A novel family of bacterial dioxygenases that catalyse the hydroxylation of free l-amino acids
Abstract l-isoleucine-4-hydroxylase (IDO) is a recently discovered member of the Pfam family PF10014 (the former DUF 2257 family) of uncharacterized conserved bacterial proteins. To uncover the range of biochemical activities carried out by PF10014 members, eight in silico-selected IDO homologues be...
Gespeichert in:
| Veröffentlicht in: | FEMS microbiology letters 2012-06, Vol.331 (2), p.97-104 |
|---|---|
| Hauptverfasser: | , , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 104 |
|---|---|
| container_issue | 2 |
| container_start_page | 97 |
| container_title | FEMS microbiology letters |
| container_volume | 331 |
| creator | Smirnov, Sergey V. Sokolov, Pavel M. Kodera, Tomohiro Sugiyama, Masakazu Hibi, Makoto Shimizu, Sakayu Yokozeki, Kenzo Ogawa, Jun |
| description | Abstract
l-isoleucine-4-hydroxylase (IDO) is a recently discovered member of the Pfam family PF10014 (the former DUF 2257 family) of uncharacterized conserved bacterial proteins. To uncover the range of biochemical activities carried out by PF10014 members, eight in silico-selected IDO homologues belonging to the PF10014 were cloned and expressed in Escherichia coli. l-methionine, l-leucine, l-isoleucine and l-threonine were found to be catalysed by the investigated enzymes, producing l-methionine sulfoxide, 4-hydroxyleucine, 4-hydroxyisoleucine and 4-hydroxythreonine, respectively. An investigation of enzyme kinetics suggested the existence of a novel subfamily of bacterial dioxygenases within the PF10014 family for which free l-amino acids could be accepted as in vivo substrates. A hypothesis regarding the physiological significance of hydroxylated l-amino acids is also discussed. |
| doi_str_mv | 10.1111/j.1574-6968.2012.02558.x |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1015094553</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><oup_id>10.1111/j.1574-6968.2012.02558.x</oup_id><sourcerecordid>2305790383</sourcerecordid><originalsourceid>FETCH-LOGICAL-c4418-4938db2f88aa34a805ff0b6ec5f86dacf041b55024723e6c316b0c83356a6fa43</originalsourceid><addsrcrecordid>eNqNkc1u1DAUhS1ERYfCKyBLbNgkXP_GWbCoqrYgDeoGtliOY9OMPPFgJzB5exymdAFCwhvb8neOr85BCBOoSVlvdzURDa9kK1VNgdAaqBCqPj5Bm8eHp2gDrFEVgbY5R89z3gEApyCfoXNKOVeq4Rv05RKP8bsL2Jv9EBYcPe6MnVwaTMD9EI_LVzea7DKe7s2ErZlMWLIrN4fvlz4VIJhpiOOq9Mk5HKriNEZs7NDnF-jMm5Ddy4f9An2-uf509b7a3t1-uLrcVpZzoireMtV31CtlDONGgfAeOums8Er2xnrgpBMCKG8oc9IyIjuwijEhjfSGswv05uR7SPHb7PKk90O2LgQzujhnTYAIaLkQrKCv_0B3cU5jmU5TBqJpgamVUifKpphzcl4f0rA3aSlWeu1A7_QatV6j1msH-lcH-likrx4-mLu96x-Fv0MvwLsT8GMIbvlvY33zcbueip6d9HE-_ENd_T3WTwfFo7w</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2305790383</pqid></control><display><type>article</type><title>A novel family of bacterial dioxygenases that catalyse the hydroxylation of free l-amino acids</title><source>MEDLINE</source><source>Access via Wiley Online Library</source><source>Oxford University Press Journals All Titles (1996-Current)</source><creator>Smirnov, Sergey V. ; Sokolov, Pavel M. ; Kodera, Tomohiro ; Sugiyama, Masakazu ; Hibi, Makoto ; Shimizu, Sakayu ; Yokozeki, Kenzo ; Ogawa, Jun</creator><creatorcontrib>Smirnov, Sergey V. ; Sokolov, Pavel M. ; Kodera, Tomohiro ; Sugiyama, Masakazu ; Hibi, Makoto ; Shimizu, Sakayu ; Yokozeki, Kenzo ; Ogawa, Jun</creatorcontrib><description>Abstract
l-isoleucine-4-hydroxylase (IDO) is a recently discovered member of the Pfam family PF10014 (the former DUF 2257 family) of uncharacterized conserved bacterial proteins. To uncover the range of biochemical activities carried out by PF10014 members, eight in silico-selected IDO homologues belonging to the PF10014 were cloned and expressed in Escherichia coli. l-methionine, l-leucine, l-isoleucine and l-threonine were found to be catalysed by the investigated enzymes, producing l-methionine sulfoxide, 4-hydroxyleucine, 4-hydroxyisoleucine and 4-hydroxythreonine, respectively. An investigation of enzyme kinetics suggested the existence of a novel subfamily of bacterial dioxygenases within the PF10014 family for which free l-amino acids could be accepted as in vivo substrates. A hypothesis regarding the physiological significance of hydroxylated l-amino acids is also discussed.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.2012.02558.x</identifier><identifier>PMID: 22448874</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>4‐hydroxyisoleucine ; 4‐hydroxythreonine ; Amino acids ; Amino Acids - metabolism ; Bacteria ; Bacteria - classification ; Bacteria - enzymology ; Bacteria - genetics ; Cloning, Molecular ; dioxygenase ; Dioxygenases - classification ; Dioxygenases - genetics ; Dioxygenases - metabolism ; E coli ; Enzyme kinetics ; Escherichia coli - enzymology ; Escherichia coli - genetics ; Homology ; Hydroxylase ; Hydroxylation ; Isoleucine ; Isoleucine - metabolism ; Kinetics ; Leucine ; Leucine - metabolism ; l‐methionine sulfoxide ; Methionine ; Methionine - metabolism ; Microbiology ; plant pathogenic bacteria ; Reaction kinetics ; Substrate Specificity ; Substrates ; Threonine ; Threonine - metabolism ; vitamin B6 biosynthesis</subject><ispartof>FEMS microbiology letters, 2012-06, Vol.331 (2), p.97-104</ispartof><rights>2012 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved 2012</rights><rights>2012 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved</rights><rights>2012 Federation of European Microbiological Societies. Published by Blackwell Publishing Ltd. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4418-4938db2f88aa34a805ff0b6ec5f86dacf041b55024723e6c316b0c83356a6fa43</citedby><cites>FETCH-LOGICAL-c4418-4938db2f88aa34a805ff0b6ec5f86dacf041b55024723e6c316b0c83356a6fa43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1574-6968.2012.02558.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1574-6968.2012.02558.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22448874$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Smirnov, Sergey V.</creatorcontrib><creatorcontrib>Sokolov, Pavel M.</creatorcontrib><creatorcontrib>Kodera, Tomohiro</creatorcontrib><creatorcontrib>Sugiyama, Masakazu</creatorcontrib><creatorcontrib>Hibi, Makoto</creatorcontrib><creatorcontrib>Shimizu, Sakayu</creatorcontrib><creatorcontrib>Yokozeki, Kenzo</creatorcontrib><creatorcontrib>Ogawa, Jun</creatorcontrib><title>A novel family of bacterial dioxygenases that catalyse the hydroxylation of free l-amino acids</title><title>FEMS microbiology letters</title><addtitle>FEMS Microbiol Lett</addtitle><description>Abstract
l-isoleucine-4-hydroxylase (IDO) is a recently discovered member of the Pfam family PF10014 (the former DUF 2257 family) of uncharacterized conserved bacterial proteins. To uncover the range of biochemical activities carried out by PF10014 members, eight in silico-selected IDO homologues belonging to the PF10014 were cloned and expressed in Escherichia coli. l-methionine, l-leucine, l-isoleucine and l-threonine were found to be catalysed by the investigated enzymes, producing l-methionine sulfoxide, 4-hydroxyleucine, 4-hydroxyisoleucine and 4-hydroxythreonine, respectively. An investigation of enzyme kinetics suggested the existence of a novel subfamily of bacterial dioxygenases within the PF10014 family for which free l-amino acids could be accepted as in vivo substrates. A hypothesis regarding the physiological significance of hydroxylated l-amino acids is also discussed.</description><subject>4‐hydroxyisoleucine</subject><subject>4‐hydroxythreonine</subject><subject>Amino acids</subject><subject>Amino Acids - metabolism</subject><subject>Bacteria</subject><subject>Bacteria - classification</subject><subject>Bacteria - enzymology</subject><subject>Bacteria - genetics</subject><subject>Cloning, Molecular</subject><subject>dioxygenase</subject><subject>Dioxygenases - classification</subject><subject>Dioxygenases - genetics</subject><subject>Dioxygenases - metabolism</subject><subject>E coli</subject><subject>Enzyme kinetics</subject><subject>Escherichia coli - enzymology</subject><subject>Escherichia coli - genetics</subject><subject>Homology</subject><subject>Hydroxylase</subject><subject>Hydroxylation</subject><subject>Isoleucine</subject><subject>Isoleucine - metabolism</subject><subject>Kinetics</subject><subject>Leucine</subject><subject>Leucine - metabolism</subject><subject>l‐methionine sulfoxide</subject><subject>Methionine</subject><subject>Methionine - metabolism</subject><subject>Microbiology</subject><subject>plant pathogenic bacteria</subject><subject>Reaction kinetics</subject><subject>Substrate Specificity</subject><subject>Substrates</subject><subject>Threonine</subject><subject>Threonine - metabolism</subject><subject>vitamin B6 biosynthesis</subject><issn>0378-1097</issn><issn>1574-6968</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</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>eNqNkc1u1DAUhS1ERYfCKyBLbNgkXP_GWbCoqrYgDeoGtliOY9OMPPFgJzB5exymdAFCwhvb8neOr85BCBOoSVlvdzURDa9kK1VNgdAaqBCqPj5Bm8eHp2gDrFEVgbY5R89z3gEApyCfoXNKOVeq4Rv05RKP8bsL2Jv9EBYcPe6MnVwaTMD9EI_LVzea7DKe7s2ErZlMWLIrN4fvlz4VIJhpiOOq9Mk5HKriNEZs7NDnF-jMm5Ddy4f9An2-uf509b7a3t1-uLrcVpZzoireMtV31CtlDONGgfAeOums8Er2xnrgpBMCKG8oc9IyIjuwijEhjfSGswv05uR7SPHb7PKk90O2LgQzujhnTYAIaLkQrKCv_0B3cU5jmU5TBqJpgamVUifKpphzcl4f0rA3aSlWeu1A7_QatV6j1msH-lcH-likrx4-mLu96x-Fv0MvwLsT8GMIbvlvY33zcbueip6d9HE-_ENd_T3WTwfFo7w</recordid><startdate>20120601</startdate><enddate>20120601</enddate><creator>Smirnov, Sergey V.</creator><creator>Sokolov, Pavel M.</creator><creator>Kodera, Tomohiro</creator><creator>Sugiyama, Masakazu</creator><creator>Hibi, Makoto</creator><creator>Shimizu, Sakayu</creator><creator>Yokozeki, Kenzo</creator><creator>Ogawa, Jun</creator><general>Blackwell Publishing Ltd</general><general>Oxford University Press</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>7T7</scope><scope>7TK</scope><scope>7TM</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</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>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20120601</creationdate><title>A novel family of bacterial dioxygenases that catalyse the hydroxylation of free l-amino acids</title><author>Smirnov, Sergey V. ; Sokolov, Pavel M. ; Kodera, Tomohiro ; Sugiyama, Masakazu ; Hibi, Makoto ; Shimizu, Sakayu ; Yokozeki, Kenzo ; Ogawa, Jun</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4418-4938db2f88aa34a805ff0b6ec5f86dacf041b55024723e6c316b0c83356a6fa43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>4‐hydroxyisoleucine</topic><topic>4‐hydroxythreonine</topic><topic>Amino acids</topic><topic>Amino Acids - metabolism</topic><topic>Bacteria</topic><topic>Bacteria - classification</topic><topic>Bacteria - enzymology</topic><topic>Bacteria - genetics</topic><topic>Cloning, Molecular</topic><topic>dioxygenase</topic><topic>Dioxygenases - classification</topic><topic>Dioxygenases - genetics</topic><topic>Dioxygenases - metabolism</topic><topic>E coli</topic><topic>Enzyme kinetics</topic><topic>Escherichia coli - enzymology</topic><topic>Escherichia coli - genetics</topic><topic>Homology</topic><topic>Hydroxylase</topic><topic>Hydroxylation</topic><topic>Isoleucine</topic><topic>Isoleucine - metabolism</topic><topic>Kinetics</topic><topic>Leucine</topic><topic>Leucine - metabolism</topic><topic>l‐methionine sulfoxide</topic><topic>Methionine</topic><topic>Methionine - metabolism</topic><topic>Microbiology</topic><topic>plant pathogenic bacteria</topic><topic>Reaction kinetics</topic><topic>Substrate Specificity</topic><topic>Substrates</topic><topic>Threonine</topic><topic>Threonine - metabolism</topic><topic>vitamin B6 biosynthesis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Smirnov, Sergey V.</creatorcontrib><creatorcontrib>Sokolov, Pavel M.</creatorcontrib><creatorcontrib>Kodera, Tomohiro</creatorcontrib><creatorcontrib>Sugiyama, Masakazu</creatorcontrib><creatorcontrib>Hibi, Makoto</creatorcontrib><creatorcontrib>Shimizu, Sakayu</creatorcontrib><creatorcontrib>Yokozeki, Kenzo</creatorcontrib><creatorcontrib>Ogawa, Jun</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>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech 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>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>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>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science 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>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>FEMS microbiology letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Smirnov, Sergey V.</au><au>Sokolov, Pavel M.</au><au>Kodera, Tomohiro</au><au>Sugiyama, Masakazu</au><au>Hibi, Makoto</au><au>Shimizu, Sakayu</au><au>Yokozeki, Kenzo</au><au>Ogawa, Jun</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A novel family of bacterial dioxygenases that catalyse the hydroxylation of free l-amino acids</atitle><jtitle>FEMS microbiology letters</jtitle><addtitle>FEMS Microbiol Lett</addtitle><date>2012-06-01</date><risdate>2012</risdate><volume>331</volume><issue>2</issue><spage>97</spage><epage>104</epage><pages>97-104</pages><issn>0378-1097</issn><eissn>1574-6968</eissn><abstract>Abstract
l-isoleucine-4-hydroxylase (IDO) is a recently discovered member of the Pfam family PF10014 (the former DUF 2257 family) of uncharacterized conserved bacterial proteins. To uncover the range of biochemical activities carried out by PF10014 members, eight in silico-selected IDO homologues belonging to the PF10014 were cloned and expressed in Escherichia coli. l-methionine, l-leucine, l-isoleucine and l-threonine were found to be catalysed by the investigated enzymes, producing l-methionine sulfoxide, 4-hydroxyleucine, 4-hydroxyisoleucine and 4-hydroxythreonine, respectively. An investigation of enzyme kinetics suggested the existence of a novel subfamily of bacterial dioxygenases within the PF10014 family for which free l-amino acids could be accepted as in vivo substrates. A hypothesis regarding the physiological significance of hydroxylated l-amino acids is also discussed.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><pmid>22448874</pmid><doi>10.1111/j.1574-6968.2012.02558.x</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0378-1097 |
| ispartof | FEMS microbiology letters, 2012-06, Vol.331 (2), p.97-104 |
| issn | 0378-1097 1574-6968 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_1015094553 |
| source | MEDLINE; Access via Wiley Online Library; Oxford University Press Journals All Titles (1996-Current) |
| subjects | 4‐hydroxyisoleucine 4‐hydroxythreonine Amino acids Amino Acids - metabolism Bacteria Bacteria - classification Bacteria - enzymology Bacteria - genetics Cloning, Molecular dioxygenase Dioxygenases - classification Dioxygenases - genetics Dioxygenases - metabolism E coli Enzyme kinetics Escherichia coli - enzymology Escherichia coli - genetics Homology Hydroxylase Hydroxylation Isoleucine Isoleucine - metabolism Kinetics Leucine Leucine - metabolism l‐methionine sulfoxide Methionine Methionine - metabolism Microbiology plant pathogenic bacteria Reaction kinetics Substrate Specificity Substrates Threonine Threonine - metabolism vitamin B6 biosynthesis |
| title | A novel family of bacterial dioxygenases that catalyse the hydroxylation of free l-amino acids |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-12-19T16%3A49%3A53IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=A%20novel%20family%20of%20bacterial%20dioxygenases%20that%20catalyse%20the%20hydroxylation%20of%20free%20l-amino%20acids&rft.jtitle=FEMS%20microbiology%20letters&rft.au=Smirnov,%20Sergey%20V.&rft.date=2012-06-01&rft.volume=331&rft.issue=2&rft.spage=97&rft.epage=104&rft.pages=97-104&rft.issn=0378-1097&rft.eissn=1574-6968&rft_id=info:doi/10.1111/j.1574-6968.2012.02558.x&rft_dat=%3Cproquest_cross%3E2305790383%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=2305790383&rft_id=info:pmid/22448874&rft_oup_id=10.1111/j.1574-6968.2012.02558.x&rfr_iscdi=true |