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- W2169595886 endingPage "848" @default.
- W2169595886 startingPage "826" @default.
- W2169595886 abstract "The multienzyme polyketide synthases (PKSs), nonribosomal polypeptide synthetases (NRPSs), and their hybrids are responsible for the construction in bacteria of numerous natural products of clinical value. These systems generate high structural complexity by using a simple biosynthetic logic—that of the assembly line. Each of the individual steps in building the metabolites is designated to an independently folded domain within gigantic polypeptides. The domains are clustered into functional modules, and the modules are strung out along the proteins in the order in which they act. Every metabolite results, therefore, from the successive action of up to 100 individual catalysts. Despite the conceptual simplicity of this division-of-labor organization, we are only beginning to decipher the molecular details of the numerous protein–protein interactions that support assembly-line biosynthesis, and which are critical to attempts to re-engineer these systems as a tool in drug discovery. This review aims to summarize the state of knowledge about several aspects of protein–protein interactions, including current architectural models for PKS and NRPS systems, the central role of carrier proteins, and the structural basis for intersubunit recognition." @default.
- W2169595886 created "2016-06-24" @default.
- W2169595886 creator A5067406705 @default.
- W2169595886 creator A5077818118 @default.
- W2169595886 date "2008-04-14" @default.
- W2169595886 modified "2023-10-18" @default.
- W2169595886 title "Protein–Protein Interactions in Multienzyme Megasynthetases" @default.
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