Glaci T. Zancan, Eduardo F. Recondo, Luis F. Leloir
{"title":"二磷酸腺苷磷酸甘油酸的酶解磷酸化","authors":"Glaci T. Zancan, Eduardo F. Recondo, Luis F. Leloir","doi":"10.1016/0926-6569(64)90276-7","DOIUrl":null,"url":null,"abstract":"<div><p>An enzyme from muscle which acts on adenosine diphosphate phosphoglyceric acid and leads to the hydrolysis of the phosphate group at the 2-position of the glyceric acid moiety has been studied. The enzyme is strongly stimulated by inorgamoc pyrophosphate. This action is very specific. The enzyme also acts on 2,3-diphosphoglycerate.</p></div>","PeriodicalId":100170,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects","volume":"92 1","pages":"Pages 125-131"},"PeriodicalIF":0.0000,"publicationDate":"1964-10-23","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0926-6569(64)90276-7","citationCount":"10","resultStr":"{\"title\":\"Enzymid dephosphorylation of adenosine diphosphate phosphoglyceric acid\",\"authors\":\"Glaci T. Zancan, Eduardo F. Recondo, Luis F. Leloir\",\"doi\":\"10.1016/0926-6569(64)90276-7\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>An enzyme from muscle which acts on adenosine diphosphate phosphoglyceric acid and leads to the hydrolysis of the phosphate group at the 2-position of the glyceric acid moiety has been studied. The enzyme is strongly stimulated by inorgamoc pyrophosphate. This action is very specific. The enzyme also acts on 2,3-diphosphoglycerate.</p></div>\",\"PeriodicalId\":100170,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects\",\"volume\":\"92 1\",\"pages\":\"Pages 125-131\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1964-10-23\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0926-6569(64)90276-7\",\"citationCount\":\"10\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0926656964902767\",\"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 Enzymological Subjects","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0926656964902767","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Enzymid dephosphorylation of adenosine diphosphate phosphoglyceric acid
An enzyme from muscle which acts on adenosine diphosphate phosphoglyceric acid and leads to the hydrolysis of the phosphate group at the 2-position of the glyceric acid moiety has been studied. The enzyme is strongly stimulated by inorgamoc pyrophosphate. This action is very specific. The enzyme also acts on 2,3-diphosphoglycerate.