{"title":"磷酸与ATP的反应:肌酸磷酸转移酶","authors":"Elizabeth James , J.F. Morrison","doi":"10.1016/0926-6593(66)90179-2","DOIUrl":null,"url":null,"abstract":"<div><p></p><ul><li><span>1.</span><span><p>1. A kinetic investigation has been made of the effect of various phosphagens on the reverse reaction catalysed by creatine kinase (ATP: creatine phosphotransferase, EC 2.7.3.2.).</p></span></li><li><span>2.</span><span><p>2. The results indicate that phosphoglycocyamine functions as a substrate of the enzyme with a maximum velocity only 0.18% of that obtained with phospho-creatine. Phosphotautocyamine and phosphoarginine were found not to act as substrates although they could combine with the enzyme as inhibitors.</p></span></li><li><span>3.</span><span><p>3. Values have been obtained for the tru kinetic constants associated with the reaction of each phosphagen with both the free enzyme and the enzyme-MgADP complex.</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":"1966-11-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6593(66)90179-2","citationCount":"10","resultStr":"{\"title\":\"The reaction of phosphages with ATP: Creatine phosphotransferase\",\"authors\":\"Elizabeth James , J.F. Morrison\",\"doi\":\"10.1016/0926-6593(66)90179-2\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p></p><ul><li><span>1.</span><span><p>1. A kinetic investigation has been made of the effect of various phosphagens on the reverse reaction catalysed by creatine kinase (ATP: creatine phosphotransferase, EC 2.7.3.2.).</p></span></li><li><span>2.</span><span><p>2. The results indicate that phosphoglycocyamine functions as a substrate of the enzyme with a maximum velocity only 0.18% of that obtained with phospho-creatine. Phosphotautocyamine and phosphoarginine were found not to act as substrates although they could combine with the enzyme as inhibitors.</p></span></li><li><span>3.</span><span><p>3. Values have been obtained for the tru kinetic constants associated with the reaction of each phosphagen with both the free enzyme and the enzyme-MgADP complex.</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\":\"1966-11-15\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0926-6593(66)90179-2\",\"citationCount\":\"10\",\"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/0926659366901792\",\"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/0926659366901792","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
The reaction of phosphages with ATP: Creatine phosphotransferase
1.
1. A kinetic investigation has been made of the effect of various phosphagens on the reverse reaction catalysed by creatine kinase (ATP: creatine phosphotransferase, EC 2.7.3.2.).
2.
2. The results indicate that phosphoglycocyamine functions as a substrate of the enzyme with a maximum velocity only 0.18% of that obtained with phospho-creatine. Phosphotautocyamine and phosphoarginine were found not to act as substrates although they could combine with the enzyme as inhibitors.
3.
3. Values have been obtained for the tru kinetic constants associated with the reaction of each phosphagen with both the free enzyme and the enzyme-MgADP complex.
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