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

Stable Identifier
R-HSA-8932633
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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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
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
19082953 Paraoxonases (PON1, PON2, PON3) analyses in vitro and in vivo in relation to cardiovascular diseases

Aviram, M, Rosenblat, M

Methods Mol. Biol. 2008
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
acyl-L-homoserine-lactone lactonohydrolase activity of PON1,2,3:2xCa2+ dimers [extracellular region]
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Activity
Orthologous Events
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