The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli

Paolo Truffa-Bachi, Gisèle Le Bras, Georges N. Cohen
{"title":"The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli","authors":"Paolo Truffa-Bachi,&nbsp;Gisèle Le Bras,&nbsp;Georges N. Cohen","doi":"10.1016/0926-6593(66)90005-1","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. Homoserine dehydrogenase I (<span>l</span>-homoserine:NADP<sup>+</sup> oxidoreductase, EC 1.1.1.3) of <em>Escherichia coli</em> is inactivated with apparent first-order kinetics by exposure at pH 9 in Tris buffer. This inactivation is accompanied by desensitization of the enzyme towards threonine.</p></span></li><li><span>2.</span><span><p>2. <span>L</span>-Aspartate and ATP, the substrates of the associated activity, β-aspartokinase I (ATP:<span>L</span>-aspartate 4-phosphotransferase, EC 2.7.2.4) protect against the desensitization of homoserine dehydrogenase.</p></span></li></ul></div>","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":"128 3","pages":"Pages 450-453"},"PeriodicalIF":0.0000,"publicationDate":"1966-12-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90005-1","citationCount":"21","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0926659366900051","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 21

Abstract

  • 1.

    1. Homoserine dehydrogenase I (l-homoserine:NADP+ oxidoreductase, EC 1.1.1.3) of Escherichia coli is inactivated with apparent first-order kinetics by exposure at pH 9 in Tris buffer. This inactivation is accompanied by desensitization of the enzyme towards threonine.

  • 2.

    2. L-Aspartate and ATP, the substrates of the associated activity, β-aspartokinase I (ATP:L-aspartate 4-phosphotransferase, EC 2.7.2.4) protect against the desensitization of homoserine dehydrogenase.

大肠杆菌对苏氨酸敏感的同型丝氨酸脱氢酶和天冬氨酸激酶活性
1.1. 在pH为9的Tris缓冲液中,对大肠杆菌的同型丝氨酸脱氢酶I (l-homoserine:NADP+ oxidoreductase, EC 1.1.1.3)进行了一级动力学灭活。这种失活伴随着酶对苏氨酸的脱敏。l -天冬氨酸和ATP,相关活性的底物,β-天冬氨酸激酶I (ATP: l -天冬氨酸4-磷酸转移酶,EC 2.7.2.4)保护抵抗同型丝氨酸脱氢酶的脱敏。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
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