PON1 (paraoxonase 1)

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PON1 (paraoxonase 1), a member of paraoxonase gene family, is a calcium-dependent esterase that binds closely to HDL in blood circulation. Its relative molecular weight is between 43~45kDa. It was originally named because of its role in the hydrolysis of paraoxon in organophosphorus pesticides. It was found that the free sulfhydryl group of cysteine (Cys284) at position 284 of PON1 may be the key site of its antioxidant enzyme activity. It has been found that PON1 has a variety of biological activities in vivo, such as lactone enzyme, aromatic esterase, phospholipase A2 and so on, which can act on different substrates, decompose hydrogen peroxide, phospholipid oxide, lysophosphatidylcholine, oxidized free fatty acid, platelet activating factor, homocysteine thiolactone and so on. It is considered that PON1 is one of the most important antioxidant enzymes binding to HDL in circulation and an important structural basis for maintaining the structural integrity and function of HDL.

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