Bacterial CYP153A monooxygenases for the synthesis of omega-hydroxylated fatty acidsElectronic supplementary information (ESI) available: Materials and methods. Detailed substrate conversions and product distributions. Gas chromatograms and mass spectra. Michaelis-Menten plots. See DOI: 10.1039/c2cc18103g

Bacterial CYP153A monooxygenases for the synthesis of omega-hydroxylated fatty acidsElectronic supplementary information (ESI) available: Materials and methods. Detailed substrate conversions and product distributions. Gas chromatograms and mass spectra. Michaelis-Menten plots. See DOI: 10.1039/c2cc18103g

CYP153A from Marinobacter aquaeolei has been identified as a fatty acid ω-hydroxylase with a broad substrate range. Two hotspots predicted to influence substrate specificity and selectivity were exchanged. Mutant G307A is 2- to 20-fold more active towards fatty acids than the wild-type. Residue L354...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Hauptverfasser: Honda Malca, Sumire, Scheps, Daniel, Kühnel, Lisa, Venegas-Venegas, Elena, Seifert, Alexander, Nestl, Bettina M, Hauer, Bernhard
Format: Artikel
Sprache:eng
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 5117
container_issue 42
container_start_page 5115
container_title
container_volume 48
creator Honda Malca, Sumire
Scheps, Daniel
Kühnel, Lisa
Venegas-Venegas, Elena
Seifert, Alexander
Nestl, Bettina M
Hauer, Bernhard
description CYP153A from Marinobacter aquaeolei has been identified as a fatty acid ω-hydroxylase with a broad substrate range. Two hotspots predicted to influence substrate specificity and selectivity were exchanged. Mutant G307A is 2- to 20-fold more active towards fatty acids than the wild-type. Residue L354 is determinant for the enzyme ω-regioselectivity. A CYP153A monooxygenase has been characterized as a fatty acid ω-hydroxylase with a broad substrate range. Using a sequence-based approach, two hotspots were identified as pivotal for activity and selectivity.
doi_str_mv 10.1039/c2cc18103g
format Article
fullrecord <record><control><sourceid>rsc</sourceid><recordid>TN_cdi_rsc_primary_c2cc18103g</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>c2cc18103g</sourcerecordid><originalsourceid>FETCH-rsc_primary_c2cc18103g3</originalsourceid><addsrcrecordid>eNqFkDFPwzAQRgMCCSgs7EjHBkNK0zTQdoO2QIcKpDLAVF3tS2Pk2JHPqci_x1UrMSCBlzvJ7959dhSdJ5120kkHN6IrRNIP7Wo_Ok7S216c9frvB5s-G8R3aS87ik6YPzvhJFn_eK_7gMKTU6hh9PGaZOk9lNZY-9WsyCATQ24d-IKAGxMKKwabgy1phXHRSBdIjZ4k5Oh9AyiU5Ikm4Z01SgDXVaWpJOPRNaBMsJXolTVwNZlPrwHXqDQuNQ1hhtsgDGgklOQLK7kNY_IBCQu4XrJ3AQJhzZocB8uWrZyVtfAgVQDUst74w-QTMojC2bDQrhyWOzEyA1ebhNiGmRIFklYcz0JGMlBp68PsnAjGL9Mh_P7Z0-gwDynpbFdb0cXj5G30HDsWi8qpMrx08YOnrejyr_tFJfP0P8c35dec3w</addsrcrecordid><sourcetype>Enrichment Source</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Bacterial CYP153A monooxygenases for the synthesis of omega-hydroxylated fatty acidsElectronic supplementary information (ESI) available: Materials and methods. Detailed substrate conversions and product distributions. Gas chromatograms and mass spectra. Michaelis-Menten plots. See DOI: 10.1039/c2cc18103g</title><source>Royal Society Of Chemistry Journals 2008-</source><source>Alma/SFX Local Collection</source><creator>Honda Malca, Sumire ; Scheps, Daniel ; Kühnel, Lisa ; Venegas-Venegas, Elena ; Seifert, Alexander ; Nestl, Bettina M ; Hauer, Bernhard</creator><creatorcontrib>Honda Malca, Sumire ; Scheps, Daniel ; Kühnel, Lisa ; Venegas-Venegas, Elena ; Seifert, Alexander ; Nestl, Bettina M ; Hauer, Bernhard</creatorcontrib><description>CYP153A from Marinobacter aquaeolei has been identified as a fatty acid ω-hydroxylase with a broad substrate range. Two hotspots predicted to influence substrate specificity and selectivity were exchanged. Mutant G307A is 2- to 20-fold more active towards fatty acids than the wild-type. Residue L354 is determinant for the enzyme ω-regioselectivity. A CYP153A monooxygenase has been characterized as a fatty acid ω-hydroxylase with a broad substrate range. Using a sequence-based approach, two hotspots were identified as pivotal for activity and selectivity.</description><identifier>ISSN: 1359-7345</identifier><identifier>EISSN: 1364-548X</identifier><identifier>DOI: 10.1039/c2cc18103g</identifier><language>eng</language><creationdate>2012-04</creationdate><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>314,780,784,27923,27924</link.rule.ids></links><search><creatorcontrib>Honda Malca, Sumire</creatorcontrib><creatorcontrib>Scheps, Daniel</creatorcontrib><creatorcontrib>Kühnel, Lisa</creatorcontrib><creatorcontrib>Venegas-Venegas, Elena</creatorcontrib><creatorcontrib>Seifert, Alexander</creatorcontrib><creatorcontrib>Nestl, Bettina M</creatorcontrib><creatorcontrib>Hauer, Bernhard</creatorcontrib><title>Bacterial CYP153A monooxygenases for the synthesis of omega-hydroxylated fatty acidsElectronic supplementary information (ESI) available: Materials and methods. Detailed substrate conversions and product distributions. Gas chromatograms and mass spectra. Michaelis-Menten plots. See DOI: 10.1039/c2cc18103g</title><description>CYP153A from Marinobacter aquaeolei has been identified as a fatty acid ω-hydroxylase with a broad substrate range. Two hotspots predicted to influence substrate specificity and selectivity were exchanged. Mutant G307A is 2- to 20-fold more active towards fatty acids than the wild-type. Residue L354 is determinant for the enzyme ω-regioselectivity. A CYP153A monooxygenase has been characterized as a fatty acid ω-hydroxylase with a broad substrate range. Using a sequence-based approach, two hotspots were identified as pivotal for activity and selectivity.</description><issn>1359-7345</issn><issn>1364-548X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid/><recordid>eNqFkDFPwzAQRgMCCSgs7EjHBkNK0zTQdoO2QIcKpDLAVF3tS2Pk2JHPqci_x1UrMSCBlzvJ7959dhSdJ5120kkHN6IrRNIP7Wo_Ok7S216c9frvB5s-G8R3aS87ik6YPzvhJFn_eK_7gMKTU6hh9PGaZOk9lNZY-9WsyCATQ24d-IKAGxMKKwabgy1phXHRSBdIjZ4k5Oh9AyiU5Ikm4Z01SgDXVaWpJOPRNaBMsJXolTVwNZlPrwHXqDQuNQ1hhtsgDGgklOQLK7kNY_IBCQu4XrJ3AQJhzZocB8uWrZyVtfAgVQDUst74w-QTMojC2bDQrhyWOzEyA1ebhNiGmRIFklYcz0JGMlBp68PsnAjGL9Mh_P7Z0-gwDynpbFdb0cXj5G30HDsWi8qpMrx08YOnrejyr_tFJfP0P8c35dec3w</recordid><startdate>20120430</startdate><enddate>20120430</enddate><creator>Honda Malca, Sumire</creator><creator>Scheps, Daniel</creator><creator>Kühnel, Lisa</creator><creator>Venegas-Venegas, Elena</creator><creator>Seifert, Alexander</creator><creator>Nestl, Bettina M</creator><creator>Hauer, Bernhard</creator><scope/></search><sort><creationdate>20120430</creationdate><title>Bacterial CYP153A monooxygenases for the synthesis of omega-hydroxylated fatty acidsElectronic supplementary information (ESI) available: Materials and methods. Detailed substrate conversions and product distributions. Gas chromatograms and mass spectra. Michaelis-Menten plots. See DOI: 10.1039/c2cc18103g</title><author>Honda Malca, Sumire ; Scheps, Daniel ; Kühnel, Lisa ; Venegas-Venegas, Elena ; Seifert, Alexander ; Nestl, Bettina M ; Hauer, Bernhard</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-rsc_primary_c2cc18103g3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Honda Malca, Sumire</creatorcontrib><creatorcontrib>Scheps, Daniel</creatorcontrib><creatorcontrib>Kühnel, Lisa</creatorcontrib><creatorcontrib>Venegas-Venegas, Elena</creatorcontrib><creatorcontrib>Seifert, Alexander</creatorcontrib><creatorcontrib>Nestl, Bettina M</creatorcontrib><creatorcontrib>Hauer, Bernhard</creatorcontrib></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Honda Malca, Sumire</au><au>Scheps, Daniel</au><au>Kühnel, Lisa</au><au>Venegas-Venegas, Elena</au><au>Seifert, Alexander</au><au>Nestl, Bettina M</au><au>Hauer, Bernhard</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Bacterial CYP153A monooxygenases for the synthesis of omega-hydroxylated fatty acidsElectronic supplementary information (ESI) available: Materials and methods. Detailed substrate conversions and product distributions. Gas chromatograms and mass spectra. Michaelis-Menten plots. See DOI: 10.1039/c2cc18103g</atitle><date>2012-04-30</date><risdate>2012</risdate><volume>48</volume><issue>42</issue><spage>5115</spage><epage>5117</epage><pages>5115-5117</pages><issn>1359-7345</issn><eissn>1364-548X</eissn><abstract>CYP153A from Marinobacter aquaeolei has been identified as a fatty acid ω-hydroxylase with a broad substrate range. Two hotspots predicted to influence substrate specificity and selectivity were exchanged. Mutant G307A is 2- to 20-fold more active towards fatty acids than the wild-type. Residue L354 is determinant for the enzyme ω-regioselectivity. A CYP153A monooxygenase has been characterized as a fatty acid ω-hydroxylase with a broad substrate range. Using a sequence-based approach, two hotspots were identified as pivotal for activity and selectivity.</abstract><doi>10.1039/c2cc18103g</doi><tpages>3</tpages></addata></record>
fulltext fulltext
identifier ISSN: 1359-7345
ispartof
issn 1359-7345
1364-548X
language eng
recordid cdi_rsc_primary_c2cc18103g
source Royal Society Of Chemistry Journals 2008-; Alma/SFX Local Collection
title Bacterial CYP153A monooxygenases for the synthesis of omega-hydroxylated fatty acidsElectronic supplementary information (ESI) available: Materials and methods. Detailed substrate conversions and product distributions. Gas chromatograms and mass spectra. Michaelis-Menten plots. See DOI: 10.1039/c2cc18103g
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-10T14%3A37%3A48IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-rsc&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Bacterial%20CYP153A%20monooxygenases%20for%20the%20synthesis%20of%20omega-hydroxylated%20fatty%20acidsElectronic%20supplementary%20information%20(ESI)%20available:%20Materials%20and%20methods.%20Detailed%20substrate%20conversions%20and%20product%20distributions.%20Gas%20chromatograms%20and%20mass%20spectra.%20Michaelis-Menten%20plots.%20See%20DOI:%2010.1039/c2cc18103g&rft.au=Honda%20Malca,%20Sumire&rft.date=2012-04-30&rft.volume=48&rft.issue=42&rft.spage=5115&rft.epage=5117&rft.pages=5115-5117&rft.issn=1359-7345&rft.eissn=1364-548X&rft_id=info:doi/10.1039/c2cc18103g&rft_dat=%3Crsc%3Ec2cc18103g%3C/rsc%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_id=info:pmid/&rfr_iscdi=true