Post-translational modifications of chloroperoxidase from Caldariomyces fumago.
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 acids. Finally, structural arguments suggest that Cys87 may be the axial heme ligand in the active site of chloroperoxidase.
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000378:metabolism; D001216:Asparagine / Q000378:metabolism; D002711:Chloride Peroxidase / Q000302:isolation & purification / Q000378:metabolism*; D002851:Chromatography, High Pressure Liquid; D005971:Glutamates / Q000378:metabolism; D018698:Glutamic Acid; D005973:Glutamine / Q000378:metabolism; D006031:Glycosylation; D007527:Isoenzymes / Q000302:isolation & purification / Q000378:metabolism*; D003904:Mitosporic Fungi / Q000201:enzymology*; D010446:Peptide Fragments; D010544:Peroxidases / Q000378:metabolism*; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational; D021382:Protein Sorting Signals
D000596:Amino Acids; D005971:Glutamates; D007527:Isoenzymes; D010446:Peptide Fragments; D021382:Protein Sorting Signals; D005973:Glutamine; D018698:Glutamic Acid; D001216:Asparagine; D010544:Peroxidases; D002711:Chloride Peroxidase