Evolution of Novel O-methyltransferases from the Vanilla planifolia Caffeic Acid O-methyltransferase
The biosynthesis of many plant secondary compounds involves the methylation of one or more hydroxyl groups, catalyzed by O-methyltransferases (OMTs). Here, we report the characterization of two OMTs, Van OMT-2 and Van OMT-3, from the orchid Vanilla planifolia Andrews. These enzymes catalyze the meth...
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| Veröffentlicht in: | Plant molecular biology 2006-06, Vol.61 (3), p.537-552 |
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| creator | Li, H.M Rotter, D Hartman, T.G Pak, F.E Havkin-Frenkel, D Belanger, F.C |
| description | The biosynthesis of many plant secondary compounds involves the methylation of one or more hydroxyl groups, catalyzed by O-methyltransferases (OMTs). Here, we report the characterization of two OMTs, Van OMT-2 and Van OMT-3, from the orchid Vanilla planifolia Andrews. These enzymes catalyze the methylation of a single outer hydroxyl group in substrates possessing a 1,2,3-trihydroxybenzene moiety, such as methyl gallate and myricetin. This is a substrate requirement not previously reported for any OMTs. Based on sequence analysis these enzymes are most similar to caffeic acid O-methyltransferases (COMTs), but they have negligible activity with typical COMT substrates. Seven of 12 conserved substrate-binding residues in COMTs are altered in Van OMT-2 and Van OMT-3. Phylogenetic analysis of the sequences suggests that Van OMT-2 and Van OMT-3 evolved from the V. planifolia COMT. These V. planifolia OMTs are new instances of COMT-like enzymes with novel substrate preferences. |
| doi_str_mv | 10.1007/s11103-006-0029-4 |
| format | Article |
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Here, we report the characterization of two OMTs, Van OMT-2 and Van OMT-3, from the orchid Vanilla planifolia Andrews. These enzymes catalyze the methylation of a single outer hydroxyl group in substrates possessing a 1,2,3-trihydroxybenzene moiety, such as methyl gallate and myricetin. This is a substrate requirement not previously reported for any OMTs. Based on sequence analysis these enzymes are most similar to caffeic acid O-methyltransferases (COMTs), but they have negligible activity with typical COMT substrates. Seven of 12 conserved substrate-binding residues in COMTs are altered in Van OMT-2 and Van OMT-3. Phylogenetic analysis of the sequences suggests that Van OMT-2 and Van OMT-3 evolved from the V. planifolia COMT. These V. planifolia OMTs are new instances of COMT-like enzymes with novel substrate preferences.</description><identifier>ISSN: 0167-4412</identifier><identifier>EISSN: 1573-5028</identifier><identifier>DOI: 10.1007/s11103-006-0029-4</identifier><identifier>PMID: 16830185</identifier><language>eng</language><publisher>Netherlands: Springer Nature B.V</publisher><subject>Amino Acid Sequence ; amino acid sequences ; Biosynthesis ; caffeic acid O-methyltransferase ; Catalysis ; Cloning, Molecular ; complementary DNA ; DNA, Complementary - analysis ; enzyme activity ; enzyme substrates ; Enzymes ; Escherichia coli - genetics ; Evolution, Molecular ; Methylation ; methyltransferases ; Methyltransferases - chemistry ; Methyltransferases - genetics ; Methyltransferases - metabolism ; Molecular Sequence Data ; nucleotide sequences ; Phylogeny ; Plant biology ; Plant Proteins - chemistry ; Plant Proteins - genetics ; Plant Proteins - metabolism ; Sequence Alignment ; Substrate Specificity ; Substrates ; Vanilla - enzymology ; Vanilla - genetics ; Vanilla planifolia</subject><ispartof>Plant molecular biology, 2006-06, Vol.61 (3), p.537-552</ispartof><rights>Springer 2006</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c416t-3dc1388d44a1cdda395d09c17b780e19113646b517ae9ae879f9a1b7607098723</citedby><cites>FETCH-LOGICAL-c416t-3dc1388d44a1cdda395d09c17b780e19113646b517ae9ae879f9a1b7607098723</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16830185$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Li, H.M</creatorcontrib><creatorcontrib>Rotter, D</creatorcontrib><creatorcontrib>Hartman, T.G</creatorcontrib><creatorcontrib>Pak, F.E</creatorcontrib><creatorcontrib>Havkin-Frenkel, D</creatorcontrib><creatorcontrib>Belanger, F.C</creatorcontrib><title>Evolution of Novel O-methyltransferases from the Vanilla planifolia Caffeic Acid O-methyltransferase</title><title>Plant molecular biology</title><addtitle>Plant Mol Biol</addtitle><description>The biosynthesis of many plant secondary compounds involves the methylation of one or more hydroxyl groups, catalyzed by O-methyltransferases (OMTs). Here, we report the characterization of two OMTs, Van OMT-2 and Van OMT-3, from the orchid Vanilla planifolia Andrews. These enzymes catalyze the methylation of a single outer hydroxyl group in substrates possessing a 1,2,3-trihydroxybenzene moiety, such as methyl gallate and myricetin. This is a substrate requirement not previously reported for any OMTs. Based on sequence analysis these enzymes are most similar to caffeic acid O-methyltransferases (COMTs), but they have negligible activity with typical COMT substrates. Seven of 12 conserved substrate-binding residues in COMTs are altered in Van OMT-2 and Van OMT-3. Phylogenetic analysis of the sequences suggests that Van OMT-2 and Van OMT-3 evolved from the V. planifolia COMT. These V. planifolia OMTs are new instances of COMT-like enzymes with novel substrate preferences.</description><subject>Amino Acid Sequence</subject><subject>amino acid sequences</subject><subject>Biosynthesis</subject><subject>caffeic acid O-methyltransferase</subject><subject>Catalysis</subject><subject>Cloning, Molecular</subject><subject>complementary DNA</subject><subject>DNA, Complementary - analysis</subject><subject>enzyme activity</subject><subject>enzyme substrates</subject><subject>Enzymes</subject><subject>Escherichia coli - genetics</subject><subject>Evolution, Molecular</subject><subject>Methylation</subject><subject>methyltransferases</subject><subject>Methyltransferases - chemistry</subject><subject>Methyltransferases - genetics</subject><subject>Methyltransferases - metabolism</subject><subject>Molecular Sequence Data</subject><subject>nucleotide sequences</subject><subject>Phylogeny</subject><subject>Plant biology</subject><subject>Plant Proteins - chemistry</subject><subject>Plant Proteins - genetics</subject><subject>Plant Proteins - metabolism</subject><subject>Sequence Alignment</subject><subject>Substrate Specificity</subject><subject>Substrates</subject><subject>Vanilla - enzymology</subject><subject>Vanilla - genetics</subject><subject>Vanilla planifolia</subject><issn>0167-4412</issn><issn>1573-5028</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>BENPR</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNptkEtLxDAQx4Mouj4-gBcNHrxVZ5o0j6MsvkD04OMasm2ilbZZk1bw2xvZBUE8DDMwv_8w_Ag5RDhDAHmeEBFYASBylbrgG2SGlWRFBaXaJDNAIQvOsdwhuym9A-QUE9tkB4VigKqakebyM3TT2IaBBk_vw6fr6EPRu_HtqxujHZJ30SaXqI-hp-Oboy92aLvO0mWXBx-61tK59d61Nb2o2-a_9D7Z8rZL7mDd98jz1eXT_Ka4e7i-nV_cFTVHMRasqZEp1XBusW4ay3TVgK5RLqQChxqRCS4WFUrrtHVKaq8tLqQACVrJku2R09XdZQwfk0uj6dtUu_zt4MKUjFCilJKLDJ78Ad_DFIf8m5FCIxdCVBnCFVTHkFJ03ixj29v4ZRDMj3-z8m-yf_Pj3_CcOVofnha9a34Ta-EZOF4B3gZjX2ObzPNjCZi3oDQHxr4BFlGJKg</recordid><startdate>20060601</startdate><enddate>20060601</enddate><creator>Li, H.M</creator><creator>Rotter, D</creator><creator>Hartman, T.G</creator><creator>Pak, F.E</creator><creator>Havkin-Frenkel, D</creator><creator>Belanger, F.C</creator><general>Springer Nature B.V</general><scope>FBQ</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>7TM</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>8G5</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</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>GUQSH</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2O</scope><scope>M7P</scope><scope>MBDVC</scope><scope>P64</scope><scope>PHGZM</scope><scope>PHGZT</scope><scope>PJZUB</scope><scope>PKEHL</scope><scope>PPXIY</scope><scope>PQEST</scope><scope>PQGLB</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20060601</creationdate><title>Evolution of Novel O-methyltransferases from the Vanilla planifolia Caffeic Acid O-methyltransferase</title><author>Li, H.M ; Rotter, D ; Hartman, T.G ; Pak, F.E ; Havkin-Frenkel, D ; Belanger, F.C</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c416t-3dc1388d44a1cdda395d09c17b780e19113646b517ae9ae879f9a1b7607098723</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Amino Acid Sequence</topic><topic>amino acid sequences</topic><topic>Biosynthesis</topic><topic>caffeic acid O-methyltransferase</topic><topic>Catalysis</topic><topic>Cloning, Molecular</topic><topic>complementary DNA</topic><topic>DNA, Complementary - analysis</topic><topic>enzyme activity</topic><topic>enzyme substrates</topic><topic>Enzymes</topic><topic>Escherichia coli - genetics</topic><topic>Evolution, Molecular</topic><topic>Methylation</topic><topic>methyltransferases</topic><topic>Methyltransferases - chemistry</topic><topic>Methyltransferases - genetics</topic><topic>Methyltransferases - metabolism</topic><topic>Molecular Sequence Data</topic><topic>nucleotide sequences</topic><topic>Phylogeny</topic><topic>Plant biology</topic><topic>Plant Proteins - chemistry</topic><topic>Plant Proteins - genetics</topic><topic>Plant Proteins - metabolism</topic><topic>Sequence Alignment</topic><topic>Substrate Specificity</topic><topic>Substrates</topic><topic>Vanilla - enzymology</topic><topic>Vanilla - genetics</topic><topic>Vanilla planifolia</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Li, H.M</creatorcontrib><creatorcontrib>Rotter, D</creatorcontrib><creatorcontrib>Hartman, T.G</creatorcontrib><creatorcontrib>Pak, F.E</creatorcontrib><creatorcontrib>Havkin-Frenkel, D</creatorcontrib><creatorcontrib>Belanger, F.C</creatorcontrib><collection>AGRIS</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>Nucleic Acids 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>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>Research Library (Alumni Edition)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</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 (ProQuest)</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>Research Library Prep</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>Research Library</collection><collection>Biological Science Database</collection><collection>Research Library (Corporate)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest Central (New)</collection><collection>ProQuest One Academic (New)</collection><collection>ProQuest Health & Medical Research Collection</collection><collection>ProQuest One Academic Middle East (New)</collection><collection>ProQuest One Health & Nursing</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Applied & Life Sciences</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Plant molecular biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Li, H.M</au><au>Rotter, D</au><au>Hartman, T.G</au><au>Pak, F.E</au><au>Havkin-Frenkel, D</au><au>Belanger, F.C</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Evolution of Novel O-methyltransferases from the Vanilla planifolia Caffeic Acid O-methyltransferase</atitle><jtitle>Plant molecular biology</jtitle><addtitle>Plant Mol Biol</addtitle><date>2006-06-01</date><risdate>2006</risdate><volume>61</volume><issue>3</issue><spage>537</spage><epage>552</epage><pages>537-552</pages><issn>0167-4412</issn><eissn>1573-5028</eissn><abstract>The biosynthesis of many plant secondary compounds involves the methylation of one or more hydroxyl groups, catalyzed by O-methyltransferases (OMTs). Here, we report the characterization of two OMTs, Van OMT-2 and Van OMT-3, from the orchid Vanilla planifolia Andrews. These enzymes catalyze the methylation of a single outer hydroxyl group in substrates possessing a 1,2,3-trihydroxybenzene moiety, such as methyl gallate and myricetin. This is a substrate requirement not previously reported for any OMTs. Based on sequence analysis these enzymes are most similar to caffeic acid O-methyltransferases (COMTs), but they have negligible activity with typical COMT substrates. Seven of 12 conserved substrate-binding residues in COMTs are altered in Van OMT-2 and Van OMT-3. Phylogenetic analysis of the sequences suggests that Van OMT-2 and Van OMT-3 evolved from the V. planifolia COMT. These V. planifolia OMTs are new instances of COMT-like enzymes with novel substrate preferences.</abstract><cop>Netherlands</cop><pub>Springer Nature B.V</pub><pmid>16830185</pmid><doi>10.1007/s11103-006-0029-4</doi><tpages>16</tpages></addata></record> |
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| ispartof | Plant molecular biology, 2006-06, Vol.61 (3), p.537-552 |
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| subjects | Amino Acid Sequence amino acid sequences Biosynthesis caffeic acid O-methyltransferase Catalysis Cloning, Molecular complementary DNA DNA, Complementary - analysis enzyme activity enzyme substrates Enzymes Escherichia coli - genetics Evolution, Molecular Methylation methyltransferases Methyltransferases - chemistry Methyltransferases - genetics Methyltransferases - metabolism Molecular Sequence Data nucleotide sequences Phylogeny Plant biology Plant Proteins - chemistry Plant Proteins - genetics Plant Proteins - metabolism Sequence Alignment Substrate Specificity Substrates Vanilla - enzymology Vanilla - genetics Vanilla planifolia |
| title | Evolution of Novel O-methyltransferases from the Vanilla planifolia Caffeic Acid O-methyltransferase |
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