{"title":"美洲杨羟基肉桂酰基辅酶a - Shikimate羟基肉桂酰基转移酶的研究","authors":"B. Kim, In-Ah Kim, Joong-Hoon Ahn","doi":"10.3839/JKSABC.2011.125","DOIUrl":null,"url":null,"abstract":"Hydroxycinnamoyl-coenzyme A shikimate/quinate hydroxycinnamoyltransferase (HCT), PeHCT was cloned from Populus euramericana. The predicted amino acid sequence revealed that PeHCT contained a conserved HXXXDG motif that was found in acyltransferase. The in vitro substrate was determined using recombinant PeHCT. The recombinant PeHCT showed substrate-specificity towards shikimic acid. In addition, PeHCT displayed higher expression in the stem than in the leaf, and its expression increased during the growth stage of the leaf. Results indicate PeHCT could be involved in lignin biosynthesis by formation of p-coumaroyl shikimate.","PeriodicalId":17424,"journal":{"name":"Journal of the Korean Society for Applied Biological Chemistry","volume":"46 1","pages":"817-821"},"PeriodicalIF":0.0000,"publicationDate":"2011-10-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"12","resultStr":"{\"title\":\"Characterization of hydroxycinnamoyl-coenzyme a Shikimate hydroxycinnamoyltransferase from Populus euramericana\",\"authors\":\"B. Kim, In-Ah Kim, Joong-Hoon Ahn\",\"doi\":\"10.3839/JKSABC.2011.125\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"Hydroxycinnamoyl-coenzyme A shikimate/quinate hydroxycinnamoyltransferase (HCT), PeHCT was cloned from Populus euramericana. The predicted amino acid sequence revealed that PeHCT contained a conserved HXXXDG motif that was found in acyltransferase. The in vitro substrate was determined using recombinant PeHCT. The recombinant PeHCT showed substrate-specificity towards shikimic acid. In addition, PeHCT displayed higher expression in the stem than in the leaf, and its expression increased during the growth stage of the leaf. Results indicate PeHCT could be involved in lignin biosynthesis by formation of p-coumaroyl shikimate.\",\"PeriodicalId\":17424,\"journal\":{\"name\":\"Journal of the Korean Society for Applied Biological Chemistry\",\"volume\":\"46 1\",\"pages\":\"817-821\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2011-10-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"12\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of the Korean Society for Applied Biological Chemistry\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.3839/JKSABC.2011.125\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of the Korean Society for Applied Biological Chemistry","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.3839/JKSABC.2011.125","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Characterization of hydroxycinnamoyl-coenzyme a Shikimate hydroxycinnamoyltransferase from Populus euramericana
Hydroxycinnamoyl-coenzyme A shikimate/quinate hydroxycinnamoyltransferase (HCT), PeHCT was cloned from Populus euramericana. The predicted amino acid sequence revealed that PeHCT contained a conserved HXXXDG motif that was found in acyltransferase. The in vitro substrate was determined using recombinant PeHCT. The recombinant PeHCT showed substrate-specificity towards shikimic acid. In addition, PeHCT displayed higher expression in the stem than in the leaf, and its expression increased during the growth stage of the leaf. Results indicate PeHCT could be involved in lignin biosynthesis by formation of p-coumaroyl shikimate.
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