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Enzymology
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- EnzymologyOpen Access
Multidomain Human Peroxidasin 1 Is a Highly Glycosylated and Stable Homotrimeric High Spin Ferric Peroxidase
Journal of Biological ChemistryVol. 290Issue 17p10876–10890Published online: February 24, 2015- Monika Soudi
- Martina Paumann-Page
- Cedric Delporte
- Katharina F. Pirker
- Marzia Bellei
- Eva Edenhofer
- and others
Cited in Scopus: 25Background: Human peroxidasin 1 (hsPxd01) mediates the formation of sulfilimine cross-links within the collagen IV scaffold of basement membranes.Results: Overexpressed hsPxd01 contains covalently linked heme catalytically active for production of hypobromous acid.Conclusion: hsPxd01 has peroxidase-like active site structure but restricted substrate accessibility.Significance: Architecture of hsPxd01 facilitates product release and its interactions with the physiological substrate collagen IV.