@value":"<jats:title>ABSTRACT</jats:title>\n          <jats:p>\n            The cytochrome P450 enzymes MycCI and MycG are encoded within the mycinamicin biosynthetic gene cluster and are involved in the biosynthesis of mycinamicin II (a 16-membered macrolide antibiotic produced by\n            <jats:named-content xmlns:xlink=\"http://www.w3.org/1999/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">Micromonospora griseorubida</jats:named-content>\n            ). Based on recent enzymatic studies, MycCI is characterized as the C-21 methyl hydroxylase of mycinamicin VIII, while MycG is designated multifunctional P450, which catalyzes hydroxylation and also epoxidation at C-14 and C-12/13 on the macrolactone ring of mycinamicin. Here, we confirm the functions of MycCI and MycG in\n            <jats:named-content xmlns:xlink=\"http://www.w3.org/1999/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">M. griseorubida</jats:named-content>\n            . Protomycinolide IV and mycinamicin VIII accumulated in the culture broth of the\n            <jats:italic>mycCI</jats:italic>\n            disruption mutant; moreover, the\n            <jats:italic>mycCI</jats:italic>\n            gene fragment complemented the production of mycinamicin I and mycinamicin II, which are produced as major mycinamicins by the wild strain\n            <jats:named-content xmlns:xlink=\"http://www.w3.org/1999/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">M. griseorubida</jats:named-content>\n            A11725. The\n            <jats:italic>mycG</jats:italic>\n            disruption mutant did not produce mycinamicin I and mycinamicin II; however, mycinamicin IV accumulated in the culture broth. The\n            <jats:italic>mycG</jats:italic>\n            gene was located immediately downstream of the self-resistance gene\n            <jats:italic>myrB</jats:italic>\n            . The\n            <jats:italic>mycG</jats:italic>\n            gene under the control of\n            <jats:italic>mycGp</jats:italic>\n            complemented the production of mycinamicin I and mycinamicin II. Furthermore, the amount of mycinamicin II produced by the strain complemented with the\n            <jats:italic>mycG</jats:italic>\n            gene under the control of\n            <jats:italic>myrBp</jats:italic>\n            was approximately 2-fold higher than that produced by the wild strain. In\n            <jats:named-content xmlns:xlink=\"http://www.w3.org/1999/xlink\" content-type=\"genus-species\" xlink:type=\"simple\">M. griseorubida</jats:named-content>\n            , MycG recognized mycinamicin IV, mycinamicin V, and also mycinamicin III as the substrates. Moreover, it catalyzed hydroxylation and also epoxidation at C-14 and C-12/13 on these intermediates. However, C-14 on mycinamicin I was not hydroxylated.\n          </jats:p>"}]}],"creator":[{"@id":"https://cir.nii.ac.jp/crid/1420564276160495872","@type":"Researcher","personIdentifier":[{"@type":"KAKEN_RESEARCHERS","@value":"20318299"},{"@type":"NRID","@value":"1000020318299"},{"@type":"NRID","@value":"9000006385549"},{"@type":"NRID","@value":"9000000719122"},{"@type":"NRID","@value":"9000003065022"},{"@type":"NRID","@value":"9000405895709"},{"@type":"NRID","@value":"9000253209860"},{"@type":"NRID","@value":"9000257986571"},{"@type":"NRID","@value":"9000005285032"},{"@type":"RESEARCHMAP","@value":"https://researchmap.jp/read0193495"}],"foaf:name":[{"@value":"Yojiro Anzai"}],"jpcoar:affiliationName":[{"@value":"Faculty of Pharmaceutical Sciences, Toho University, Funabashi, Chiba, Japan"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670318354094338","@type":"Researcher","foaf:name":[{"@value":"Shu-ichi Tsukada"}],"jpcoar:affiliationName":[{"@value":"Faculty of Pharmaceutical Sciences, Toho University, Funabashi, Chiba, Japan"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670318354094340","@type":"Researcher","foaf:name":[{"@value":"Ayami Sakai"}],"jpcoar:affiliationName":[{"@value":"Faculty of Pharmaceutical Sciences, Toho University, Funabashi, Chiba, Japan"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670318354094344","@type":"Researcher","foaf:name":[{"@value":"Ryohei Masuda"}],"jpcoar:affiliationName":[{"@value":"Faculty of Pharmaceutical Sciences, Toho University, Funabashi, Chiba, Japan"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670318354094339","@type":"Researcher","foaf:name":[{"@value":"Chie Harada"}],"jpcoar:affiliationName":[{"@value":"Faculty of Pharmaceutical Sciences, Toho University, Funabashi, Chiba, Japan"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670318354094336","@type":"Researcher","foaf:name":[{"@value":"Ayaka Domeki"}],"jpcoar:affiliationName":[{"@value":"Faculty of Pharmaceutical Sciences, Toho University, Funabashi, Chiba, Japan"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670318354094345","@type":"Researcher","foaf:name":[{"@value":"Shengying Li"}],"jpcoar:affiliationName":[{"@value":"Life Sciences Institute, Department of Medicinal Chemistry, Chemistry, and Microbiology and Immunology, University of Michigan, Ann Arbor, Michigan, USA"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670318354094337","@type":"Researcher","foaf:name":[{"@value":"Kenji Kinoshita"}],"jpcoar:affiliationName":[{"@value":"School of Pharmaceutical Sciences, Mukogawa Women's University, Nishinomiya, Hyogo, Japan"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670318354094341","@type":"Researcher","foaf:name":[{"@value":"David H. Sherman"}],"jpcoar:affiliationName":[{"@value":"Life Sciences Institute, Department of Medicinal Chemistry, Chemistry, and Microbiology and Immunology, University of Michigan, Ann Arbor, Michigan, USA"}]},{"@id":"https://cir.nii.ac.jp/crid/1383670318354094343","@type":"Researcher","foaf:name":[{"@value":"Fumio Kato"}],"jpcoar:affiliationName":[{"@value":"Faculty of Pharmaceutical Sciences, Toho University, Funabashi, Chiba, Japan"}]}],"publication":{"publicationIdentifier":[{"@type":"PISSN","@value":"00664804"},{"@type":"EISSN","@value":"10986596"}],"prism:publicationName":[{"@value":"Antimicrobial Agents and Chemotherapy"}],"dc:publisher":[{"@value":"American Society for Microbiology"}],"prism:publicationDate":"2012-07","prism:volume":"56","prism:number":"7","prism:startingPage":"3648","prism:endingPage":"3656"},"reviewed":"false","dcterms:accessRights":"http://purl.org/coar/access_right/c_abf2","dc:rights":["https://journals.asm.org/non-commercial-tdm-license"],"url":[{"@id":"https://journals.asm.org/doi/pdf/10.1128/AAC.06063-11"}],"createdAt":"2012-05-01","modifiedAt":"2022-02-21","foaf:topic":[{"@id":"https://cir.nii.ac.jp/all?q=Magnetic%20Resonance%20Spectroscopy","dc:title":"Magnetic Resonance Spectroscopy"},{"@id":"https://cir.nii.ac.jp/all?q=Bacterial%20Proteins","dc:title":"Bacterial Proteins"},{"@id":"https://cir.nii.ac.jp/all?q=Cytochrome%20P-450%20Enzyme%20System","dc:title":"Cytochrome P-450 Enzyme System"},{"@id":"https://cir.nii.ac.jp/all?q=Macrolides","dc:title":"Macrolides"},{"@id":"https://cir.nii.ac.jp/all?q=Micromonospora","dc:title":"Micromonospora"},{"@id":"https://cir.nii.ac.jp/all?q=Polymerase%20Chain%20Reaction","dc:title":"Polymerase Chain Reaction"},{"@id":"https://cir.nii.ac.jp/all?q=Signal%20Transduction","dc:title":"Signal Transduction"}],"relatedProduct":[{"@id":"https://cir.nii.ac.jp/crid/1050023461222098560","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@language":"en","@value":"Production of hybrid macrolide antibiotics by exploiting the specific substrate recognition characteristics of multifunctional cytochrome P450 enzyme MycG"}]},{"@id":"https://cir.nii.ac.jp/crid/1360290617724644992","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"An overview of the cytochrome P450 enzymes that catalyze the same-site multistep oxidation reactions in biotechnologically relevant selected actinomycete strains"}]},{"@id":"https://cir.nii.ac.jp/crid/1360294643777997184","@type":"Article","resourceType":"学術雑誌論文(journal article)","relationType":["isReferencedBy"],"jpcoar:relatedTitle":[{"@value":"Engineering sequence and selectivity of late-stage C-H oxidation in the MycG iterative cytochrome P450"}]}],"dataSourceIdentifier":[{"@type":"CROSSREF","@value":"10.1128/aac.06063-11"},{"@type":"OPENAIRE","@value":"doi_dedup___::a4aecab95bd34ed86e72afda0c5baeb4"},{"@type":"CROSSREF","@value":"10.1093/femsle/fnae080_references_DOI_QE6ZHFvk19SvRwPZOfHQBsUBvhk"},{"@type":"CROSSREF","@value":"10.1007/s00253-021-11216-y_references_DOI_QE6ZHFvk19SvRwPZOfHQBsUBvhk"},{"@type":"CROSSREF","@value":"10.1093/jimb/kuab069_references_DOI_QE6ZHFvk19SvRwPZOfHQBsUBvhk"}]}