{"title":"核黄素的生物合成","authors":"Peter Nielsen, Adelbert Bacher","doi":"10.1016/0005-2744(81)90044-9","DOIUrl":null,"url":null,"abstract":"<div><p>The 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5′-phosphate deaminase was partially purified from cell extracts of <em>Candida guilliermondii</em> ATCC 9058. The enzyme requires Mg<sup>2+</sup> for activity. Maximal activity was observed at pH 7.3. The enzyme converts its substrate, 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5′-phosphate, to 2,5-diamino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5′-phosphate. This labile compound was treated with diacetyl and the resulting 6,7-dimethyl-8-ribityllumazine 5′-phosphate was identified by comparison with a synthetic sample.</p></div>","PeriodicalId":100159,"journal":{"name":"Biochimica et Biophysica Acta (BBA) - Enzymology","volume":"662 2","pages":"Pages 312-317"},"PeriodicalIF":0.0000,"publicationDate":"1981-12-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/0005-2744(81)90044-9","citationCount":"38","resultStr":"{\"title\":\"Biosynthesis of riboflavin\",\"authors\":\"Peter Nielsen, Adelbert Bacher\",\"doi\":\"10.1016/0005-2744(81)90044-9\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>The 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5′-phosphate deaminase was partially purified from cell extracts of <em>Candida guilliermondii</em> ATCC 9058. The enzyme requires Mg<sup>2+</sup> for activity. Maximal activity was observed at pH 7.3. The enzyme converts its substrate, 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5′-phosphate, to 2,5-diamino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5′-phosphate. This labile compound was treated with diacetyl and the resulting 6,7-dimethyl-8-ribityllumazine 5′-phosphate was identified by comparison with a synthetic sample.</p></div>\",\"PeriodicalId\":100159,\"journal\":{\"name\":\"Biochimica et Biophysica Acta (BBA) - Enzymology\",\"volume\":\"662 2\",\"pages\":\"Pages 312-317\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1981-12-15\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/0005-2744(81)90044-9\",\"citationCount\":\"38\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Biochimica et Biophysica Acta (BBA) - Enzymology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/0005274481900449\",\"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","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/0005274481900449","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
The 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5′-phosphate deaminase was partially purified from cell extracts of Candida guilliermondii ATCC 9058. The enzyme requires Mg2+ for activity. Maximal activity was observed at pH 7.3. The enzyme converts its substrate, 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5′-phosphate, to 2,5-diamino-6-ribitylamino-2,4(1H,3H)-pyrimidinedione 5′-phosphate. This labile compound was treated with diacetyl and the resulting 6,7-dimethyl-8-ribityllumazine 5′-phosphate was identified by comparison with a synthetic sample.
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