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Nonribosomal polypeptide synthesis

Lipmann, F. (1973) Nonribosomal polypeptide synthesis on polyenzyme templates. Acc. Chem. Res., 6, 361-367. [Pg.158]

Figure 7. General scheme of nonribosomal peptide synthesis (NRPS). Each NRPS module incorporates one amino acid into the growing peptide chain. The modules are composed of several domains Adenylation domain (red) is responsible for substrate selectivity, peptidyl carrier protein domain (orange) and condensation domain (green) work synergistically to form the peptide bond, and thioester domain (blue) which terminates the reaction, resulting in either a linear or cyclic polypeptide. Figure 7. General scheme of nonribosomal peptide synthesis (NRPS). Each NRPS module incorporates one amino acid into the growing peptide chain. The modules are composed of several domains Adenylation domain (red) is responsible for substrate selectivity, peptidyl carrier protein domain (orange) and condensation domain (green) work synergistically to form the peptide bond, and thioester domain (blue) which terminates the reaction, resulting in either a linear or cyclic polypeptide.
Elongation Factors Nonribosomal protein factors that are necessary participants in the chain-elongation cycle of polypeptide synthesis they interact with the ribosome-mRNA complex or with other major cycle participants. [Pg.889]


See other pages where Nonribosomal polypeptide synthesis is mentioned: [Pg.198]    [Pg.51]    [Pg.272]    [Pg.198]    [Pg.51]    [Pg.272]    [Pg.245]    [Pg.271]    [Pg.1722]    [Pg.438]    [Pg.809]   
See also in sourсe #XX -- [ Pg.53 ]




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