The Role of Cytochrome P-450sca in Streptomyces

Azole compounds inhibited both hydroxylation catalyzed by cytochrome P-450sca and the growth of Streptomyces carbophilus. The growth inhibition could be overcome by inducing cytochrome P-450sca production in the cells. These results suggest that cytochrome P-450sca has an intrinsic substrate as well...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Bioscience, biotechnology, and biochemistry biotechnology, and biochemistry, 1993-10, Vol.57 (10), p.1777
Hauptverfasser: Serizawa, Nobufusa, Matsuoka, Tatsuji
Format: Artikel
Sprache:eng
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page
container_issue 10
container_start_page 1777
container_title Bioscience, biotechnology, and biochemistry
container_volume 57
creator Serizawa, Nobufusa
Matsuoka, Tatsuji
description Azole compounds inhibited both hydroxylation catalyzed by cytochrome P-450sca and the growth of Streptomyces carbophilus. The growth inhibition could be overcome by inducing cytochrome P-450sca production in the cells. These results suggest that cytochrome P-450sca has an intrinsic substrate as well as xenobiotics. Such a P-450 that has both substrates seems to be unique among the prokaryotic P-450 enzymes.
format Article
fullrecord <record><control><sourceid>proquest</sourceid><recordid>TN_cdi_proquest_journals_1449395951</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>3121590571</sourcerecordid><originalsourceid>FETCH-proquest_journals_14493959513</originalsourceid><addsrcrecordid>eNpjYuA0NDYx1zWzNDFnYeA0sDQ007UwMTXkYOAqLs4yMAAKmBpyMuiHZKQqBOXnpCrkpyk4V5bkJ2cU5eemKgTompgaFCcnKmTmKQSXFKUWlOTnVianFvMwsKYl5hSn8kJpbgZlN9cQZw_dgqL8wtLU4pL4rPzSojygVLyhiYmlsaWppamhMXGqAInPMv4</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1449395951</pqid></control><display><type>article</type><title>The Role of Cytochrome P-450sca in Streptomyces</title><source>J-STAGE (Japan Science &amp; Technology Information Aggregator, Electronic) Freely Available Titles - Japanese</source><source>Open Access Titles of Japan</source><source>EZB-FREE-00999 freely available EZB journals</source><source>Free Full-Text Journals in Chemistry</source><creator>Serizawa, Nobufusa ; Matsuoka, Tatsuji</creator><creatorcontrib>Serizawa, Nobufusa ; Matsuoka, Tatsuji</creatorcontrib><description>Azole compounds inhibited both hydroxylation catalyzed by cytochrome P-450sca and the growth of Streptomyces carbophilus. The growth inhibition could be overcome by inducing cytochrome P-450sca production in the cells. These results suggest that cytochrome P-450sca has an intrinsic substrate as well as xenobiotics. Such a P-450 that has both substrates seems to be unique among the prokaryotic P-450 enzymes.</description><identifier>ISSN: 0916-8451</identifier><identifier>EISSN: 1347-6947</identifier><language>eng</language><publisher>Tokyo: Oxford University Press</publisher><ispartof>Bioscience, biotechnology, and biochemistry, 1993-10, Vol.57 (10), p.1777</ispartof><rights>Copyright Japan Science and Technology Agency 1993</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780</link.rule.ids></links><search><creatorcontrib>Serizawa, Nobufusa</creatorcontrib><creatorcontrib>Matsuoka, Tatsuji</creatorcontrib><title>The Role of Cytochrome P-450sca in Streptomyces</title><title>Bioscience, biotechnology, and biochemistry</title><description>Azole compounds inhibited both hydroxylation catalyzed by cytochrome P-450sca and the growth of Streptomyces carbophilus. The growth inhibition could be overcome by inducing cytochrome P-450sca production in the cells. These results suggest that cytochrome P-450sca has an intrinsic substrate as well as xenobiotics. Such a P-450 that has both substrates seems to be unique among the prokaryotic P-450 enzymes.</description><issn>0916-8451</issn><issn>1347-6947</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid/><recordid>eNpjYuA0NDYx1zWzNDFnYeA0sDQ007UwMTXkYOAqLs4yMAAKmBpyMuiHZKQqBOXnpCrkpyk4V5bkJ2cU5eemKgTompgaFCcnKmTmKQSXFKUWlOTnVianFvMwsKYl5hSn8kJpbgZlN9cQZw_dgqL8wtLU4pL4rPzSojygVLyhiYmlsaWppamhMXGqAInPMv4</recordid><startdate>19931001</startdate><enddate>19931001</enddate><creator>Serizawa, Nobufusa</creator><creator>Matsuoka, Tatsuji</creator><general>Oxford University Press</general><scope/></search><sort><creationdate>19931001</creationdate><title>The Role of Cytochrome P-450sca in Streptomyces</title><author>Serizawa, Nobufusa ; Matsuoka, Tatsuji</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-proquest_journals_14493959513</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Serizawa, Nobufusa</creatorcontrib><creatorcontrib>Matsuoka, Tatsuji</creatorcontrib><jtitle>Bioscience, biotechnology, and biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Serizawa, Nobufusa</au><au>Matsuoka, Tatsuji</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The Role of Cytochrome P-450sca in Streptomyces</atitle><jtitle>Bioscience, biotechnology, and biochemistry</jtitle><date>1993-10-01</date><risdate>1993</risdate><volume>57</volume><issue>10</issue><spage>1777</spage><pages>1777-</pages><issn>0916-8451</issn><eissn>1347-6947</eissn><abstract>Azole compounds inhibited both hydroxylation catalyzed by cytochrome P-450sca and the growth of Streptomyces carbophilus. The growth inhibition could be overcome by inducing cytochrome P-450sca production in the cells. These results suggest that cytochrome P-450sca has an intrinsic substrate as well as xenobiotics. Such a P-450 that has both substrates seems to be unique among the prokaryotic P-450 enzymes.</abstract><cop>Tokyo</cop><pub>Oxford University Press</pub></addata></record>
fulltext fulltext
identifier ISSN: 0916-8451
ispartof Bioscience, biotechnology, and biochemistry, 1993-10, Vol.57 (10), p.1777
issn 0916-8451
1347-6947
language eng
recordid cdi_proquest_journals_1449395951
source J-STAGE (Japan Science & Technology Information Aggregator, Electronic) Freely Available Titles - Japanese; Open Access Titles of Japan; EZB-FREE-00999 freely available EZB journals; Free Full-Text Journals in Chemistry
title The Role of Cytochrome P-450sca in Streptomyces
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-08T10%3A19%3A08IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20Role%20of%20Cytochrome%20P-450sca%20in%20Streptomyces&rft.jtitle=Bioscience,%20biotechnology,%20and%20biochemistry&rft.au=Serizawa,%20Nobufusa&rft.date=1993-10-01&rft.volume=57&rft.issue=10&rft.spage=1777&rft.pages=1777-&rft.issn=0916-8451&rft.eissn=1347-6947&rft_id=info:doi/&rft_dat=%3Cproquest%3E3121590571%3C/proquest%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1449395951&rft_id=info:pmid/&rfr_iscdi=true