peptide synthetase

Each nonribosomal peptide synthetase can synthesize only one type of peptide.

The order of modules and domains of a complete nonribosomal peptide synthetase is as follows:

This is done by tethering the amino acid to a peptidal carrier protein via a non-ribosomal peptide synthetase.

Ciclosporin is synthesized by a nonribosomal peptide synthetase, ciclosporin synthetase.

ACVS is an example of a nonribosomal peptide synthetase (NRPS).

The catalytic domains in modules one and three of the nonribosomal peptide synthetase assembly line select and activate (S)-4-hydroxyphenylglycine and 3,5-dihydroxyphenylglycine.

It consists of a central cyclic pentapeptide code assembled from nonribosomal peptide synthetase (NRPS).

The emetic toxin (cereulide) has been isolated and characterized; it is a small ring peptide synthesised nonribosomally by a peptide synthetase.

Echinomycin is a bis-intercalator peptide and is biosynthesized by a unique nonribosomal peptide synthetase (NRPs).

-Tryptophan is introduced by a nonribosomal peptide synthetase (NRPS) module and results in the central heterocyclic tetramic acid (2,4-pyrrolidindione).

To synthesize the peptide portion of Daptomycin, the mechanism of a non-ribosomal peptide synthetase (NRPS) is employed.

The biosynthesis of codinaeopsin is manufactured by a polyketide synthase- nonribosomal peptide synthetase (PKS-NRPS) hybrid.

Its biosynthesis is via an enzymatic assembly consisting of 3 peptide synthetase proteins, TycA, TycB, and TycC, which contain 10 modules.

Ybt synthesis occurs by a mixed nonribosomal peptide synthetase (NRPS)/polyketide synthase (PKS) mechanism.

Key genes and enzymes for ergot alkaloid biosynthesis have been identified in epichloae and include dmaW, encoding dimethylallyl-tryptophan synthase and lpsA, a non-ribosomal peptide synthetase.

This antibiotic is synthesized by a linear nonribosomal peptide synthetase, surfactin synthetase, and has, in solution, a characteristic "horse saddle" conformation that explains its large spectrum of biological activity.

The biosynthesis of the rapamycin core is accomplished by a type I polyketide synthase (PKS) in conjunction with a nonribosomal peptide synthetase (NRPS).

The non-ribosomal peptide synthetase (NRPS) responsible for the synthesis of Daptomycin is encoded by three overlapping genes, dptA, dptBC and dptD.

Biosynthesis is initiated by the coupling of decanoic acid to the N-terminal tryptophan, followed by the coupling of the remaining amino acids by nonribosomal peptide synthetase (NRPS) mechanisms.

Therefore, it seems more likely that the activation of anthranilate could be a step in the formation of a siderophore or antibiotic compound that is assembled by a nonribosomal peptide synthetase mechanism (see Quadri et al .

The polyketide backbone was synthesized by type I polyketide synthase (PKS) and the thiazole ring was derived from a cysteine incorporated by a nonribosomal peptide synthetase (NRPS).

The peptide/polyketide/peptide backbone of the bleomycin aglycon is assembled by the bleomycin megasynthetase, which is made of both nonribosomal peptide synthetase (NRPS) and polyketide synthase (PKS) modules.

Lysergic acid (LA) is the substrate of lysergyl peptide synthetase, a nonribosomal peptide synthetase, which covalently links LA to the amino acids, L-alanine, L-proline, and L-phenylalanine.

They are produced by nonribosomal peptide synthetase systems in Gram-positive bacteria such as Paenibacillus polymyxa and are selectively toxic for Gram-negative bacteria due to their specificity for the lipopolysaccharide molecule that exists within many Gram-negative outer membranes.