{"title":"二氢茉莉酸和脱落酸的体外糖基化研究","authors":"E. Schwarzkopf , O. Miersch","doi":"10.1016/S0015-3796(11)80263-5","DOIUrl":null,"url":null,"abstract":"<div><p>Cell-free extracts from cell suspension cultures of <em>Lycopersicon peruvianum</em> were found to catalyze the glucosylation of [U-<sup>3</sup>H]DJA and [2-<sup>14</sup>C]ABA in the presence of UDP-glucose. The products of enzymatic reactions were identified as glucosyl esters of DJA and ABA by means of TLC, HPLC and hydrolysis with cellulase. The two activities were not separated by ammonium sulfate fractionation and gel filtration, but the transferase activity of the enzyme was enriched toward radioactive DJA about 60-fold and toward radioactive ABA nearly 2-fold. A DJA metabolyzing enzyme was described for the first time and can be classified as UDP-glucose: DJA glucosyltransferase. In addition to the glucosyl esters of DJA and ABA the formation of further labelled products with still unknown structure were observed during the incubation.</p></div>","PeriodicalId":8798,"journal":{"name":"Biochemie und Physiologie der Pflanzen","volume":"188 1","pages":"Pages 57-65"},"PeriodicalIF":0.0000,"publicationDate":"1992-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/S0015-3796(11)80263-5","citationCount":"11","resultStr":"{\"title\":\"In vitro Glucosylation of Dihydrojasmonic Acid and Abscisic Acid\",\"authors\":\"E. Schwarzkopf , O. Miersch\",\"doi\":\"10.1016/S0015-3796(11)80263-5\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Cell-free extracts from cell suspension cultures of <em>Lycopersicon peruvianum</em> were found to catalyze the glucosylation of [U-<sup>3</sup>H]DJA and [2-<sup>14</sup>C]ABA in the presence of UDP-glucose. The products of enzymatic reactions were identified as glucosyl esters of DJA and ABA by means of TLC, HPLC and hydrolysis with cellulase. The two activities were not separated by ammonium sulfate fractionation and gel filtration, but the transferase activity of the enzyme was enriched toward radioactive DJA about 60-fold and toward radioactive ABA nearly 2-fold. A DJA metabolyzing enzyme was described for the first time and can be classified as UDP-glucose: DJA glucosyltransferase. In addition to the glucosyl esters of DJA and ABA the formation of further labelled products with still unknown structure were observed during the incubation.</p></div>\",\"PeriodicalId\":8798,\"journal\":{\"name\":\"Biochemie und Physiologie der Pflanzen\",\"volume\":\"188 1\",\"pages\":\"Pages 57-65\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1992-02-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/S0015-3796(11)80263-5\",\"citationCount\":\"11\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochemie und Physiologie der Pflanzen\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S0015379611802635\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochemie und Physiologie der Pflanzen","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S0015379611802635","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
In vitro Glucosylation of Dihydrojasmonic Acid and Abscisic Acid
Cell-free extracts from cell suspension cultures of Lycopersicon peruvianum were found to catalyze the glucosylation of [U-3H]DJA and [2-14C]ABA in the presence of UDP-glucose. The products of enzymatic reactions were identified as glucosyl esters of DJA and ABA by means of TLC, HPLC and hydrolysis with cellulase. The two activities were not separated by ammonium sulfate fractionation and gel filtration, but the transferase activity of the enzyme was enriched toward radioactive DJA about 60-fold and toward radioactive ABA nearly 2-fold. A DJA metabolyzing enzyme was described for the first time and can be classified as UDP-glucose: DJA glucosyltransferase. In addition to the glucosyl esters of DJA and ABA the formation of further labelled products with still unknown structure were observed during the incubation.
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