Paraoxonase

Paraoxonases are a family of mammalian enzymes with aryldialkylphosphatase activity. There are three paraoxonase isozymes, which were originally discovered for their involvement in the hydrolysis of organophosphates.^[1]

Research has indicated the enzymatic activity of paraoxonases is more diversified than its activity as an organophosphatase. Esterase and lactonase activity has also been observed from these enzymes and though the physiologically relevant substrates for these enzymes are unknown, it is likely that lactones are the main substrate (although there is a relatively high level of variation in substrate specificity among these enzymes). Most of the studies on the paraoxonase family have specifically looked at the paraoxonase 1 type, leaving much to be learned about the remaining two.^[2]

The study of this enzyme family has many potential consequences in preventative medicine and toxicology as well as in certain societal contexts. The genes that encode for these enzymes have a number of different polymorphisms, which created additional interest in the study of this enzyme group and its potential ethnic variations.^[3] Additional research on the inhibition and selective inhibition, specifically of PON1, has been done to shed some light on the connections between decreases in enzymatic activity of individuals with cardiovascular diseases.^[4] Evidence also suggests that this family of enzymes has some role in our innate immune system.^[5]