{"title":"大肠杆菌的多核苷酸合成酶:一种具有多核苷酸磷酸化酶作为脱酶的酶复合体","authors":"Jannis G. Stavrianopoulos , Erwin Chargaff","doi":"10.1016/0005-2787(81)90040-X","DOIUrl":null,"url":null,"abstract":"<div><p>A previously described synthetase system of <em>Escherichia coli</em> that utilizes ribonucleoside triphosphates has been purified extensively and shown to consist of an apoenzyme and three protein factors. The apoenzyme itself was revealed to be polynucleotide phosphorylase. The conditions under which the latter — an enzyme incorporating nucleoside diphosphates — is converted to a system catalyzing the uptake of nucleoside triphosphates have been studied in detail with respect to primer requirements, the influence of triphosphates on diphosphate utilization and vice versa, and the possibly regulatory effect of the guanosine di- and triphosphates. The fully supplemented enzyme system (polynucleotide synthetase) incorporates GTP only in the presence of ATP, producing a polynucleotide with an A : G ratio near unity.</p></div>","PeriodicalId":100164,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis","volume":"655 3","pages":"Pages 307-322"},"PeriodicalIF":0.0000,"publicationDate":"1981-10-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2787(81)90040-X","citationCount":"0","resultStr":"{\"title\":\"Polynucleotide synthetase of E. coli: An enzyme complex having polynucleotide phosphorylase as apoenzyme\",\"authors\":\"Jannis G. Stavrianopoulos , Erwin Chargaff\",\"doi\":\"10.1016/0005-2787(81)90040-X\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>A previously described synthetase system of <em>Escherichia coli</em> that utilizes ribonucleoside triphosphates has been purified extensively and shown to consist of an apoenzyme and three protein factors. The apoenzyme itself was revealed to be polynucleotide phosphorylase. The conditions under which the latter — an enzyme incorporating nucleoside diphosphates — is converted to a system catalyzing the uptake of nucleoside triphosphates have been studied in detail with respect to primer requirements, the influence of triphosphates on diphosphate utilization and vice versa, and the possibly regulatory effect of the guanosine di- and triphosphates. The fully supplemented enzyme system (polynucleotide synthetase) incorporates GTP only in the presence of ATP, producing a polynucleotide with an A : G ratio near unity.</p></div>\",\"PeriodicalId\":100164,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis\",\"volume\":\"655 3\",\"pages\":\"Pages 307-322\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1981-10-27\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0005-2787(81)90040-X\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/000527878190040X\",\"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) - Nucleic Acids and Protein Synthesis","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/000527878190040X","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Polynucleotide synthetase of E. coli: An enzyme complex having polynucleotide phosphorylase as apoenzyme
A previously described synthetase system of Escherichia coli that utilizes ribonucleoside triphosphates has been purified extensively and shown to consist of an apoenzyme and three protein factors. The apoenzyme itself was revealed to be polynucleotide phosphorylase. The conditions under which the latter — an enzyme incorporating nucleoside diphosphates — is converted to a system catalyzing the uptake of nucleoside triphosphates have been studied in detail with respect to primer requirements, the influence of triphosphates on diphosphate utilization and vice versa, and the possibly regulatory effect of the guanosine di- and triphosphates. The fully supplemented enzyme system (polynucleotide synthetase) incorporates GTP only in the presence of ATP, producing a polynucleotide with an A : G ratio near unity.