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dc.creatorAmoutzias, G. D.en
dc.creatorVan De Peer, Y.en
dc.creatorMossialos, D.en
dc.date.accessioned2015-11-23T10:22:06Z
dc.date.available2015-11-23T10:22:06Z
dc.date.issued2008
dc.identifier10.2217/17460913.3.3.361
dc.identifier.issn1746-0913
dc.identifier.urihttp://hdl.handle.net/11615/25503
dc.description.abstractThe majority of nonribosomal peptide synthases and type I polyketide synthases are multimodular megasynthases of oligopeptide and polyketide secondary metabolites, respectively. Owing to their multimodular architecture, they synthesize their metabolites in assembly line logic. The ongoing genomic revolution together with the application of computational tools has provided the opportunity to mine the various genomes for these enzymes and identify those organisms that produce many oligopeptide and polyketide metabolites. In addition, scientists have started to comprehend the molecular mechanisms of megasynthase evolution, by duplication, recombination, point mutation and module skipping. This knowledge and computational analyses have been implemented towards predicting the specificity of these megasynthases and the structure of their end products. It is an exciting field, both for gaining deeper insight into their basic molecular mechanisms and exploiting them biotechnologically.en
dc.sourceFuture Microbiologyen
dc.source.uri<Go to ISI>://WOS:000256788600017
dc.subjectantibioticsen
dc.subjectbioinformaticsen
dc.subjectdistributionen
dc.subjectevolutionen
dc.subjectnonribosomalen
dc.subjectpeptide synthaseen
dc.subjectNRPSen
dc.subjectPKSen
dc.subjectpolyketide synthaseen
dc.subjectpredictionen
dc.subjectsiderophoresen
dc.subjectADENYLATION DOMAINSen
dc.subjectPHYLOGENETIC ANALYSISen
dc.subjectMULTIDOMAIN PROTEINSen
dc.subjectCONDENSATION DOMAINSen
dc.subjectSEQUENCE ALIGNMENTSen
dc.subjectMEDIATING DOMAINSen
dc.subjectGENE-CLUSTERen
dc.subjectSYNTHETASESen
dc.subjectBIOSYNTHESISen
dc.subjectSPECIFICITYen
dc.subjectMicrobiologyen
dc.titleEvolution and taxonomic distribution of nonribosomal peptide and polyketide synthasesen
dc.typejournalArticleen


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