Big Chemical Encyclopedia

Chemical substances, components, reactions, process design ...

Articles Figures Tables About

Peptide biosynthesis, non-ribosomal

In marked contrast to the ribosomal biosynthesis of peptides and proteins where a biological production line interprets the genetic code of mRNA, many natural peptides are known to be synthesized by a [Pg.535]

A typical module consists of an adenylation (A) domain, a peptidyl carrier protein (PCP) domain, and a condensation (C) or elongation domain. The A domain activates a specific amino acid as an [Pg.535]

Nucleophilic attack by the amino group of the neighbouring aminoacyl thioester is catalysed by the C domain, and this results in amide (peptide) bond formation. Enzyme-controlled biosynthesis in this manner is a feature of many microbial peptides, especially those containing unusual amino acids not encoded by DNA and where post-translational modification (see Section 13.1) is unlikely. [Pg.536]

As well as activating the amino acids and catalysing formation of the peptide linkages, the enzyme may possess other domains that are responsible for epimerizing L-amino acids to o-amino acids, [Pg.536]

Many medicinally useful peptides have cyclic structures. Cyclization may result if the amino acids at the two termini of a linear peptide link up to form another peptide bond. Alternatively, ring formation can very often be the resnlt of ester or amide linkages that utilize side-chain functionalities (CO2H, NH2, OH) in the constituent amino acids. [Pg.536]


The amino acid components of proteins have the L conhguration (see Section 3.4.10), but many peptides are known that contain one or more D-amino acids in their stmctures. o-Amino acids are not encoded by DNA, and peptides containing them are produced by what is termed non-ribosomal peptide biosynthesis (see Section 13.5.2). o-Amino acids generally arise by epimerization of L-amino acids (see Box 10.10). All the protein L-amino acids have the S conhguration, except for glycine, which is not chiral, and L-methionine which is R, a consequence of the priority mles for systematic descriptors of conhguration (see Section 3.4.10). [Pg.499]

ACV is produced by the modular system for non-ribosomal peptide biosynthesis. The amino acid precursors are L-a-aminoadipic acid (an unusual amino acid derived by modification of L-lysine), L-cysteine, and L-valine during tripeptide formation, the L-valine is epimerized to o-valine (see Box 10.10). [Pg.537]

T Stachelhaus, HD Mootz, V Bergendahl, MA Marahiel. Peptide bond formation in non-ribosomal peptide biosynthesis catalytic role of the condensation domain. J Biol Chem 273 22773-22781, 1998. [Pg.36]

NRPS (non-ribosomal peptide synthetase) genes. For further information on non-ribosomal peptide biosynthesis, see Schwarzer, Finking, and Marahiel (2003), Dorrestein and KeUeher (2006) and Wenzel et al. (2006). [Pg.849]

Bacitracin biosynthesis requires a non-ribosomal peptide synthetase with three major protein components, BacABC. This synthetase has a modular structure. There are associated regulatory and transport systems. Biosynthesis of bacitracin has been engineered in the surrogate host, B. subtilis, by genetic techniques. A strain, B. subtilis KE 350, expresses the entire 49-kb bacitracin... [Pg.678]

Recent studies on the mechanism of biosynthesis of cyclic lipopeptide antibiotics have proved that these are systematically synthesized by the multifunctional proteins, non-ribosomal peptide synthetase (NRPS). [Pg.693]

Unlike primary metabolites, the genes that regulate the formation of the enzymes of seeondary metaboUte biosynthesis are often clustered. In several eases the loei of these genes have been determined. This has considerable sig-nifieanee in the control of secondary metabolite biosynthesis. The genes that eode for several important polyketide pathways such as those leading to the aflatoxins and the statins have been identified. Similar work has also been reported for penicillin biosynthesis and some non-ribosomal peptides as well as terpenoid pathways such as that leading to the gibberellins. [Pg.31]

Fig. 5.2 Organization of polyketide synthases (PKSs). (A) The type I erythromycin PKS (DEBS) which catalyzes the biosynthesis of 6-dEB. The PKS consists of three polypeptides, DEBSl, DEBS2, and DEBS3, each possessing two modules. (B) The type I epothilone PKS consists of six polypeptides EpoA, EpoB [a non-ribosomal peptide synthase (NRPS)], EpoC, EpoD (possessing four modules), EpoE (possessing two modules), and EpoF. (C) The type II actinorhodin PKS con-... Fig. 5.2 Organization of polyketide synthases (PKSs). (A) The type I erythromycin PKS (DEBS) which catalyzes the biosynthesis of 6-dEB. The PKS consists of three polypeptides, DEBSl, DEBS2, and DEBS3, each possessing two modules. (B) The type I epothilone PKS consists of six polypeptides EpoA, EpoB [a non-ribosomal peptide synthase (NRPS)], EpoC, EpoD (possessing four modules), EpoE (possessing two modules), and EpoF. (C) The type II actinorhodin PKS con-...
U. Keller, F. Schauwecker, Combinatorial biosynthesis of non-ribosomal peptides, Comb. Chem. [Pg.534]

Tlie sequential reactions in elongating acyl transfers in the synthesis of polyketide natural products and non-ribosomal peptide antibiotics such as erythromycin, rapamycin, epotliilone, lovastatin, penicillins, cyclosporin and vancomycin resemble molecular solid-state assembly lines. Such multimodular enzymes may be utilized in combinatorial biosynthesis by way of reprogramming for the manufacture of unnaUiral analogs of natural products. [Pg.219]

Staunton J, Wilkinson B (2001). Combinatorial biosynthesis of polyketides and non-ribosomal peptides. Curr. Opin. Chem. Biol. 5 159-164. [Pg.45]


See other pages where Peptide biosynthesis, non-ribosomal is mentioned: [Pg.282]    [Pg.533]    [Pg.535]    [Pg.591]    [Pg.85]    [Pg.85]    [Pg.85]    [Pg.239]    [Pg.282]    [Pg.533]    [Pg.535]    [Pg.591]    [Pg.85]    [Pg.85]    [Pg.85]    [Pg.239]    [Pg.212]    [Pg.104]    [Pg.535]    [Pg.46]    [Pg.137]    [Pg.402]    [Pg.79]    [Pg.64]    [Pg.424]    [Pg.228]    [Pg.300]    [Pg.446]    [Pg.131]    [Pg.77]    [Pg.255]    [Pg.108]    [Pg.151]   
See also in sourсe #XX -- [ Pg.535 ]

See also in sourсe #XX -- [ Pg.37 , Pg.189 ]




SEARCH



Peptide biosynthesis

Ribosomal peptide

Ribosomal peptide biosynthesis

© 2024 chempedia.info