{"title":"大肠杆菌β -酮酰基- acp合成酶I在不饱和脂肪酸合成中的作用。","authors":"M Siggaard-Andersen","doi":"10.1007/BF02983312","DOIUrl":null,"url":null,"abstract":"<p><p>Two activities were found in E. coli extracts which could complement unsaturated fatty acid synthesis of a cerulenin treated E. coli fatty acid synthetase. One of these is beta-ketoacyl-ACP synthase I, but it is not known whether the other activity represents the previously characterized beta-ketoacyl-ACP synthase II. A mutant strain exhibiting a temperature sensitive unsaturated fatty acid synthetic activity apparently lacked an active beta-ketoacyl-ACP synthase I.</p>","PeriodicalId":9616,"journal":{"name":"Carlsberg Research Communications","volume":"53 6","pages":"371-9"},"PeriodicalIF":0.0000,"publicationDate":"1988-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1007/BF02983312","citationCount":"8","resultStr":"{\"title\":\"Role of Escherichia coli beta-ketoacyl-ACP synthase I in unsaturated fatty acid synthesis.\",\"authors\":\"M Siggaard-Andersen\",\"doi\":\"10.1007/BF02983312\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Two activities were found in E. coli extracts which could complement unsaturated fatty acid synthesis of a cerulenin treated E. coli fatty acid synthetase. One of these is beta-ketoacyl-ACP synthase I, but it is not known whether the other activity represents the previously characterized beta-ketoacyl-ACP synthase II. A mutant strain exhibiting a temperature sensitive unsaturated fatty acid synthetic activity apparently lacked an active beta-ketoacyl-ACP synthase I.</p>\",\"PeriodicalId\":9616,\"journal\":{\"name\":\"Carlsberg Research Communications\",\"volume\":\"53 6\",\"pages\":\"371-9\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1988-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1007/BF02983312\",\"citationCount\":\"8\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Carlsberg Research Communications\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1007/BF02983312\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Carlsberg Research Communications","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1007/BF02983312","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Role of Escherichia coli beta-ketoacyl-ACP synthase I in unsaturated fatty acid synthesis.
Two activities were found in E. coli extracts which could complement unsaturated fatty acid synthesis of a cerulenin treated E. coli fatty acid synthetase. One of these is beta-ketoacyl-ACP synthase I, but it is not known whether the other activity represents the previously characterized beta-ketoacyl-ACP synthase II. A mutant strain exhibiting a temperature sensitive unsaturated fatty acid synthetic activity apparently lacked an active beta-ketoacyl-ACP synthase I.
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