Paolo Truffa-Bachi, Gérard Le Bras, Georges N. Cohen
{"title":"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","authors":"Paolo Truffa-Bachi, Gérard Le Bras, Georges N. Cohen","doi":"10.1016/0926-6593(66)90004-X","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 in two steps by <span><math><mtext>p-</mtext><mtext>mercuribenzoic</mtext></math></span> acid (PMB). The first inactivation step is accompanied by desensitization of the enzyme activity towards its allosteric effector, <span>L</span>-threonine. The desensitized dehydrogenase activity is protected against further action of PMB by its own substrates and by the substrates of the associated activity, aspartokinase I (ATP:<span>L</span>-aspartate 4-phosphotransferase, EC 2.7.2.4).</p></span></li><li><span>2.</span><span><p>2. ATP and aspartate, the substrates of the kinase reaction induce conformational changes in the part of the complex enzyme molecule responsible for the dehydrogenase atalytic activity.</p></span></li></ul></div>","PeriodicalId":100160,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation","volume":null,"pages":null},"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)90004-X","citationCount":"9","resultStr":"{\"title\":\"The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli\",\"authors\":\"Paolo Truffa-Bachi, Gérard Le Bras, Georges N. Cohen\",\"doi\":\"10.1016/0926-6593(66)90004-X\",\"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 in two steps by <span><math><mtext>p-</mtext><mtext>mercuribenzoic</mtext></math></span> acid (PMB). The first inactivation step is accompanied by desensitization of the enzyme activity towards its allosteric effector, <span>L</span>-threonine. The desensitized dehydrogenase activity is protected against further action of PMB by its own substrates and by the substrates of the associated activity, aspartokinase I (ATP:<span>L</span>-aspartate 4-phosphotransferase, EC 2.7.2.4).</p></span></li><li><span>2.</span><span><p>2. ATP and aspartate, the substrates of the kinase reaction induce conformational changes in the part of the complex enzyme molecule responsible for the dehydrogenase atalytic activity.</p></span></li></ul></div>\",\"PeriodicalId\":100160,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Enzymology and Biological Oxidation\",\"volume\":null,\"pages\":null},\"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)90004-X\",\"citationCount\":\"9\",\"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/092665936690004X\",\"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) - Enzymology and Biological Oxidation","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/092665936690004X","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
The threonine-sensitive homoserine dehydrogenase and aspartokinase activities of Escherichia coli
1.
1. Homoserine dehydrogenase I (L-homoserine: NADP+ oxidoreductase, EC 1.1.1.3) of Escherichia coli is inactivated in two steps by acid (PMB). The first inactivation step is accompanied by desensitization of the enzyme activity towards its allosteric effector, L-threonine. The desensitized dehydrogenase activity is protected against further action of PMB by its own substrates and by the substrates of the associated activity, aspartokinase I (ATP:L-aspartate 4-phosphotransferase, EC 2.7.2.4).
2.
2. ATP and aspartate, the substrates of the kinase reaction induce conformational changes in the part of the complex enzyme molecule responsible for the dehydrogenase atalytic activity.
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