Two O-methyltransferases from Picea abies: characterization and molecular basis of different reactivity
O-Methyltransferase (OMT) catalyzes the transfer of a methyl group from S-adenosyl methionine (SAM) to hydroxyl groups of methyl acceptors. Two OMTs, PaOMT2 and PaOMT3, from Picea abies showed 93.5% identity at the amino acid level. However, PaOMT3 catalyzed the reaction more efficiently than PaOMT2...
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| Veröffentlicht in: | Planta 2010-09, Vol.232 (4), p.837-844 |
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| creator | Kim, Bong-Gyu Kim, Dae Hwan Sung, Su Hyun Kim, Dong-Eun Chong, Youhoon Ahn, Joong-Hoon |
| description | O-Methyltransferase (OMT) catalyzes the transfer of a methyl group from S-adenosyl methionine (SAM) to hydroxyl groups of methyl acceptors. Two OMTs, PaOMT2 and PaOMT3, from Picea abies showed 93.5% identity at the amino acid level. However, PaOMT3 catalyzed the reaction more efficiently than PaOMT2 with several phenolic compounds, including quercetin and caffeoyl-CoA. To determine the critical amino acids for the different reactivity of the two OMTs, site-directed mutagenesis was carried out. The amino acid proline at position 35 in PaOMT2 and leucine in PaOMT3 is a critical amino acid for their reactivity. Molecular modeling showed that the sequential change triggered by Leu35 resulted in a change in the size of the substrate binding pocket, which could account for the different catalytic reactivity of two OMTs. |
| doi_str_mv | 10.1007/s00425-010-1223-9 |
| format | Article |
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Two OMTs, PaOMT2 and PaOMT3, from Picea abies showed 93.5% identity at the amino acid level. However, PaOMT3 catalyzed the reaction more efficiently than PaOMT2 with several phenolic compounds, including quercetin and caffeoyl-CoA. To determine the critical amino acids for the different reactivity of the two OMTs, site-directed mutagenesis was carried out. The amino acid proline at position 35 in PaOMT2 and leucine in PaOMT3 is a critical amino acid for their reactivity. Molecular modeling showed that the sequential change triggered by Leu35 resulted in a change in the size of the substrate binding pocket, which could account for the different catalytic reactivity of two OMTs.</description><identifier>ISSN: 0032-0935</identifier><identifier>EISSN: 1432-2048</identifier><identifier>DOI: 10.1007/s00425-010-1223-9</identifier><identifier>PMID: 20628758</identifier><identifier>CODEN: PLANAB</identifier><language>eng</language><publisher>Berlin/Heidelberg: Springer-Verlag</publisher><subject>Agriculture ; Amino Acid Sequence ; Amino acids ; Binding sites ; Biological and medical sciences ; Biomedical and Life Sciences ; Biosynthesis ; Chromatography, High Pressure Liquid ; Ecology ; Enzymes ; Flavonoids ; Forestry ; Fundamental and applied biological sciences. Psychology ; Hydroxyls ; Life Sciences ; Lignin ; Methyltransferases - chemistry ; Methyltransferases - genetics ; Methyltransferases - metabolism ; Molecular Sequence Data ; Original Article ; Phenols ; Picea - enzymology ; Picea - genetics ; Plant Proteins - chemistry ; Plant Proteins - genetics ; Plant Proteins - metabolism ; Plant Sciences ; Protein Binding ; Protein Structure, Secondary ; Reaction products ; Reactivity ; Reverse Transcriptase Polymerase Chain Reaction ; Sequence Homology, Amino Acid ; Substrate specificity</subject><ispartof>Planta, 2010-09, Vol.232 (4), p.837-844</ispartof><rights>Springer-Verlag Berlin Heidelberg 2010</rights><rights>Springer-Verlag 2010</rights><rights>2015 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c422t-1a9de5331a09a8f4b6417b4e66025a29e1dd9ca002be5376c21c62d81842c0483</citedby><cites>FETCH-LOGICAL-c422t-1a9de5331a09a8f4b6417b4e66025a29e1dd9ca002be5376c21c62d81842c0483</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/23391985$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/23391985$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,776,780,799,27903,27904,41467,42536,51298,57996,58229</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=23204403$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/20628758$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kim, Bong-Gyu</creatorcontrib><creatorcontrib>Kim, Dae Hwan</creatorcontrib><creatorcontrib>Sung, Su Hyun</creatorcontrib><creatorcontrib>Kim, Dong-Eun</creatorcontrib><creatorcontrib>Chong, Youhoon</creatorcontrib><creatorcontrib>Ahn, Joong-Hoon</creatorcontrib><title>Two O-methyltransferases from Picea abies: characterization and molecular basis of different reactivity</title><title>Planta</title><addtitle>Planta</addtitle><addtitle>Planta</addtitle><description>O-Methyltransferase (OMT) catalyzes the transfer of a methyl group from S-adenosyl methionine (SAM) to hydroxyl groups of methyl acceptors. Two OMTs, PaOMT2 and PaOMT3, from Picea abies showed 93.5% identity at the amino acid level. However, PaOMT3 catalyzed the reaction more efficiently than PaOMT2 with several phenolic compounds, including quercetin and caffeoyl-CoA. To determine the critical amino acids for the different reactivity of the two OMTs, site-directed mutagenesis was carried out. The amino acid proline at position 35 in PaOMT2 and leucine in PaOMT3 is a critical amino acid for their reactivity. Molecular modeling showed that the sequential change triggered by Leu35 resulted in a change in the size of the substrate binding pocket, which could account for the different catalytic reactivity of two OMTs.</description><subject>Agriculture</subject><subject>Amino Acid Sequence</subject><subject>Amino acids</subject><subject>Binding sites</subject><subject>Biological and medical sciences</subject><subject>Biomedical and Life Sciences</subject><subject>Biosynthesis</subject><subject>Chromatography, High Pressure Liquid</subject><subject>Ecology</subject><subject>Enzymes</subject><subject>Flavonoids</subject><subject>Forestry</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Hydroxyls</subject><subject>Life Sciences</subject><subject>Lignin</subject><subject>Methyltransferases - chemistry</subject><subject>Methyltransferases - genetics</subject><subject>Methyltransferases - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Original Article</subject><subject>Phenols</subject><subject>Picea - enzymology</subject><subject>Picea - genetics</subject><subject>Plant Proteins - chemistry</subject><subject>Plant Proteins - genetics</subject><subject>Plant Proteins - metabolism</subject><subject>Plant Sciences</subject><subject>Protein Binding</subject><subject>Protein Structure, Secondary</subject><subject>Reaction products</subject><subject>Reactivity</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>Sequence Homology, Amino Acid</subject><subject>Substrate specificity</subject><issn>0032-0935</issn><issn>1432-2048</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2010</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>eNp9kUtP3DAUhS1UVKbAD2DRyqrUZej1Iw93V6EWKiHBgq6jG8cBj5KY-npaDb--HmUKXbGyrfudc-xjxs4EnAuA-jMBaFkWIKAQUqrCHLCV0EoWEnTzhq0A8h6MKo_YO6I1QB7W9Vt2JKGSTV02K3Z_9yfwm2Jy6WE7pogzDS4iOeJDDBO_9dYhx847-sLtA0a0yUX_hMmHmePc8ymMzm5GjLxD8sTDwHs_ZBM3Jx5d5v1vn7Yn7HDAkdzpfj1mP79_u7u4Kq5vLn9cfL0urJYyFQJN70qlBILBZtBdpUXdaVdVIEuUxom-NxYBZJexurJS2Er2jWi0tPnR6ph9XHwfY_i1cZTaddjEOUe2ta5NBZVRGRILZGMgim5oH6OfMG5bAe2u2XZptoXdOTfbmqz5sDfedJPrnxX_qszApz2AZHEccpfW0wun8qdo2IXLhaM8mu9dfLnha-nvF9GaUoj_mSojTFOqv8XVmjc</recordid><startdate>20100901</startdate><enddate>20100901</enddate><creator>Kim, Bong-Gyu</creator><creator>Kim, Dae Hwan</creator><creator>Sung, Su Hyun</creator><creator>Kim, Dong-Eun</creator><creator>Chong, Youhoon</creator><creator>Ahn, Joong-Hoon</creator><general>Springer-Verlag</general><general>Springer</general><general>Springer Nature B.V</general><scope>IQODW</scope><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>7QP</scope><scope>7QR</scope><scope>7TM</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</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>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope></search><sort><creationdate>20100901</creationdate><title>Two O-methyltransferases from Picea abies: characterization and molecular basis of different reactivity</title><author>Kim, Bong-Gyu ; Kim, Dae Hwan ; Sung, Su Hyun ; Kim, Dong-Eun ; Chong, Youhoon ; Ahn, Joong-Hoon</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c422t-1a9de5331a09a8f4b6417b4e66025a29e1dd9ca002be5376c21c62d81842c0483</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2010</creationdate><topic>Agriculture</topic><topic>Amino Acid Sequence</topic><topic>Amino acids</topic><topic>Binding sites</topic><topic>Biological and medical sciences</topic><topic>Biomedical and Life Sciences</topic><topic>Biosynthesis</topic><topic>Chromatography, High Pressure Liquid</topic><topic>Ecology</topic><topic>Enzymes</topic><topic>Flavonoids</topic><topic>Forestry</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Hydroxyls</topic><topic>Life Sciences</topic><topic>Lignin</topic><topic>Methyltransferases - chemistry</topic><topic>Methyltransferases - genetics</topic><topic>Methyltransferases - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Original Article</topic><topic>Phenols</topic><topic>Picea - enzymology</topic><topic>Picea - genetics</topic><topic>Plant Proteins - chemistry</topic><topic>Plant Proteins - genetics</topic><topic>Plant Proteins - metabolism</topic><topic>Plant Sciences</topic><topic>Protein Binding</topic><topic>Protein Structure, Secondary</topic><topic>Reaction products</topic><topic>Reactivity</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>Sequence Homology, Amino Acid</topic><topic>Substrate specificity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kim, Bong-Gyu</creatorcontrib><creatorcontrib>Kim, Dae Hwan</creatorcontrib><creatorcontrib>Sung, Su Hyun</creatorcontrib><creatorcontrib>Kim, Dong-Eun</creatorcontrib><creatorcontrib>Chong, Youhoon</creatorcontrib><creatorcontrib>Ahn, Joong-Hoon</creatorcontrib><collection>Pascal-Francis</collection><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>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Agricultural Science Collection</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>ProQuest Pharma Collection</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 One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Agricultural & Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</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 Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</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><jtitle>Planta</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kim, Bong-Gyu</au><au>Kim, Dae Hwan</au><au>Sung, Su Hyun</au><au>Kim, Dong-Eun</au><au>Chong, Youhoon</au><au>Ahn, Joong-Hoon</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Two O-methyltransferases from Picea abies: characterization and molecular basis of different reactivity</atitle><jtitle>Planta</jtitle><stitle>Planta</stitle><addtitle>Planta</addtitle><date>2010-09-01</date><risdate>2010</risdate><volume>232</volume><issue>4</issue><spage>837</spage><epage>844</epage><pages>837-844</pages><issn>0032-0935</issn><eissn>1432-2048</eissn><coden>PLANAB</coden><abstract>O-Methyltransferase (OMT) catalyzes the transfer of a methyl group from S-adenosyl methionine (SAM) to hydroxyl groups of methyl acceptors. Two OMTs, PaOMT2 and PaOMT3, from Picea abies showed 93.5% identity at the amino acid level. However, PaOMT3 catalyzed the reaction more efficiently than PaOMT2 with several phenolic compounds, including quercetin and caffeoyl-CoA. To determine the critical amino acids for the different reactivity of the two OMTs, site-directed mutagenesis was carried out. The amino acid proline at position 35 in PaOMT2 and leucine in PaOMT3 is a critical amino acid for their reactivity. Molecular modeling showed that the sequential change triggered by Leu35 resulted in a change in the size of the substrate binding pocket, which could account for the different catalytic reactivity of two OMTs.</abstract><cop>Berlin/Heidelberg</cop><pub>Springer-Verlag</pub><pmid>20628758</pmid><doi>10.1007/s00425-010-1223-9</doi><tpages>8</tpages></addata></record> |
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| subjects | Agriculture Amino Acid Sequence Amino acids Binding sites Biological and medical sciences Biomedical and Life Sciences Biosynthesis Chromatography, High Pressure Liquid Ecology Enzymes Flavonoids Forestry Fundamental and applied biological sciences. Psychology Hydroxyls Life Sciences Lignin Methyltransferases - chemistry Methyltransferases - genetics Methyltransferases - metabolism Molecular Sequence Data Original Article Phenols Picea - enzymology Picea - genetics Plant Proteins - chemistry Plant Proteins - genetics Plant Proteins - metabolism Plant Sciences Protein Binding Protein Structure, Secondary Reaction products Reactivity Reverse Transcriptase Polymerase Chain Reaction Sequence Homology, Amino Acid Substrate specificity |
| title | Two O-methyltransferases from Picea abies: characterization and molecular basis of different reactivity |
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