Title : Autocatalytic modification of the prosthetic heme of horseradish but not lactoperoxidase by thiocyanate oxidation products. A role for heme-protein covalent cross-linking.

Pub. Date : 2005 Nov 16

PMID : 16277530






3 Functional Relationships(s)
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Protein Name
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1 The mammalian peroxidases eosinophil peroxidase, lactoperoxidase (LPO), and myeloperoxidase oxidize thiocyanate to the antimicrobial agents hypothiocyanous acid (HOSCN) and (SCN)2 and are part of a defense system that protects the host from infections. thiocyanate lactoperoxidase Homo sapiens
2 The mammalian peroxidases eosinophil peroxidase, lactoperoxidase (LPO), and myeloperoxidase oxidize thiocyanate to the antimicrobial agents hypothiocyanous acid (HOSCN) and (SCN)2 and are part of a defense system that protects the host from infections. thiocyanate lactoperoxidase Homo sapiens
3 In contrast, oxidation by LPO of thiocyanate, the normal substrate of this enzyme, does not result in heme modification. thiocyanate lactoperoxidase Homo sapiens