{"title":"l-鼠李糖激酶的纯化及性质研究","authors":"T.H. Chiu, David Sidney Feingold","doi":"10.1016/0926-6569(64)90009-4","DOIUrl":null,"url":null,"abstract":"<div><p><span>l</span>-Rhamnulokinase (ATP:<span>l</span>-rhamnulose phosphotransferase, EC 2.7.1.5.) has been purified 34-fold from extracts of <em>Escherichia coli</em> K40. The purified enzyme catalyzes the phosphorylation of <span>l</span>-rhamnulose, but not of <span>l</span>-rhamnose, in the presence of Mg<sup>2+</sup> and adenosine 5′-triphosphate. Uridine triphosphate, cytidine 5′-triphosphate, guanosine 5′-triphosphate, and thymidine triphosphate also can act as phosphoryl donors, but less well than adenosine 5′-triphosphate.</p><p>The product of the phosphorylation of <span>l</span>-rhamnulose by the enzyme has been isolated and characterized by periodic acid oxidation studies as <span>l</span>-rhamnulose <span>i</span>-phosphate.</p></div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 3","pages":"Pages 489-497"},"PeriodicalIF":0.0000,"publicationDate":"1964-12-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90009-4","citationCount":"28","resultStr":"{\"title\":\"The purification and properties of l-rhamnulokinase\",\"authors\":\"T.H. Chiu, David Sidney Feingold\",\"doi\":\"10.1016/0926-6569(64)90009-4\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p><span>l</span>-Rhamnulokinase (ATP:<span>l</span>-rhamnulose phosphotransferase, EC 2.7.1.5.) has been purified 34-fold from extracts of <em>Escherichia coli</em> K40. The purified enzyme catalyzes the phosphorylation of <span>l</span>-rhamnulose, but not of <span>l</span>-rhamnose, in the presence of Mg<sup>2+</sup> and adenosine 5′-triphosphate. Uridine triphosphate, cytidine 5′-triphosphate, guanosine 5′-triphosphate, and thymidine triphosphate also can act as phosphoryl donors, but less well than adenosine 5′-triphosphate.</p><p>The product of the phosphorylation of <span>l</span>-rhamnulose by the enzyme has been isolated and characterized by periodic acid oxidation studies as <span>l</span>-rhamnulose <span>i</span>-phosphate.</p></div>\",\"PeriodicalId\":100170,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects\",\"volume\":\"92 3\",\"pages\":\"Pages 489-497\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1964-12-23\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0926-6569(64)90009-4\",\"citationCount\":\"28\",\"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/0926656964900094\",\"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/0926656964900094","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
The purification and properties of l-rhamnulokinase
l-Rhamnulokinase (ATP:l-rhamnulose phosphotransferase, EC 2.7.1.5.) has been purified 34-fold from extracts of Escherichia coli K40. The purified enzyme catalyzes the phosphorylation of l-rhamnulose, but not of l-rhamnose, in the presence of Mg2+ and adenosine 5′-triphosphate. Uridine triphosphate, cytidine 5′-triphosphate, guanosine 5′-triphosphate, and thymidine triphosphate also can act as phosphoryl donors, but less well than adenosine 5′-triphosphate.
The product of the phosphorylation of l-rhamnulose by the enzyme has been isolated and characterized by periodic acid oxidation studies as l-rhamnulose i-phosphate.
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