{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,25]],"date-time":"2026-09-25T10:25:26Z","timestamp":1790331926047,"version":"4.1.0"},"reference-count":36,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2018,6,8]],"date-time":"2018-06-08T00:00:00Z","timestamp":1528416000000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/501100000038","name":"Natural Sciences and Engineering Research Council of Canada","doi-asserted-by":"publisher","id":[{"id":"10.13039\/501100000038","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The Plant Journal"],"published-print":{"date-parts":[[2018,7]]},"abstract":"<jats:title>Summary<\/jats:title>\n                  <jats:p>\n                    Noscapine biosynthesis in opium poppy involves three characterized\n                    <jats:italic>O<\/jats:italic>\n                    \u2010methyltransferases (\n                    <jats:styled-content style=\"fixed-case\">OMT<\/jats:styled-content>\n                    s) and a fourth responsible for the 4\u02b9\u2010methoxyl on the phthalide isoquinoline scaffold. The first three enzymes are homodimers, whereas the latter is a heterodimer encoded by two linked genes (\n                    <jats:italic>\n                      <jats:styled-content style=\"fixed-case\">OMT<\/jats:styled-content>\n                      2\n                    <\/jats:italic>\n                    and\n                    <jats:italic>\n                      <jats:styled-content style=\"fixed-case\">OMT<\/jats:styled-content>\n                      3\n                    <\/jats:italic>\n                    ). Neither\n                    <jats:styled-content style=\"fixed-case\">OMT<\/jats:styled-content>\n                    2 nor\n                    <jats:styled-content style=\"fixed-case\">OMT<\/jats:styled-content>\n                    3 form stable homodimers, but yield a substrate\u2010specific heterodimer when their genes are co\u2010expressed in\n                    <jats:italic>Escherichia coli<\/jats:italic>\n                    . The only substrate, 4\u02b9\u2010\n                    <jats:italic>O<\/jats:italic>\n                    \u2010desmethyl\u20103\u2010\n                    <jats:italic>O\u2010<\/jats:italic>\n                    acetylpapaveroxine, is a\n                    <jats:italic>seco<\/jats:italic>\n                    \u2010berbine pathway intermediate that undergoes ester hydrolysis subsequent to 4\u02b9\u2010\n                    <jats:italic>O<\/jats:italic>\n                    \u2010methylation leading to the formation of narcotine hemiacetal. In the absence of 4\u02b9\u2010\n                    <jats:italic>O<\/jats:italic>\n                    \u2010methylation, a parallel pathway yields narcotoline hemiacetal. Dehydrogenation produces noscapine and narcotoline from the corresponding hemiacetals. Phthalide isoquinoline intermediates with a 4\u02b9\u2010hydroxyl (i.e. narcotoline and narcotoline hemiacetal), or the corresponding 1\u2010hydroxyl on protoberberine intermediates, were not accepted. Norcoclaurine 6\n                    <jats:styled-content style=\"fixed-case\">OMT<\/jats:styled-content>\n                    , which shares 81% amino acid sequence identity with\n                    <jats:styled-content style=\"fixed-case\">OMT<\/jats:styled-content>\n                    3, also formed a functionally similar heterodimer with\n                    <jats:styled-content style=\"fixed-case\">OMT<\/jats:styled-content>\n                    2. Suppression of\n                    <jats:italic>\n                      <jats:styled-content style=\"fixed-case\">OMT<\/jats:styled-content>\n                      2\n                    <\/jats:italic>\n                    transcript levels in opium poppy increased narcotoline accumulation, whereas reduced\n                    <jats:italic>\n                      <jats:styled-content style=\"fixed-case\">OMT<\/jats:styled-content>\n                      3\n                    <\/jats:italic>\n                    transcript abundance caused no detectable change in the alkaloid phenotype. Opium poppy chemotype Marianne accumulates high levels of narcotoline and showed no detectable\n                    <jats:styled-content style=\"fixed-case\">OMT<\/jats:styled-content>\n                    2:\n                    <jats:styled-content style=\"fixed-case\">OMT<\/jats:styled-content>\n                    3 activity. Compared with the active subunit from the Bea's Choice chemotype, Marianne\n                    <jats:styled-content style=\"fixed-case\">OMT<\/jats:styled-content>\n                    2 exhibited a single S122Y mutation in the dimerization domain that precluded heterodimer formation based on homology models. Both subunits contributed to the formation of the substrate\u2010binding domain, although site\u2010directed mutagenesis revealed\n                    <jats:styled-content style=\"fixed-case\">OMT<\/jats:styled-content>\n                    2 as the active subunit. The occurrence of physiologically relevant\n                    <jats:styled-content style=\"fixed-case\">OMT<\/jats:styled-content>\n                    heterodimers increases the catalytic diversity of enzymes derived from a smaller number of gene products.\n                  <\/jats:p>","DOI":"10.1111\/tpj.13947","type":"journal-article","created":{"date-parts":[[2018,5,3]],"date-time":"2018-05-03T18:48:38Z","timestamp":1525373318000},"page":"252-267","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":36,"title":["Heterodimeric\n                    <i>O<\/i>\n                    \u2010methyltransferases involved in the biosynthesis of noscapine in opium poppy"],"prefix":"10.1111","volume":"95","author":[{"given":"Myung R.","family":"Park","sequence":"first","affiliation":[{"name":"Department of Biological Sciences University of Calgary Calgary AB T2N 1N4 Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xue","family":"Chen","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences University of Calgary Calgary AB T2N 1N4 Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Dean E.","family":"Lang","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences University of Calgary Calgary AB T2N 1N4 Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Kenneth K.S.","family":"Ng","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences University of Calgary Calgary AB T2N 1N4 Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Peter J.","family":"Facchini","sequence":"additional","affiliation":[{"name":"Department of Biological Sciences University of Calgary Calgary AB T2N 1N4 Canada"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2018,6,8]]},"reference":[{"key":"e_1_2_9_2_1","doi-asserted-by":"publisher","DOI":"10.1104\/pp.15.01240"},{"key":"e_1_2_9_3_1","doi-asserted-by":"publisher","DOI":"10.1111\/tpj.12379"},{"key":"e_1_2_9_4_1","doi-asserted-by":"publisher","DOI":"10.1107\/S0907444909042073"},{"key":"e_1_2_9_5_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.phytochem.2014.09.008"},{"key":"e_1_2_9_6_1","doi-asserted-by":"publisher","DOI":"10.1104\/pp.112.194886"},{"key":"e_1_2_9_7_1","doi-asserted-by":"publisher","DOI":"10.1016\/j.febslet.2013.11.037"},{"key":"e_1_2_9_8_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M113.505099"},{"key":"e_1_2_9_9_1","doi-asserted-by":"publisher","DOI":"10.1038\/nchembio.1717"},{"key":"e_1_2_9_10_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-313X.2012.05084.x"},{"key":"e_1_2_9_11_1","doi-asserted-by":"publisher","DOI":"10.1007\/s11103-012-9913-2"},{"key":"e_1_2_9_12_1","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-313X.1999.00379.x"},{"key":"e_1_2_9_13_1","doi-asserted-by":"publisher","DOI":"10.1021\/np0496643"},{"key":"e_1_2_9_14_1","doi-asserted-by":"publisher","DOI":"10.1093\/pcp\/pct020"},{"key":"e_1_2_9_15_1","doi-asserted-by":"publisher","DOI":"10.1186\/s12870-015-0596-0"},{"key":"e_1_2_9_16_1","doi-asserted-by":"publisher","DOI":"10.1023\/A:1005939803300"},{"key":"e_1_2_9_17_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0031-9422(00)98100-7"},{"key":"e_1_2_9_18_1","first-page":"5","article-title":"SLIC: a method for sequence\u2010 and ligation\u2010independent cloning","volume":"852","author":"Li M.Z.","year":"2012","journal-title":"Methods Mol. Biol."},{"key":"e_1_2_9_19_1","doi-asserted-by":"publisher","DOI":"10.1038\/ncomms12137"},{"key":"e_1_2_9_20_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M611908200"},{"key":"e_1_2_9_21_1","doi-asserted-by":"publisher","DOI":"10.1039\/c2np20029e"},{"key":"e_1_2_9_22_1","doi-asserted-by":"publisher","DOI":"10.1006\/meth.2001.1262"},{"key":"e_1_2_9_23_1","doi-asserted-by":"publisher","DOI":"10.4067\/S0716-97602005000100010"},{"key":"e_1_2_9_24_1","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M002439200"},{"key":"e_1_2_9_25_1","doi-asserted-by":"publisher","DOI":"10.1046\/j.1432-1033.2002.03275.x"},{"key":"e_1_2_9_26_1","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-313X.2003.01928.x"},{"key":"e_1_2_9_27_1","doi-asserted-by":"publisher","DOI":"10.1111\/j.1365-313X.2009.03937.x"},{"key":"e_1_2_9_28_1","doi-asserted-by":"publisher","DOI":"10.1002\/med.21357"},{"key":"e_1_2_9_29_1","doi-asserted-by":"publisher","DOI":"10.1111\/tpj.13225"},{"key":"e_1_2_9_30_1","doi-asserted-by":"publisher","DOI":"10.1093\/nar\/gkp045"},{"key":"e_1_2_9_31_1","doi-asserted-by":"publisher","DOI":"10.1006\/jmbi.1993.1626"},{"key":"e_1_2_9_32_1","doi-asserted-by":"publisher","DOI":"10.1016\/S0968-0004(03)00090-2"},{"key":"e_1_2_9_33_1","doi-asserted-by":"publisher","DOI":"10.1038\/msb.2011.75"},{"key":"e_1_2_9_34_1","first-page":"29","article-title":"Molecular cloning and characterization of S\u2010adenosyl\u2010L\u2010methionine:scoulerine\u20109\u2010O\u2010methyltransferase from cultured cells of Coptis japonica","volume":"36","author":"Takeshita N.","year":"1995","journal-title":"Plant Cell Physiol."},{"key":"e_1_2_9_35_1","doi-asserted-by":"publisher","DOI":"10.1126\/science.1220757"},{"key":"e_1_2_9_36_1","doi-asserted-by":"publisher","DOI":"10.1007\/s00425-005-1550-4"},{"key":"e_1_2_9_37_1","doi-asserted-by":"publisher","DOI":"10.1038\/85029"}],"container-title":["The Plant Journal"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.wiley.com\/onlinelibrary\/tdm\/v1\/articles\/10.1111%2Ftpj.13947","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/pdf\/10.1111\/tpj.13947","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2023,9,18]],"date-time":"2023-09-18T09:11:53Z","timestamp":1695028313000},"score":1,"resource":{"primary":{"URL":"https:\/\/onlinelibrary.wiley.com\/doi\/10.1111\/tpj.13947"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2018,6,8]]},"references-count":36,"journal-issue":{"issue":"2","published-print":{"date-parts":[[2018,7]]}},"alternative-id":["10.1111\/tpj.13947"],"URL":"https:\/\/doi.org\/10.1111\/tpj.13947","archive":["Portico"],"relation":{},"ISSN":["0960-7412","1365-313X"],"issn-type":[{"value":"0960-7412","type":"print"},{"value":"1365-313X","type":"electronic"}],"subject":[],"published":{"date-parts":[[2018,6,8]]},"assertion":[{"value":"2017-12-24","order":0,"name":"received","label":"Received","group":{"name":"publication_history","label":"Publication History"}},{"value":"2018-04-13","order":1,"name":"accepted","label":"Accepted","group":{"name":"publication_history","label":"Publication History"}},{"value":"2018-06-08","order":2,"name":"published","label":"Published","group":{"name":"publication_history","label":"Publication History"}}]}}