No Cover Image

Journal article 811 views

Cyclization of a Cellular Dipentaenone by Streptomyces coelicolor Cytochrome P450 154A1 without Oxidation/Reduction

Q Cheng, DC Lamb, Steven Kelly Orcid Logo, L Lei, FP Guenguerich, Diane Kelly

Journal of the American Chemical Society, Volume: 132, Issue: 43, Pages: 15173 - 15175

Swansea University Authors: Steven Kelly Orcid Logo, Diane Kelly

Full text not available from this repository: check for access using links below.

Check full text

DOI (Published version): 10.1021/ja107801v

Abstract

We report a comprehensive genetic, metabolomic, and biochemical study on the catalytic properties of Streptomyces coelicolor cytochrome P450 (P450) 154A1, known to have a unique heme orientation in its crystal structure. Deletion of the P450 154A1 gene compromised the long-term stability of the bact...

Full description

Published in: Journal of the American Chemical Society
ISSN: 0002-7863 1520-5126
Published: 1155 16TH ST, NW, WASHINGTON, DC 20036 USA AMER CHEMICAL SOC 2010
Online Access: Check full text

URI: https://cronfa.swan.ac.uk/Record/cronfa9901
Tags: Add Tag
No Tags, Be the first to tag this record!
first_indexed 2013-07-23T12:02:23Z
last_indexed 2021-10-30T02:21:16Z
id cronfa9901
recordtype SURis
fullrecord <?xml version="1.0"?><rfc1807><datestamp>2021-10-29T09:34:32.9620785</datestamp><bib-version>v2</bib-version><id>9901</id><entry>2012-03-21</entry><title>Cyclization of a Cellular Dipentaenone by Streptomyces coelicolor Cytochrome P450 154A1 without Oxidation/Reduction</title><swanseaauthors><author><sid>b17cebaf09b4d737b9378a3581e3de93</sid><ORCID>0000-0001-7991-5040</ORCID><firstname>Steven</firstname><surname>Kelly</surname><name>Steven Kelly</name><active>true</active><ethesisStudent>false</ethesisStudent></author><author><sid>5ccf81e5d5beedf32ef8d7c3d7ac6c8c</sid><firstname>Diane</firstname><surname>Kelly</surname><name>Diane Kelly</name><active>true</active><ethesisStudent>false</ethesisStudent></author></swanseaauthors><date>2012-03-21</date><deptcode>BMS</deptcode><abstract>We report a comprehensive genetic, metabolomic, and biochemical study on the catalytic properties of Streptomyces coelicolor cytochrome P450 (P450) 154A1, known to have a unique heme orientation in its crystal structure. Deletion of the P450 154A1 gene compromised the long-term stability of the bacterial spores. A novel dipentaenone (1) with a high degree of conjugation was identified as an endogenous substrate of P450 154A1 using a metabolomics approach. The biotransformation of 1 by P450 154A1 was shown to be an unexpected intramolecular cyclization to a Paterno-Buchi-like product, without oxidation/reduction</abstract><type>Journal Article</type><journal>Journal of the American Chemical Society</journal><volume>132</volume><journalNumber>43</journalNumber><paginationStart>15173</paginationStart><paginationEnd>15175</paginationEnd><publisher>AMER CHEMICAL SOC</publisher><placeOfPublication>1155 16TH ST, NW, WASHINGTON, DC 20036 USA</placeOfPublication><isbnPrint/><isbnElectronic/><issnPrint>0002-7863</issnPrint><issnElectronic>1520-5126</issnElectronic><keywords>DRUG DISCOVERY; A3(2); IDENTIFICATION; MODEL</keywords><publishedDay>30</publishedDay><publishedMonth>11</publishedMonth><publishedYear>2010</publishedYear><publishedDate>2010-11-30</publishedDate><doi>10.1021/ja107801v</doi><url/><notes/><college>COLLEGE NANME</college><department>Biomedical Sciences</department><CollegeCode>COLLEGE CODE</CollegeCode><DepartmentCode>BMS</DepartmentCode><institution>Swansea University</institution><apcterm/><lastEdited>2021-10-29T09:34:32.9620785</lastEdited><Created>2012-03-21T16:17:30.0000000</Created><path><level id="1">Faculty of Medicine, Health and Life Sciences</level><level id="2">Swansea University Medical School - Medicine</level></path><authors><author><firstname>Q</firstname><surname>Cheng</surname><order>1</order></author><author><firstname>DC</firstname><surname>Lamb</surname><order>2</order></author><author><firstname>Steven</firstname><surname>Kelly</surname><orcid>0000-0001-7991-5040</orcid><order>3</order></author><author><firstname>L</firstname><surname>Lei</surname><order>4</order></author><author><firstname>FP</firstname><surname>Guenguerich</surname><order>5</order></author><author><firstname>Diane</firstname><surname>Kelly</surname><order>6</order></author></authors><documents/><OutputDurs/></rfc1807>
spelling 2021-10-29T09:34:32.9620785 v2 9901 2012-03-21 Cyclization of a Cellular Dipentaenone by Streptomyces coelicolor Cytochrome P450 154A1 without Oxidation/Reduction b17cebaf09b4d737b9378a3581e3de93 0000-0001-7991-5040 Steven Kelly Steven Kelly true false 5ccf81e5d5beedf32ef8d7c3d7ac6c8c Diane Kelly Diane Kelly true false 2012-03-21 BMS We report a comprehensive genetic, metabolomic, and biochemical study on the catalytic properties of Streptomyces coelicolor cytochrome P450 (P450) 154A1, known to have a unique heme orientation in its crystal structure. Deletion of the P450 154A1 gene compromised the long-term stability of the bacterial spores. A novel dipentaenone (1) with a high degree of conjugation was identified as an endogenous substrate of P450 154A1 using a metabolomics approach. The biotransformation of 1 by P450 154A1 was shown to be an unexpected intramolecular cyclization to a Paterno-Buchi-like product, without oxidation/reduction Journal Article Journal of the American Chemical Society 132 43 15173 15175 AMER CHEMICAL SOC 1155 16TH ST, NW, WASHINGTON, DC 20036 USA 0002-7863 1520-5126 DRUG DISCOVERY; A3(2); IDENTIFICATION; MODEL 30 11 2010 2010-11-30 10.1021/ja107801v COLLEGE NANME Biomedical Sciences COLLEGE CODE BMS Swansea University 2021-10-29T09:34:32.9620785 2012-03-21T16:17:30.0000000 Faculty of Medicine, Health and Life Sciences Swansea University Medical School - Medicine Q Cheng 1 DC Lamb 2 Steven Kelly 0000-0001-7991-5040 3 L Lei 4 FP Guenguerich 5 Diane Kelly 6
title Cyclization of a Cellular Dipentaenone by Streptomyces coelicolor Cytochrome P450 154A1 without Oxidation/Reduction
spellingShingle Cyclization of a Cellular Dipentaenone by Streptomyces coelicolor Cytochrome P450 154A1 without Oxidation/Reduction
Steven Kelly
Diane Kelly
title_short Cyclization of a Cellular Dipentaenone by Streptomyces coelicolor Cytochrome P450 154A1 without Oxidation/Reduction
title_full Cyclization of a Cellular Dipentaenone by Streptomyces coelicolor Cytochrome P450 154A1 without Oxidation/Reduction
title_fullStr Cyclization of a Cellular Dipentaenone by Streptomyces coelicolor Cytochrome P450 154A1 without Oxidation/Reduction
title_full_unstemmed Cyclization of a Cellular Dipentaenone by Streptomyces coelicolor Cytochrome P450 154A1 without Oxidation/Reduction
title_sort Cyclization of a Cellular Dipentaenone by Streptomyces coelicolor Cytochrome P450 154A1 without Oxidation/Reduction
author_id_str_mv b17cebaf09b4d737b9378a3581e3de93
5ccf81e5d5beedf32ef8d7c3d7ac6c8c
author_id_fullname_str_mv b17cebaf09b4d737b9378a3581e3de93_***_Steven Kelly
5ccf81e5d5beedf32ef8d7c3d7ac6c8c_***_Diane Kelly
author Steven Kelly
Diane Kelly
author2 Q Cheng
DC Lamb
Steven Kelly
L Lei
FP Guenguerich
Diane Kelly
format Journal article
container_title Journal of the American Chemical Society
container_volume 132
container_issue 43
container_start_page 15173
publishDate 2010
institution Swansea University
issn 0002-7863
1520-5126
doi_str_mv 10.1021/ja107801v
publisher AMER CHEMICAL SOC
college_str Faculty of Medicine, Health and Life Sciences
hierarchytype
hierarchy_top_id facultyofmedicinehealthandlifesciences
hierarchy_top_title Faculty of Medicine, Health and Life Sciences
hierarchy_parent_id facultyofmedicinehealthandlifesciences
hierarchy_parent_title Faculty of Medicine, Health and Life Sciences
department_str Swansea University Medical School - Medicine{{{_:::_}}}Faculty of Medicine, Health and Life Sciences{{{_:::_}}}Swansea University Medical School - Medicine
document_store_str 0
active_str 0
description We report a comprehensive genetic, metabolomic, and biochemical study on the catalytic properties of Streptomyces coelicolor cytochrome P450 (P450) 154A1, known to have a unique heme orientation in its crystal structure. Deletion of the P450 154A1 gene compromised the long-term stability of the bacterial spores. A novel dipentaenone (1) with a high degree of conjugation was identified as an endogenous substrate of P450 154A1 using a metabolomics approach. The biotransformation of 1 by P450 154A1 was shown to be an unexpected intramolecular cyclization to a Paterno-Buchi-like product, without oxidation/reduction
published_date 2010-11-30T03:15:30Z
_version_ 1756506284878725120
score 10.926911