{"title":"The metabolism of l-rhamnose in escherichia coli","authors":"Yasuyuki Takagi , Hideo Sawada","doi":"10.1016/0926-6569(64)90263-9","DOIUrl":null,"url":null,"abstract":"<div><p><span>l</span>-Rhamnose isomearse (<span>l</span>-rhamnose ketol-isomerase) has been purified about 50-fold from extracts of <em>Escherichia coli</em>. THe enzyme appears to be an SH enzyme, and catalyzes the reversible reaction <span>l</span>-rhamnose ⇆ <span>l</span>-rhamnulose. The enzyme was activated by the addition of manganous ions. At equilibrium about 60% of the total methylpentose was present as <span>l</span>-rhamnulose.</p><p>The enzyme was specific for <span>l</span>-rhamnose and <span>l</span>-rhamnulose; no other sugars were found to react.</p></div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 10-17"},"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)90263-9","citationCount":"53","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/0926656964902639","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 53
Abstract
l-Rhamnose isomearse (l-rhamnose ketol-isomerase) has been purified about 50-fold from extracts of Escherichia coli. THe enzyme appears to be an SH enzyme, and catalyzes the reversible reaction l-rhamnose ⇆ l-rhamnulose. The enzyme was activated by the addition of manganous ions. At equilibrium about 60% of the total methylpentose was present as l-rhamnulose.
The enzyme was specific for l-rhamnose and l-rhamnulose; no other sugars were found to react.
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