尿苷二磷酸乙酰氨基葡萄糖的酶降解

T.N. Pattabiraman, T.N. Sekhara Varma, B.K. Bachhawat
{"title":"尿苷二磷酸乙酰氨基葡萄糖的酶降解","authors":"T.N. Pattabiraman,&nbsp;T.N. Sekhara Varma,&nbsp;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,&nbsp;T.N. Sekhara Varma,&nbsp;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}
引用次数: 21

摘要

尿苷二磷酸乙酰氨基葡萄糖被羊脑中的一种酶水解裂解。该反应的产物经鉴定为n -乙酰氨基葡萄糖-磷酸和UMP。负责这种降解的酶在大鼠的组织中广泛分布。ATP、UTP、ADP和n -乙酰氨基葡萄糖-磷酸是该酶的有效抑制剂。这种酶需要Co2+才能发挥最大的活性。它显示出较宽的最佳pH范围为8-9。该酶制剂对尿苷二磷酸葡萄糖和尿苷二磷酸葡萄糖醛酸的裂解程度低于尿苷二磷酸乙酰氨基葡萄糖。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信