Post-translational modifications of chloroperoxidase from Caldariomyces fumago |
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| Authors: | P Kenigsberg G H Fang L P Hager |
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| Affiliation: | 1. Research School of Chemistry, Australian National University, Canberra, ACT 2601, Australia;2. Department of Biochemistry and Molecular Biology, Biomedicine Discovery Institute, Monash University, Clayton, Victoria 3800, Australia;3. Michael Smith Laboratories, University of British Columbia, Vancouver, British Columbia V6T 1Z2, Canada;1. Department of Psychiatry and the Semel Institute for Neuroscience and Behavior, David Geffen School of Medicine at UCLA, 635 Charles E. Young Drive South, Los Angeles, CA 90095, USA;2. Department of Bioengineering, UCLA, 410 Westwood Plaza, Los Angeles, CA 90095, USA;3. Department of Neurology, David Geffen School of Medicine at UCLA, 635 Charles E. Young Drive South, Los Angeles, CA 90095, USA;4. Department of Cell and Developmental Biology, Northwestern University, 303 E. Superior St. SQBRC 8-300, Chicago, IL 60611, USA;5. Department of Pathology and Laboratory Medicine, David Geffen School of Medicine at UCLA, 635 Charles E. Young Drive South, Los Angeles, CA 90095, USA;6. Voyager Therapeutics, 64 Sidney St., Cambridge, MA 02139, USA;7. Department of Neurosurgery, David Geffen School of Medicine at UCLA, 635 Charles E. Young Drive South, Los Angeles, CA 90095, USA;8. Center for Translational Neuromedicine, University of Rochester Medical Center and University of Copenhagen Faculty of Medical Sciences, 601 Elmwood Ave, Box 645, Rochester, NY 14642, USA;9. Research and Development Center for Precision Medicine, Tsukuba University, Tsukuba, Japan;10. Departments of Pediatrics and Pharmacology, David Geffen School of Medicine at UCLA, 635 Charles E. Young Drive South, Los Angeles, CA 90095, USA;1. BBSRC/EPSRC Synthetic Biology Research Centre, School of Life Sciences, Centre for Biomolecular Sciences, University of Nottingham, Nottingham, UK;2. Tan Tao University, School of Medicine, Tan Duc e-City, Duc Hoa, Long An, Vietnam;3. Université de Toulouse, INSA, UPS, INP, TBI, Toulouse, France;4. INRA, UMR792, Toulouse, France;5. CNRS, UMR5504, Toulouse, France;6. Metabolic Explorer, Biopôle Clermont-Limagne, Saint Beauzire, France;1. National and Local Joint Engineering Research Center for Biomanufacturing of Choral Chemicals, Zhejiang University of Technology, Hangzhou 310014, PR China;2. Key Laboratory of Bioorganic Synthesis of Zhejiang Province, College of Biotechnology and Bioengineering, Zhejiang University of Technology, Hangzhou 310014, PR China |
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| Abstract: | 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. |
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