PNPLA4 hydrolyzes retinyl palmitate

Stable Identifier
R-HSA-8848355
Type
Reaction [transition]
Species
Homo sapiens
Compartment
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PNPLA4 (patatin-like phospholipase domain-containing protein 4, also known as GS2 and iPLA2(eta)) catalyzes the hydrolysis of atR-PALM (all-trans retinyl palmitate) to atROL (all-trans retinol) and a molecule of PALM (palmitate) (Gao and Simon 2006; Gao and Simon 2007). The reaction is inhibited by cytosolic PLIN3 (perilipin 3). The enzyme may also catalyze transacylation reactions to form retinyl esters or promote the activity of other enzymes that do so (Gao et al. 2009).

Literature References
PubMed ID Title Journal Year
19181555 GS2 as a retinol transacylase and as a catalytic dyad independent regulator of retinylester accretion

Gao, JG, Shih, A, Gruber, R, Schmuth, M, Simon, M

Mol. Genet. Metab. 2009
16741517 Molecular screening for GS2 lipase regulators: inhibition of keratinocyte retinylester hydrolysis by TIP47

Gao, JG, Simon, M

J. Invest. Dermatol. 2006
17603008 A comparative study of human GS2, its paralogues, and its rat orthologue

Gao, JG, Simon, M

Biochem. Biophys. Res. Commun. 2007
Participants
Participates
Catalyst Activity

retinyl-palmitate esterase activity of PNPLA4 [cytosol]

This event is regulated
Negatively by
Orthologous Events
Cross References
Rhea
Authored
Reviewed
Created
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