{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,14]],"date-time":"2026-05-14T11:51:56Z","timestamp":1778759516680,"version":"3.51.4"},"reference-count":29,"publisher":"Wiley","issue":"3","license":[{"start":{"date-parts":[[2002,1,5]],"date-time":"2002-01-05T00:00:00Z","timestamp":1010188800000},"content-version":"vor","delay-in-days":1253,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["The Plant Journal"],"published-print":{"date-parts":[[1998,8]]},"abstract":"<jats:title>Summary<\/jats:title><jats:p> <jats:bold>cDNA clones encoding a novel 3\u2010ketoacyl\u2010ACP synthase (KAS) have been isolated from<\/jats:bold>\n          <jats:italic>\n            <jats:bold>Cuphea<\/jats:bold>\n          <\/jats:italic>\n          <jats:bold>. The amino acid sequence of this enzyme is different from the previously characterized classes of KASs, designated KAS I and III, and similar to those designated as KAS II. To define the acyl chain specificity of this enzyme, we generated transgenic<\/jats:bold>\n          <jats:italic>\n            <jats:bold>Brassica<\/jats:bold>\n          <\/jats:italic>\n          <jats:bold>plants over\u2010expressing the cDNA encoded protein in a seed specific manner. Expression of this enzyme in transgenic<\/jats:bold>\n          <jats:italic>\n            <jats:bold>Brassica<\/jats:bold>\n          <\/jats:italic>\n          <jats:bold>seeds which normally do not produce medium chain fatty acids does not result in any detectable modification of the fatty acid profile. However, co\u2010expression of the<\/jats:bold>\n          <jats:italic>\n            <jats:bold>Cuphea<\/jats:bold>\n          <\/jats:italic>\n          <jats:bold>KAS with medium chain specific thioesterases, capable of production of either 12:0 or 8:0\/10:0 fatty acids in seed oil, strongly enhances the levels of these medium chain fatty acids as compared with seed oil of plants expressing the thioesterases alone. By contrast, co\u2010expression of the<\/jats:bold>\n          <jats:italic>\n            <jats:bold>Cuphea<\/jats:bold>\n          <\/jats:italic>\n          <jats:bold>KAS along with an 18:0\/18:1\u2010ACP thioesterase does not result in any detectable modification of the fatty acids. These data indicate that the<\/jats:bold>\n          <jats:italic>\n            <jats:bold>Cuphea<\/jats:bold>\n          <\/jats:italic>\n          <jats:bold>KAS reported here has a different acyl\u2010chain specificity to the previously characterized KAS I, II and III. Therefore, we designate this enzyme KAS IV, a medium chain specific condensing enzyme.<\/jats:bold> <\/jats:p>","DOI":"10.1046\/j.1365-313x.1998.00218.x","type":"journal-article","created":{"date-parts":[[2003,3,12]],"date-time":"2003-03-12T21:54:14Z","timestamp":1047506054000},"page":"383-390","update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":65,"title":["<b>KAS IV: a 3\u2010ketoacyl\u2010ACP synthase from<\/b><i><b>Cuphea sp<\/b><\/i><b>. is a medium chain specific condensing enzyme<\/b>"],"prefix":"10.1111","volume":"15","author":[{"given":"Katayoon","family":"Dehesh","sequence":"first","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Patricia","family":"Edwards","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"JoAnne","family":"Fillatti","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Mary","family":"Slabaugh","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"James","family":"Byrne","sequence":"additional","affiliation":[],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"311","published-online":{"date-parts":[[2002,1,5]]},"reference":[{"key":"e_1_2_5_2_1","doi-asserted-by":"publisher","DOI":"10.1016\/0003-2697(86)90132-6"},{"key":"e_1_2_5_3_1","doi-asserted-by":"crossref","first-page":"20992","DOI":"10.1016\/S0021-9258(19)36787-0","article-title":"Purification and characterization of \u03b2\u2010ketoacyl\u2010 acyl carrier protein synthase III from spinach.","volume":"267","author":"Clough R.C.","year":"1992","journal-title":"J. Biol. Chem."},{"key":"e_1_2_5_4_1","doi-asserted-by":"publisher","DOI":"10.1104\/pp.110.1.203"},{"key":"e_1_2_5_5_1","doi-asserted-by":"publisher","DOI":"10.1002\/j.1460-2075.1992.tb05506.x"},{"key":"e_1_2_5_6_1","doi-asserted-by":"crossref","unstructured":"Dehesh K. Jones A. Knutzon D.S. Voelker T.A.1996bProduction of high levels of 8: 0 and 10 0 fatty acids in transgenic canola by overexpression ofCh FatB2 a thioesterase cDNA fromCuphea hookeriana.Plant J.9 167\u2013172.","DOI":"10.1046\/j.1365-313X.1996.09020167.x"},{"key":"e_1_2_5_7_1","doi-asserted-by":"publisher","DOI":"10.1105\/tpc.10.4.613"},{"key":"e_1_2_5_8_1","doi-asserted-by":"publisher","DOI":"10.1515\/znc-1993-7-815"},{"key":"e_1_2_5_9_1","unstructured":"Genez A. McCarter D. Nelsen J. Bleibaum J. Thompson G.A. Knauf V.C. Stalker D.1991Cloning and molecular characteization of \u03b2\u2010ketoacyl ACP synthase cDNAs from endosperm ofRicinus communis. Abstract presented at the Third International Congress on Plant and Molecular Biol. Tucson AZ."},{"key":"e_1_2_5_10_1","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.pp.39.060188.000533"},{"key":"e_1_2_5_11_1","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-313X.1998.00073.x"},{"key":"e_1_2_5_12_1","doi-asserted-by":"crossref","first-page":"7624","DOI":"10.1016\/S0021-9258(18)83280-X","article-title":"Acetoacetyl\u2010acyl carrier protein synthase, a target for the antibiotic thiolactomycin.","volume":"264","author":"Jackowski S.","year":"1987","journal-title":"J. Biol. Chem."},{"key":"e_1_2_5_13_1","doi-asserted-by":"publisher","DOI":"10.1104\/pp.90.1.41"},{"key":"e_1_2_5_14_1","doi-asserted-by":"crossref","first-page":"23999","DOI":"10.1016\/S0021-9258(18)35936-2","article-title":"Structure and expression of the Kas12 gene encoding a \u03b2\u2010ketoacyl\u2010 acyl carrier protein synthase I isozyme from barley.","volume":"267","author":"Kauppinen S.K.","year":"1992","journal-title":"J. Biol. Chem."},{"key":"e_1_2_5_15_1","doi-asserted-by":"publisher","DOI":"10.1017\/S0960258500000921"},{"key":"e_1_2_5_16_1","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-313X.1998.00066.x"},{"key":"e_1_2_5_17_1","doi-asserted-by":"publisher","DOI":"10.1007\/BF00018567"},{"key":"e_1_2_5_18_1","doi-asserted-by":"crossref","first-page":"1858","DOI":"10.1016\/S0021-9258(18)52372-3","article-title":"In vivo pools of free and acylated acyl carrier proteins in spinach.","volume":"266","author":"Post\u2010Beittenmiller D.","year":"1991","journal-title":"J. Biol. Chem."},{"key":"e_1_2_5_19_1","doi-asserted-by":"publisher","DOI":"10.1007\/BF00265588"},{"key":"e_1_2_5_20_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.79.19.5808"},{"key":"e_1_2_5_21_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.91.23.11027"},{"key":"e_1_2_5_22_1","doi-asserted-by":"publisher","DOI":"10.1046\/j.1365-313X.1998.00065.x"},{"key":"e_1_2_5_23_1","doi-asserted-by":"publisher","DOI":"10.1104\/pp.108.1.443"},{"key":"e_1_2_5_24_1","doi-asserted-by":"publisher","DOI":"10.1104\/pp.103.4.1361"},{"key":"e_1_2_5_25_1","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.76.9.4350"},{"key":"e_1_2_5_26_1","doi-asserted-by":"crossref","first-page":"6807","DOI":"10.1016\/S0021-9258(19)50498-7","article-title":"Isolation and characterization of the \u03b2\u2010ketoacyl\u2010acyl carrier protein synthase III gene (fabH) from Escherichia coli K\u201012.","volume":"267","author":"Tsay J.T.","year":"1992","journal-title":"J. Biol. Chem."},{"key":"e_1_2_5_27_1","first-page":"111","volume-title":"Genetic Engineering Volume 18 (Setlow, J.K., Ed.). 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