Post-translational modifications of chloroperoxidase from Caldariomyces fumago.

@article{Kenigsberg1987PosttranslationalMO,
  title={Post-translational modifications of chloroperoxidase from Caldariomyces fumago.},
  author={Paul Kenigsberg and G. H. Fang and Lowell P. Hager},
  journal={Archives of biochemistry and biophysics},
  year={1987},
  volume={254 2},
  pages={
          409-15
        }
}
  • Paul Kenigsberg, G. H. Fang, Lowell P. Hager
  • Published in
    Archives of biochemistry and…
    1987
  • Chemistry, Medicine
  • The secreted form of the halogenating glycoenzyme, chloroperoxidase, is processed from a precursor containing a 21-residue-long, moderately hydrophobic signal sequence, at an atypical Gln-Glu peptide bond. Following cleavage, the N-terminal glutamic acid readily cyclizes into pyroglutamic acid. Chloroperoxidase contains two high-mannose N-glycosylation sites, identified as Asn12 and Asn213. Other modifications include deamidation of residues Asn13, Asn198, and Gln183 into the corresponding… CONTINUE READING

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