Understanding electron transport systems of Streptomyces cytochrome P450
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Chun, Y. -J. | - |
dc.contributor.author | Shimada, T. | - |
dc.contributor.author | Waterman, M.R. | - |
dc.contributor.author | Guengerich, F.P. | - |
dc.date.accessioned | 2022-01-11T02:40:43Z | - |
dc.date.available | 2022-01-11T02:40:43Z | - |
dc.date.issued | 2006-12 | - |
dc.identifier.issn | 0300-5127 | - |
dc.identifier.issn | 1470-8752 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/53201 | - |
dc.description.abstract | Streptomyces spp. are known to produce various types of biologically active compounds including antibiotics, antiparasitic agents, herbicides and immunosuppressants. P450 (cytochrome P450) enzymes may have key roles in these biosynthetic and biotransformation reactions. Recent genomic analysis of Streptomyces coelicolor A3(2) indicates that S. coelicolor may have six ferredoxins (Fdxs), four putative Fdx reductases (FdRs) and 18 P450 genes. However, there are few clues to explain the mechanisms and functions of Streptomyces P450 systems. To solve these questions, we have expressed and purified five S. coelicolor P450s, four MRS and six Fdxs in Escherichia coli. of the purified P450s, CYP105D5 has fatty acid hydroxylation activity in a system reconstituted with putidaredoxin reductase and Fdx4 or with spinach FdR and spinach Fdx, although the reconstitutions with FdR2 or FdR3 and any of the Fdxs did not support CYP105DS-catalysed oleic acid hydroxylation. Elucidation of the detailed mechanisms of electron transport system for Streptomyces P450 may provide the perspective for usefulness of P450s as a biocatalyst. | - |
dc.format.extent | 3 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | PORTLAND PRESS LTD | - |
dc.title | Understanding electron transport systems of Streptomyces cytochrome P450 | - |
dc.type | Article | - |
dc.identifier.doi | 10.1042/BST0341183 | - |
dc.identifier.bibliographicCitation | BIOCHEMICAL SOCIETY TRANSACTIONS, v.34, no.6, pp 1183 - 1185 | - |
dc.description.isOpenAccess | N | - |
dc.identifier.wosid | 000243013500046 | - |
dc.identifier.scopusid | 2-s2.0-34248642001 | - |
dc.citation.endPage | 1185 | - |
dc.citation.number | 6 | - |
dc.citation.startPage | 1183 | - |
dc.citation.title | BIOCHEMICAL SOCIETY TRANSACTIONS | - |
dc.citation.volume | 34 | - |
dc.type.docType | Article; Proceedings Paper | - |
dc.publisher.location | 영국 | - |
dc.subject.keywordAuthor | cytochrome P450 | - |
dc.subject.keywordAuthor | electron transport | - |
dc.subject.keywordAuthor | Escherichia coli | - |
dc.subject.keywordAuthor | ferredoxin | - |
dc.subject.keywordAuthor | ferredoxin reductase | - |
dc.subject.keywordAuthor | Streptomyces coelicolor | - |
dc.subject.keywordPlus | COELICOLOR A3(2) | - |
dc.subject.keywordPlus | FERREDOXIN REDUCTASE | - |
dc.subject.keywordPlus | HYDROXYLATION | - |
dc.subject.keywordPlus | COMPLEMENT | - |
dc.subject.keywordPlus | EXPRESSION | - |
dc.subject.keywordPlus | PATHWAYS | - |
dc.subject.keywordPlus | SEQUENCE | - |
dc.subject.keywordPlus | CYP154C1 | - |
dc.subject.keywordPlus | GRISEUS | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.
84, Heukseok-ro, Dongjak-gu, Seoul, Republic of Korea (06974)02-820-6194
COPYRIGHT 2019 Chung-Ang University All Rights Reserved.
Certain data included herein are derived from the © Web of Science of Clarivate Analytics. All rights reserved.
You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.