{"title":"大肠杆菌中膦酸盐生物降解基因。","authors":"B L Wanner","doi":"","DOIUrl":null,"url":null,"abstract":"<p><p>Escherichia coli has a carbon-phosphorus (C-P) lyase with a broad substrate specificity, whose synthesis is induced many hundred fold during phosphate (Pi) limitation. Fourteen genes for phosphonate metabolism comprise the phnC-to-phnP gene cluster: three gene products (PhnC, PhnD, and PhnE) comprise a binding protein-dependent phosphonate transporter, which also transports Pi and phosphate esters; two gene products (PhnF and PhnO) may have a role in gene regulation; and nine gene products (PhnG, PhnH, PhnI, PhnJ, PhnK, PhnL, PhnM, PhnN, and PhnP) may comprise a C-P lyase enzyme complex. Phosphonate biodegradation via a C-P lyase appears to be limited by the specificity of the PhnCDE transporter and not by the specificity of the C-P lyase. These interpretations are based on results from a combination of molecular genetic and molecular biological studies on phosphonate metabolism in E. coli.</p>","PeriodicalId":77373,"journal":{"name":"SAAS bulletin, biochemistry and biotechnology","volume":"5 ","pages":"1-6"},"PeriodicalIF":0.0000,"publicationDate":"1992-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Genes for phosphonate biodegradation in Escherichia coli.\",\"authors\":\"B L Wanner\",\"doi\":\"\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Escherichia coli has a carbon-phosphorus (C-P) lyase with a broad substrate specificity, whose synthesis is induced many hundred fold during phosphate (Pi) limitation. Fourteen genes for phosphonate metabolism comprise the phnC-to-phnP gene cluster: three gene products (PhnC, PhnD, and PhnE) comprise a binding protein-dependent phosphonate transporter, which also transports Pi and phosphate esters; two gene products (PhnF and PhnO) may have a role in gene regulation; and nine gene products (PhnG, PhnH, PhnI, PhnJ, PhnK, PhnL, PhnM, PhnN, and PhnP) may comprise a C-P lyase enzyme complex. Phosphonate biodegradation via a C-P lyase appears to be limited by the specificity of the PhnCDE transporter and not by the specificity of the C-P lyase. These interpretations are based on results from a combination of molecular genetic and molecular biological studies on phosphonate metabolism in E. coli.</p>\",\"PeriodicalId\":77373,\"journal\":{\"name\":\"SAAS bulletin, biochemistry and biotechnology\",\"volume\":\"5 \",\"pages\":\"1-6\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"1992-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"SAAS bulletin, biochemistry and biotechnology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"SAAS bulletin, biochemistry and biotechnology","FirstCategoryId":"1085","ListUrlMain":"","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
Genes for phosphonate biodegradation in Escherichia coli.
Escherichia coli has a carbon-phosphorus (C-P) lyase with a broad substrate specificity, whose synthesis is induced many hundred fold during phosphate (Pi) limitation. Fourteen genes for phosphonate metabolism comprise the phnC-to-phnP gene cluster: three gene products (PhnC, PhnD, and PhnE) comprise a binding protein-dependent phosphonate transporter, which also transports Pi and phosphate esters; two gene products (PhnF and PhnO) may have a role in gene regulation; and nine gene products (PhnG, PhnH, PhnI, PhnJ, PhnK, PhnL, PhnM, PhnN, and PhnP) may comprise a C-P lyase enzyme complex. Phosphonate biodegradation via a C-P lyase appears to be limited by the specificity of the PhnCDE transporter and not by the specificity of the C-P lyase. These interpretations are based on results from a combination of molecular genetic and molecular biological studies on phosphonate metabolism in E. coli.