Interkingdom pharmacology of Angiotensin-I converting enzyme inhibitor phosphonates produced by actinomycetes.

@article{Kramer2014InterkingdomPO,
  title={Interkingdom pharmacology of Angiotensin-I converting enzyme inhibitor phosphonates produced by actinomycetes.},
  author={Glenna J. Kramer and Akif Mohd and Sylva L. U. Schwager and Geoffrey Masuyer and K Ravi Acharya and Edward D. Sturrock and Brian O Bachmann},
  journal={ACS medicinal chemistry letters},
  year={2014},
  volume={5 4},
  pages={
          346-51
        }
}
The K-26 family of bacterial secondary metabolites are N-modified tripeptides terminated by an unusual phosphonate analog of tyrosine. These natural products, produced via three different actinomycetales, are potent inhibitors of human angiotensin-I converting enzyme (ACE). Herein we investigate the interkingdom pharmacology of the K-26 family by synthesizing these metabolites and assessing their potency as inhibitors of both the N-terminal and C-terminal domains of human ACE. In most cases… CONTINUE READING
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References

Publications referenced by this paper.
SHOWING 1-10 OF 31 REFERENCES

Catalytic properties of recombinant dipeptidyl carboxypeptidase from Escherichia coli : a comparative study with angiotensin I - converting enzyme

C. E. Cunha, F. Magliarelli Hde, +7 authors A. K. Carmona
  • Biol . Chem .
  • 2009