Post-translational modifications of chloroperoxidase from Caldariomyces fumago.

@article{Kenigsberg1987PosttranslationalMO,
  title={Post-translational modifications of chloroperoxidase from Caldariomyces fumago.},
  author={P. Kenigsberg and G. Fang and L. Hager},
  journal={Archives of biochemistry and biophysics},
  year={1987},
  volume={254 2},
  pages={
          409-15
        }
}
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… Expand
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