Heme peroxidase

Heme peroxidases are a superfamily of enzymes that utilize a heme cofactor to catalyze the oxidation of various substrates using hydrogen peroxide as the electron acceptor [1: https://www.uniprot.org]. In humans, prominent members include myeloperoxidase (MPO), which is vital for the innate immune response, and thyroid peroxidase (TPO), which is essential for the synthesis of thyroid hormones [2: https://pmc.ncbi.nlm.nih.gov/articles/PMC4112147/]. While these enzymes are necessary for normal physiology, their excessive activity can lead to oxidative stress and tissue damage, contributing to diseases such as atherosclerosis, neurodegeneration, and chronic inflammation [3: https://pubmed.ncbi.nlm.nih.gov/29107081/]. Consequently, they are significant therapeutic targets; for instance, thionamide drugs like methimazole inhibit TPO to treat hyperthyroidism, while MPO inhibitors like verdoperstat are being investigated for cardiovascular and neurodegenerative conditions [4: https://www.ncbi.nlm.nih.gov/books/NBK534833/]. The interaction between drugs and these enzymes typically involves binding to the heme group or the substrate-binding site, effectively halting the catalytic cycle and preventing the formation of reactive intermediates [5: https://pubchem.ncbi.nlm.nih.gov/compound/Verdoperstat].

Other names

Haem-containing peroxidase enzymesHemoprotein peroxidaseHeme-dependent peroxidasePeroxidase

Inhibition of the peroxidase catalytic cycle, typically by competing with substrates or binding to the heme iron, thereby preventing the oxidation of halides or organic molecules and the subsequent formation of reactive intermediates.