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

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

Stable Identifier

R-HSA-8932633

Type

Reaction [transition]

Species

Homo sapiens

Compartment

extracellular region

ReviewStatus

5/5

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

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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 arachidonate 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 Draganov, DI, Teiber, JF, Speelman, A, Osawa, Y, Sunahara, R, La Du, BN	J. Lipid Res.	2005