{"title":"l-鼠李糖在大肠杆菌中的代谢","authors":"Hideo Sawada, Yasuyuki Takagi","doi":"10.1016/0926-6569(64)90265-2","DOIUrl":null,"url":null,"abstract":"<div><p>An enzyme which catalyzes the cleavage of <span>l</span>-rhamnulose <span>i</span>-phosphate has been purified about 15-fold from extracts of <span>l</span>-rhamnose-grown <em>Escherichia coli</em>. The products of the reaction were characterized as dihydroxyacetone phosphate and <span>l</span>-lactaldehyde. The enzyme has been named <span>l</span>-rhanulose-phosphate aldolase. It is distinct from muscle hexose-diphosphate aldolase.</p></div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 26-32"},"PeriodicalIF":0.0000,"publicationDate":"1964-10-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90265-2","citationCount":"33","resultStr":"{\"title\":\"The metabolism of l-rhamnose in Escherichia coli\",\"authors\":\"Hideo Sawada, Yasuyuki Takagi\",\"doi\":\"10.1016/0926-6569(64)90265-2\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>An enzyme which catalyzes the cleavage of <span>l</span>-rhamnulose <span>i</span>-phosphate has been purified about 15-fold from extracts of <span>l</span>-rhamnose-grown <em>Escherichia coli</em>. The products of the reaction were characterized as dihydroxyacetone phosphate and <span>l</span>-lactaldehyde. The enzyme has been named <span>l</span>-rhanulose-phosphate aldolase. It is distinct from muscle hexose-diphosphate aldolase.</p></div>\",\"PeriodicalId\":100170,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects\",\"volume\":\"92 1\",\"pages\":\"Pages 26-32\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1964-10-23\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0926-6569(64)90265-2\",\"citationCount\":\"33\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0926656964902652\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0926656964902652","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
An enzyme which catalyzes the cleavage of l-rhamnulose i-phosphate has been purified about 15-fold from extracts of l-rhamnose-grown Escherichia coli. The products of the reaction were characterized as dihydroxyacetone phosphate and l-lactaldehyde. The enzyme has been named l-rhanulose-phosphate aldolase. It is distinct from muscle hexose-diphosphate aldolase.
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