Synthesis of beauvericin by a multifunctional enzyme.

@article{Peeters1988SynthesisOB,
  title={Synthesis of beauvericin by a multifunctional enzyme.},
  author={H. Peeters and R. Zocher and H. Kleinkauf},
  journal={The Journal of antibiotics},
  year={1988},
  volume={41 3},
  pages={
          352-9
        }
}
Beauvericin synthetase, a multifunctional enzyme catalyzing depsipeptide formation in Beauveria bassiana was purified to near homogeneity. The enzyme consists of a single polypeptide chain with a molecular mass of about 250 kdaltons. The mechanism of beauvericin formation is very similar to that of the cyclohexadepsipeptide enniatin. The constituents of the beauvericin molecule, L-phenylalanine and D-alpha-hydroxyisovaleric acid are activated as thioesters via the corresponding adenylates. N… Expand
Nonribosomal biosynthesis of peptide antibiotics.
Nonribosomal Peptide and Polyketide Biosynthesis
  • B. Evans
  • Chemistry
  • Methods in Molecular Biology
  • 2016
A nonribosomal system of peptide biosynthesis.
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Mechanism of depsipeptide formation catalyzed by enniatin synthetase.
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