PON1,2,3:Ca2+ dimers hydrolyse 5-HETEL to 5-HETE

Stable Identifier
Reaction [transition]
Homo sapiens
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Serum paraoxonase/arylesterases 1, 2 and 3 (PON1,2 and 3) are extracellular lactonases/lactonysing enzymes with overlapping, but also distinct substrate specificity. PONs are homodimeric proteins which bind 2 Ca2+ ions per subunit, necessary for enzyme stability and enzymatic activity. All three PONs can efficiently metabolise 5-hydroxy-eicosatetraenoic acid 1,5-lactone (5-HETEL), a product of both enzymatic and nonenzymatic oxidation of arachidonic acid and may represent one of the PONs' endogenous substrates (Draganov et al. 2005).

Literature References
PubMed ID Title Journal Year
19082953 Paraoxonases (PON1, PON2, PON3) analyses in vitro and in vivo in relation to cardiovascular diseases

Aviram, M, Rosenblat, M

Methods Mol. Biol. 2008
15772423 Human paraoxonases (PON1, PON2, and PON3) are lactonases with overlapping and distinct substrate specificities

Sunahara, R, Osawa, Y, La Du, BN, Draganov, DI, Teiber, JF, Speelman, A

J. Lipid Res. 2005
Catalyst Activity

acyl-L-homoserine-lactone lactonohydrolase activity of PON1,2,3:2xCa2+ dimers [extracellular region]

Orthologous Events
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