Expression of an active adenylate‐forming domain of peptide synthetases corresponding to acyl‐CoA‐synthetases

@article{Dieckmann1995ExpressionOA,
  title={Expression of an active adenylate‐forming domain of peptide synthetases corresponding to acyl‐CoA‐synthetases},
  author={R. Dieckmann and Y. O. Lee and H. van Liempt and H. von D{\"o}hren and H. Kleinkauf},
  journal={FEBS Letters},
  year={1995},
  volume={357}
}
Peptide synthetases and acyl‐CoA‐synthetases form acyl adenylates which are transferred to CoA or enzyme‐bound pantetheine. To verify the existence of an adenylate domain in peptide synthetases, a 60.8 kDa fragment of tyrocidine 1‐synthetase was constructed by a 1629 bp deletion, expressed in Escherichia coli, and characterized. The truncated multienzyme activated phenylalanine and substrate analogues with comparable kinetics as the over‐expressed synthetase, as judged by ATP‐[32P]PPi exchange… Expand
A nonribosomal system of peptide biosynthesis.
Substrate Specificity of Hybrid Modules from Peptide Synthetases*
Aminoacyl Adenylate Substrate Analogues for the Inhibition of Adenylation Domains of Nonribosomal Peptide Synthetases
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References

SHOWING 1-10 OF 36 REFERENCES
Nucleotide binding by multienzyme peptide synthetases.
Multidomain enzymes involved in peptide synthesis
...
1
2
3
4
...