Peroxide-dependent oxidation reactions catalyzed by CYP191A1 from Mycobacterium smegmatis
Objectives To find the catalytic activities of CYP191A1 from Mycobacterium smegmatis , in which functions of most P450s are unknown, by using a set of reductase systems, peroxides, and various substrates including fatty acids and human drugs. Results CYP191A1 was functionally expressed in Escherichi...
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| Veröffentlicht in: | Biotechnology letters 2017-08, Vol.39 (8), p.1245-1252 |
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| creator | Jo, Hye-Yeong Park, Sun-Ha Le, Thien-Kim Ma, Sang Hoon Kim, Donghak Ahn, Taeho Joung, Young Hee Yun, Chul-Ho |
| description | Objectives
To find the catalytic activities of CYP191A1 from
Mycobacterium smegmatis
, in which functions of most P450s are unknown, by using a set of reductase systems, peroxides, and various substrates including fatty acids and human drugs.
Results
CYP191A1 was functionally expressed in
Escherichia coli
and purified. Its catalytic activities were examined with fatty acids, chromogenic and fluorogenic substrates, and several human P450 substrates, in the presence of six different types of electron transfer systems, such as rat NADPH-P450 reductase,
Candida
NADPH-P450 reductase, ferredoxin/ferredoxin reductase, putidaredoxin/putidaredoxin reductase, and peroxides (H
2
O
2
and
t
-butyl hydroperoxide). The reactions catalyzed by CYP191A1 included the hydroxylation and
O
-dealkylation of several substrates.
Conclusions
CYP191A1 preferentially catalyzes the peroxide-dependent oxidation of various substrates over the reductase-dependent reaction. Its peroxygenase activity may be used an effective biocatalytic tool to synthesize the metabolites of drugs. |
| doi_str_mv | 10.1007/s10529-017-2358-6 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1900832851</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1900832851</sourcerecordid><originalsourceid>FETCH-LOGICAL-c409t-b4b14d9977c4ac09bf97d37569f9198ded62eab78442b5731396b58f0dbba2653</originalsourceid><addsrcrecordid>eNp1kM9LwzAYhoMobk7_AC9S8OIlmi_9keYow18wcQc97BSS5uvoWNuZtOD8603ZFBE8JSHP-ybfQ8g5sGtgTNx4YCmXlIGgPE5zmh2QMaQippkQ2SEZM0iAponkI3Li_YoxJgUTx2TE85QLADkmizm69qOySC1usLHYdNFw1l3VNpFDXQwbHxW60-vtJ9rIbKPpYg4SbiEqXVtHz9uiNYFDV_V15Gtc1iHtT8lRqdcez_brhLzd371OH-ns5eFpejujRcJkR01iILFSClEkumDSlFLYWKSZLCXI3KLNOGoj8iThJswGscxMmpfMGqN5lsYTcrXr3bj2vUffqbryBa7XusG29wokY3kcJoaAXv5BV23vmvC7QIHIORd8oGBHFa713mGpNq6qtdsqYGrwrnbeVfCuBu8qC5mLfXNvarQ_iW_RAeA7wIerZonu19P_tn4BTBiMyA</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1917822721</pqid></control><display><type>article</type><title>Peroxide-dependent oxidation reactions catalyzed by CYP191A1 from Mycobacterium smegmatis</title><source>MEDLINE</source><source>SpringerNature Journals</source><creator>Jo, Hye-Yeong ; Park, Sun-Ha ; Le, Thien-Kim ; Ma, Sang Hoon ; Kim, Donghak ; Ahn, Taeho ; Joung, Young Hee ; Yun, Chul-Ho</creator><creatorcontrib>Jo, Hye-Yeong ; Park, Sun-Ha ; Le, Thien-Kim ; Ma, Sang Hoon ; Kim, Donghak ; Ahn, Taeho ; Joung, Young Hee ; Yun, Chul-Ho</creatorcontrib><description>Objectives
To find the catalytic activities of CYP191A1 from
Mycobacterium smegmatis
, in which functions of most P450s are unknown, by using a set of reductase systems, peroxides, and various substrates including fatty acids and human drugs.
Results
CYP191A1 was functionally expressed in
Escherichia coli
and purified. Its catalytic activities were examined with fatty acids, chromogenic and fluorogenic substrates, and several human P450 substrates, in the presence of six different types of electron transfer systems, such as rat NADPH-P450 reductase,
Candida
NADPH-P450 reductase, ferredoxin/ferredoxin reductase, putidaredoxin/putidaredoxin reductase, and peroxides (H
2
O
2
and
t
-butyl hydroperoxide). The reactions catalyzed by CYP191A1 included the hydroxylation and
O
-dealkylation of several substrates.
Conclusions
CYP191A1 preferentially catalyzes the peroxide-dependent oxidation of various substrates over the reductase-dependent reaction. Its peroxygenase activity may be used an effective biocatalytic tool to synthesize the metabolites of drugs.</description><identifier>ISSN: 0141-5492</identifier><identifier>EISSN: 1573-6776</identifier><identifier>DOI: 10.1007/s10529-017-2358-6</identifier><identifier>PMID: 28527119</identifier><language>eng</language><publisher>Dordrecht: Springer Netherlands</publisher><subject>Animals ; Applied Microbiology ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Biochemistry ; Biomedical and Life Sciences ; Biotechnology ; Butyl hydroperoxide ; Candida - enzymology ; Candida - genetics ; Catalysis ; Chemical reactions ; Cytochrome P-450 Enzyme System - genetics ; Cytochrome P-450 Enzyme System - metabolism ; Dealkylation ; E coli ; Electron transfer ; Escherichia coli - genetics ; Fatty acids ; Fatty Acids - metabolism ; Ferredoxin reductase ; Fungal Proteins - genetics ; Fungal Proteins - metabolism ; Humans ; Hydrogen peroxide ; Hydroxylation ; Life Sciences ; Metabolites ; Microbiology ; Mycobacterium smegmatis ; Mycobacterium smegmatis - enzymology ; Mycobacterium smegmatis - genetics ; NADP ; Original Research Paper ; Oxidation ; Oxidation-Reduction ; Peroxides ; Peroxides - metabolism ; Pharmaceutical Preparations - analysis ; Pharmaceutical Preparations - metabolism ; Putidaredoxin reductase ; Rats ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Substrates</subject><ispartof>Biotechnology letters, 2017-08, Vol.39 (8), p.1245-1252</ispartof><rights>Springer Science+Business Media Dordrecht 2017</rights><rights>Biotechnology Letters is a copyright of Springer, 2017.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c409t-b4b14d9977c4ac09bf97d37569f9198ded62eab78442b5731396b58f0dbba2653</citedby><cites>FETCH-LOGICAL-c409t-b4b14d9977c4ac09bf97d37569f9198ded62eab78442b5731396b58f0dbba2653</cites><orcidid>0000-0003-2685-2968</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s10529-017-2358-6$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s10529-017-2358-6$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,780,784,27924,27925,41488,42557,51319</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/28527119$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jo, Hye-Yeong</creatorcontrib><creatorcontrib>Park, Sun-Ha</creatorcontrib><creatorcontrib>Le, Thien-Kim</creatorcontrib><creatorcontrib>Ma, Sang Hoon</creatorcontrib><creatorcontrib>Kim, Donghak</creatorcontrib><creatorcontrib>Ahn, Taeho</creatorcontrib><creatorcontrib>Joung, Young Hee</creatorcontrib><creatorcontrib>Yun, Chul-Ho</creatorcontrib><title>Peroxide-dependent oxidation reactions catalyzed by CYP191A1 from Mycobacterium smegmatis</title><title>Biotechnology letters</title><addtitle>Biotechnol Lett</addtitle><addtitle>Biotechnol Lett</addtitle><description>Objectives
To find the catalytic activities of CYP191A1 from
Mycobacterium smegmatis
, in which functions of most P450s are unknown, by using a set of reductase systems, peroxides, and various substrates including fatty acids and human drugs.
Results
CYP191A1 was functionally expressed in
Escherichia coli
and purified. Its catalytic activities were examined with fatty acids, chromogenic and fluorogenic substrates, and several human P450 substrates, in the presence of six different types of electron transfer systems, such as rat NADPH-P450 reductase,
Candida
NADPH-P450 reductase, ferredoxin/ferredoxin reductase, putidaredoxin/putidaredoxin reductase, and peroxides (H
2
O
2
and
t
-butyl hydroperoxide). The reactions catalyzed by CYP191A1 included the hydroxylation and
O
-dealkylation of several substrates.
Conclusions
CYP191A1 preferentially catalyzes the peroxide-dependent oxidation of various substrates over the reductase-dependent reaction. Its peroxygenase activity may be used an effective biocatalytic tool to synthesize the metabolites of drugs.</description><subject>Animals</subject><subject>Applied Microbiology</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biotechnology</subject><subject>Butyl hydroperoxide</subject><subject>Candida - enzymology</subject><subject>Candida - genetics</subject><subject>Catalysis</subject><subject>Chemical reactions</subject><subject>Cytochrome P-450 Enzyme System - genetics</subject><subject>Cytochrome P-450 Enzyme System - metabolism</subject><subject>Dealkylation</subject><subject>E coli</subject><subject>Electron transfer</subject><subject>Escherichia coli - genetics</subject><subject>Fatty acids</subject><subject>Fatty Acids - metabolism</subject><subject>Ferredoxin reductase</subject><subject>Fungal Proteins - genetics</subject><subject>Fungal Proteins - metabolism</subject><subject>Humans</subject><subject>Hydrogen peroxide</subject><subject>Hydroxylation</subject><subject>Life Sciences</subject><subject>Metabolites</subject><subject>Microbiology</subject><subject>Mycobacterium smegmatis</subject><subject>Mycobacterium smegmatis - enzymology</subject><subject>Mycobacterium smegmatis - genetics</subject><subject>NADP</subject><subject>Original Research Paper</subject><subject>Oxidation</subject><subject>Oxidation-Reduction</subject><subject>Peroxides</subject><subject>Peroxides - metabolism</subject><subject>Pharmaceutical Preparations - analysis</subject><subject>Pharmaceutical Preparations - metabolism</subject><subject>Putidaredoxin reductase</subject><subject>Rats</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Substrates</subject><issn>0141-5492</issn><issn>1573-6776</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp1kM9LwzAYhoMobk7_AC9S8OIlmi_9keYow18wcQc97BSS5uvoWNuZtOD8603ZFBE8JSHP-ybfQ8g5sGtgTNx4YCmXlIGgPE5zmh2QMaQippkQ2SEZM0iAponkI3Li_YoxJgUTx2TE85QLADkmizm69qOySC1usLHYdNFw1l3VNpFDXQwbHxW60-vtJ9rIbKPpYg4SbiEqXVtHz9uiNYFDV_V15Gtc1iHtT8lRqdcez_brhLzd371OH-ns5eFpejujRcJkR01iILFSClEkumDSlFLYWKSZLCXI3KLNOGoj8iThJswGscxMmpfMGqN5lsYTcrXr3bj2vUffqbryBa7XusG29wokY3kcJoaAXv5BV23vmvC7QIHIORd8oGBHFa713mGpNq6qtdsqYGrwrnbeVfCuBu8qC5mLfXNvarQ_iW_RAeA7wIerZonu19P_tn4BTBiMyA</recordid><startdate>20170801</startdate><enddate>20170801</enddate><creator>Jo, Hye-Yeong</creator><creator>Park, Sun-Ha</creator><creator>Le, Thien-Kim</creator><creator>Ma, Sang Hoon</creator><creator>Kim, Donghak</creator><creator>Ahn, Taeho</creator><creator>Joung, Young Hee</creator><creator>Yun, Chul-Ho</creator><general>Springer Netherlands</general><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7QR</scope><scope>7T7</scope><scope>7TB</scope><scope>7U5</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>L6V</scope><scope>L7M</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>Q9U</scope><scope>7X8</scope><orcidid>https://orcid.org/0000-0003-2685-2968</orcidid></search><sort><creationdate>20170801</creationdate><title>Peroxide-dependent oxidation reactions catalyzed by CYP191A1 from Mycobacterium smegmatis</title><author>Jo, Hye-Yeong ; Park, Sun-Ha ; Le, Thien-Kim ; Ma, Sang Hoon ; Kim, Donghak ; Ahn, Taeho ; Joung, Young Hee ; Yun, Chul-Ho</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c409t-b4b14d9977c4ac09bf97d37569f9198ded62eab78442b5731396b58f0dbba2653</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Animals</topic><topic>Applied Microbiology</topic><topic>Bacterial Proteins - genetics</topic><topic>Bacterial Proteins - metabolism</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Biotechnology</topic><topic>Butyl hydroperoxide</topic><topic>Candida - enzymology</topic><topic>Candida - genetics</topic><topic>Catalysis</topic><topic>Chemical reactions</topic><topic>Cytochrome P-450 Enzyme System - genetics</topic><topic>Cytochrome P-450 Enzyme System - metabolism</topic><topic>Dealkylation</topic><topic>E coli</topic><topic>Electron transfer</topic><topic>Escherichia coli - genetics</topic><topic>Fatty acids</topic><topic>Fatty Acids - metabolism</topic><topic>Ferredoxin reductase</topic><topic>Fungal Proteins - genetics</topic><topic>Fungal Proteins - metabolism</topic><topic>Humans</topic><topic>Hydrogen peroxide</topic><topic>Hydroxylation</topic><topic>Life Sciences</topic><topic>Metabolites</topic><topic>Microbiology</topic><topic>Mycobacterium smegmatis</topic><topic>Mycobacterium smegmatis - enzymology</topic><topic>Mycobacterium smegmatis - genetics</topic><topic>NADP</topic><topic>Original Research Paper</topic><topic>Oxidation</topic><topic>Oxidation-Reduction</topic><topic>Peroxides</topic><topic>Peroxides - metabolism</topic><topic>Pharmaceutical Preparations - analysis</topic><topic>Pharmaceutical Preparations - metabolism</topic><topic>Putidaredoxin reductase</topic><topic>Rats</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><topic>Substrates</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jo, Hye-Yeong</creatorcontrib><creatorcontrib>Park, Sun-Ha</creatorcontrib><creatorcontrib>Le, Thien-Kim</creatorcontrib><creatorcontrib>Ma, Sang Hoon</creatorcontrib><creatorcontrib>Kim, Donghak</creatorcontrib><creatorcontrib>Ahn, Taeho</creatorcontrib><creatorcontrib>Joung, Young Hee</creatorcontrib><creatorcontrib>Yun, Chul-Ho</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Chemoreception Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Mechanical & Transportation Engineering Abstracts</collection><collection>Solid State and Superconductivity Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Materials Science & Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Engineering Collection</collection><collection>Advanced Technologies Database with Aerospace</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Engineering Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>Engineering Collection</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><jtitle>Biotechnology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jo, Hye-Yeong</au><au>Park, Sun-Ha</au><au>Le, Thien-Kim</au><au>Ma, Sang Hoon</au><au>Kim, Donghak</au><au>Ahn, Taeho</au><au>Joung, Young Hee</au><au>Yun, Chul-Ho</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Peroxide-dependent oxidation reactions catalyzed by CYP191A1 from Mycobacterium smegmatis</atitle><jtitle>Biotechnology letters</jtitle><stitle>Biotechnol Lett</stitle><addtitle>Biotechnol Lett</addtitle><date>2017-08-01</date><risdate>2017</risdate><volume>39</volume><issue>8</issue><spage>1245</spage><epage>1252</epage><pages>1245-1252</pages><issn>0141-5492</issn><eissn>1573-6776</eissn><abstract>Objectives
To find the catalytic activities of CYP191A1 from
Mycobacterium smegmatis
, in which functions of most P450s are unknown, by using a set of reductase systems, peroxides, and various substrates including fatty acids and human drugs.
Results
CYP191A1 was functionally expressed in
Escherichia coli
and purified. Its catalytic activities were examined with fatty acids, chromogenic and fluorogenic substrates, and several human P450 substrates, in the presence of six different types of electron transfer systems, such as rat NADPH-P450 reductase,
Candida
NADPH-P450 reductase, ferredoxin/ferredoxin reductase, putidaredoxin/putidaredoxin reductase, and peroxides (H
2
O
2
and
t
-butyl hydroperoxide). The reactions catalyzed by CYP191A1 included the hydroxylation and
O
-dealkylation of several substrates.
Conclusions
CYP191A1 preferentially catalyzes the peroxide-dependent oxidation of various substrates over the reductase-dependent reaction. Its peroxygenase activity may be used an effective biocatalytic tool to synthesize the metabolites of drugs.</abstract><cop>Dordrecht</cop><pub>Springer Netherlands</pub><pmid>28527119</pmid><doi>10.1007/s10529-017-2358-6</doi><tpages>8</tpages><orcidid>https://orcid.org/0000-0003-2685-2968</orcidid></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0141-5492 |
| ispartof | Biotechnology letters, 2017-08, Vol.39 (8), p.1245-1252 |
| issn | 0141-5492 1573-6776 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1900832851 |
| source | MEDLINE; SpringerNature Journals |
| subjects | Animals Applied Microbiology Bacterial Proteins - genetics Bacterial Proteins - metabolism Biochemistry Biomedical and Life Sciences Biotechnology Butyl hydroperoxide Candida - enzymology Candida - genetics Catalysis Chemical reactions Cytochrome P-450 Enzyme System - genetics Cytochrome P-450 Enzyme System - metabolism Dealkylation E coli Electron transfer Escherichia coli - genetics Fatty acids Fatty Acids - metabolism Ferredoxin reductase Fungal Proteins - genetics Fungal Proteins - metabolism Humans Hydrogen peroxide Hydroxylation Life Sciences Metabolites Microbiology Mycobacterium smegmatis Mycobacterium smegmatis - enzymology Mycobacterium smegmatis - genetics NADP Original Research Paper Oxidation Oxidation-Reduction Peroxides Peroxides - metabolism Pharmaceutical Preparations - analysis Pharmaceutical Preparations - metabolism Putidaredoxin reductase Rats Recombinant Proteins - genetics Recombinant Proteins - metabolism Substrates |
| title | Peroxide-dependent oxidation reactions catalyzed by CYP191A1 from Mycobacterium smegmatis |
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