R Pagani, R Leoncini, M Pizzichini, D Vannoni, A Tabucchi, E Marinello
{"title":"大鼠肝脏l -苏氨酸脱氨酶的性质。","authors":"R Pagani, R Leoncini, M Pizzichini, D Vannoni, A Tabucchi, E Marinello","doi":"10.1159/000474974","DOIUrl":null,"url":null,"abstract":"<p><p>We have studied several properties of rat liver L-threonine deaminase: (1) the affinity for the two substrates, L-serine and L-threonine; (2) the threonine/serine activity ratio which changes with increasing pH; (3) the activation, by pyridoxal 5'-phosphate which is linked to the nonprotonated form of the coenzyme and to at least an -SH group of the enzyme, and (4) the reactivation by pyridoxal 5'-phosphate and pyridoxamine 5'-phosphate after dissociation of the coenzyme. The mechanism of the reactivation by pyridoxamine 5'-phosphate is the most interesting problem opened by the present research.</p>","PeriodicalId":11854,"journal":{"name":"Enzyme & protein","volume":"48 2","pages":"90-7"},"PeriodicalIF":0.0000,"publicationDate":"1994-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1159/000474974","citationCount":"4","resultStr":"{\"title\":\"Properties of rat liver L-threonine deaminase.\",\"authors\":\"R Pagani, R Leoncini, M Pizzichini, D Vannoni, A Tabucchi, E Marinello\",\"doi\":\"10.1159/000474974\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>We have studied several properties of rat liver L-threonine deaminase: (1) the affinity for the two substrates, L-serine and L-threonine; (2) the threonine/serine activity ratio which changes with increasing pH; (3) the activation, by pyridoxal 5'-phosphate which is linked to the nonprotonated form of the coenzyme and to at least an -SH group of the enzyme, and (4) the reactivation by pyridoxal 5'-phosphate and pyridoxamine 5'-phosphate after dissociation of the coenzyme. The mechanism of the reactivation by pyridoxamine 5'-phosphate is the most interesting problem opened by the present research.</p>\",\"PeriodicalId\":11854,\"journal\":{\"name\":\"Enzyme & protein\",\"volume\":\"48 2\",\"pages\":\"90-7\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1994-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1159/000474974\",\"citationCount\":\"4\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Enzyme & protein\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1159/000474974\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Enzyme & protein","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1159/000474974","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
We have studied several properties of rat liver L-threonine deaminase: (1) the affinity for the two substrates, L-serine and L-threonine; (2) the threonine/serine activity ratio which changes with increasing pH; (3) the activation, by pyridoxal 5'-phosphate which is linked to the nonprotonated form of the coenzyme and to at least an -SH group of the enzyme, and (4) the reactivation by pyridoxal 5'-phosphate and pyridoxamine 5'-phosphate after dissociation of the coenzyme. The mechanism of the reactivation by pyridoxamine 5'-phosphate is the most interesting problem opened by the present research.
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