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Enzymology
2 Results
- EnzymologyOpen Access
Pre-steady-state Kinetics Reveal the Substrate Specificity and Mechanism of Halide Oxidation of Truncated Human Peroxidasin 1
Journal of Biological ChemistryVol. 292Issue 11p4583–4592Published online: January 31, 2017- Martina Paumann-Page
- Romy-Sophie Katz
- Marzia Bellei
- Irene Schwartz
- Eva Edenhofer
- Benjamin Sevcnikar
- and others
Cited in Scopus: 33Human peroxidasin 1 is a homotrimeric multidomain peroxidase that is secreted to the extracellular matrix. The heme enzyme was shown to release hypobromous acid that mediates the formation of specific covalent sulfilimine bonds to reinforce collagen IV in basement membranes. Maturation by proteolytic cleavage is known to activate the enzyme. Here, we present the first multimixing stopped-flow study on a fully functional truncated variant of human peroxidasin 1 comprising four immunoglobulin-like domains and the catalytically active peroxidase domain. - 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: 24Background: 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.