{"title":"尿苷二磷酸乙酰氨基葡萄糖的酶降解","authors":"T.N. Pattabiraman, T.N. Sekhara Varma, B.K. Bachhawat","doi":"10.1016/0926-6526(64)90053-9","DOIUrl":null,"url":null,"abstract":"<div><p>Uridine diphosphoacetylglucosamine is shown to undergo a hydrolytic cleavage by an enzyme present in sheep brain. The products of the reaction are identified as <em>N</em>-<em>acetylglucosamine</em><span>i</span>-phosphate and UMP. The enzyme responsible for this degradation has a wide distribution in the tissues of the rat. ATP, UTP, ADP and <em>N</em>-<em>acetylglucosamine</em><span>i</span>-phosphate act as powerful inhibitors of this enzyme. The enzyme requires Co<sup>2+</sup> for its maximal activity. It shows a broad optimal range of pH from 8–9. The enzyme preparation cleaves uridine diphosphoglucose and uridine diphosphoglucuronic acid to lesser extents than uridine diphosphoacetylglucosamine.</p></div>","PeriodicalId":100172,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Mucoproteins and Mucopolysaccharides","volume":"83 1","pages":"Pages 74-83"},"PeriodicalIF":0.0000,"publicationDate":"1964-03-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6526(64)90053-9","citationCount":"21","resultStr":"{\"title\":\"Enzymic degradation of uridine diphosphoacetylglucosamine\",\"authors\":\"T.N. Pattabiraman, T.N. Sekhara Varma, B.K. Bachhawat\",\"doi\":\"10.1016/0926-6526(64)90053-9\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Uridine diphosphoacetylglucosamine is shown to undergo a hydrolytic cleavage by an enzyme present in sheep brain. The products of the reaction are identified as <em>N</em>-<em>acetylglucosamine</em><span>i</span>-phosphate and UMP. The enzyme responsible for this degradation has a wide distribution in the tissues of the rat. ATP, UTP, ADP and <em>N</em>-<em>acetylglucosamine</em><span>i</span>-phosphate act as powerful inhibitors of this enzyme. The enzyme requires Co<sup>2+</sup> for its maximal activity. It shows a broad optimal range of pH from 8–9. The enzyme preparation cleaves uridine diphosphoglucose and uridine diphosphoglucuronic acid to lesser extents than uridine diphosphoacetylglucosamine.</p></div>\",\"PeriodicalId\":100172,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Specialized Section on Mucoproteins and Mucopolysaccharides\",\"volume\":\"83 1\",\"pages\":\"Pages 74-83\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1964-03-02\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0926-6526(64)90053-9\",\"citationCount\":\"21\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et Biophysica Acta (BBA) - Specialized Section on Mucoproteins and Mucopolysaccharides\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0926652664900539\",\"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 Mucoproteins and Mucopolysaccharides","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0926652664900539","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Enzymic degradation of uridine diphosphoacetylglucosamine
Uridine diphosphoacetylglucosamine is shown to undergo a hydrolytic cleavage by an enzyme present in sheep brain. The products of the reaction are identified as N-acetylglucosaminei-phosphate and UMP. The enzyme responsible for this degradation has a wide distribution in the tissues of the rat. ATP, UTP, ADP and N-acetylglucosaminei-phosphate act as powerful inhibitors of this enzyme. The enzyme requires Co2+ for its maximal activity. It shows a broad optimal range of pH from 8–9. The enzyme preparation cleaves uridine diphosphoglucose and uridine diphosphoglucuronic acid to lesser extents than uridine diphosphoacetylglucosamine.