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Polypeptide, nonribosomal

Kleinkauf, H., and H. Dohren, Nonribosomal polypeptide formation on multifunctional proteins. Trends Biochem. Sci. 8 281-283, 1983. [Pg.766]

DE Cane. Introduction polyketide and nonribosomal polypeptide biosynthesis. From Collie to Coli. Chem Rev 97 2463-2464, 1997. [Pg.465]

Cane, D. E., ed. (1997). Polyketide and nonribosomal polypeptide biosynthesis. Chemical Reviews, 97, 2463-706 (includes 13 papers on the topic). [Pg.195]

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

There is no rigid scheme for classifying natural products—their immense diversity in structure, function, and biosynthesis is too great to allow them to fit neatly into a few simple categories. In practice, however, workers in the field often speak of five main classes of natural products terpenoids and steroids, fatty acid-derived substances and polyketides, alkaloids, nonribosomal polypeptides, and enzyme cofactors. [Pg.1016]

Nonribosomal polypeptides are peptide-like compounds that are biosynthesized from amino acids by a multifunctional enzyme complex without direct RNA transcription. The penicillins are good examples, but their chemistry is a hit complicated and weTl not discuss their biosynthesis. [Pg.1017]

Hamada, T, Matsunaga, S Fujiwara, M Fujita, K Hirota, H Schmudd, R., Grinthert, P and Firsetani, N. (2010) Solution structure of polytheonamide B, a highly cytotoxic, nonribosomal polypeptide from marine sponge. /. Am. Chem, Soc, 132, 12941-12945. [Pg.1008]

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 Polypeptide, nonribosomal is mentioned: [Pg.198]    [Pg.1202]    [Pg.51]    [Pg.271]    [Pg.272]    [Pg.198]    [Pg.1202]    [Pg.51]    [Pg.271]    [Pg.272]    [Pg.159]    [Pg.1722]    [Pg.17]    [Pg.17]    [Pg.159]    [Pg.159]    [Pg.438]    [Pg.809]    [Pg.788]    [Pg.236]    [Pg.245]   
See also in sourсe #XX -- [ Pg.1017 ]




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