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- Paumann-Page, Martina, et al. Show all 9 Authors
- Biochimica et biophysica acta 2020 v.1868 no.1 pp. 140249
- basement membrane; blood coagulation factors; chemical bonding; collagen; crosslinking; cysteine; heme; humans; iron; leucine; models; oligomerization; peroxidase; proteolysis; small-angle X-ray scattering; structure-activity relationships; transmission electron microscopy
- ... Human peroxidasin 1 is a multidomain peroxidase situated in the basement membrane. The iron enzyme with covalently bound heme oxidizes bromide to hypobromous acid which facilitates the formation of distinct sulfilimine cross-links in the collagen IV network and therefore contributes to its mechanical stability. Additional to the catalytically active peroxidase domain peroxidasin comprises a leucin ...
- Paumann-Page, Martina, et al. Show all 5 Authors
- Archives of biochemistry and biophysics 2018 v.646 pp. 120-127
- acetaminophen; bromides; catalase; collagen; crosslinking; enzyme activity; enzyme inhibitors; epithelial cells; extracellular matrix; hydrazides; hydrogen peroxide; hydroxylysine; mass spectrometry; methionine; myeloperoxidase; oxidation; peroxidase; thiocyanates
- ... Peroxidasin is a heme peroxidase that catalyses the oxidation of bromide by hydrogen peroxide to form an essential sulfilimine cross-link between methionine and hydroxylysine residues in collagen IV. We investigated cross-linking by peroxidasin embedded in extracellular matrix isolated from cultured epithelial cells and its sensitivity to alternative substrates and peroxidase inhibitors. Peroxidas ...