FEATURES

FAMILY

DESCRIPTION

Also known as PA1B2_BOVIN, PAFAH1B2P68402, PAFAHB. Alpha2 catalytic subunit of the cytosolic type I platelet-activating factor (PAF) acetylhydrolase (PAF-AH (I)) heterotetrameric enzyme that catalyzes the hydrolyze of the acetyl group at the sn-2 position of PAF and its analogs and modulates the action of PAF (PubMed:10542206). The activity and substrate specificity of PAF-AH (I) are affected by its subunit composition (PubMed:10542206). The alpha2/alpha2 homodimer (PAFAH1B2/PAFAH1B2 homodimer) hydrolyzes PAF and 1-O-alkyl-2-acetyl-sn-glycero-3-phosphorylethanolamine (AAGPE) more efficiently than 1-O-alkyl-2-acetyl-sn-glycero-3-phosphoric acid (AAGPA) (PubMed:10542206). In contrast, the alpha1/alpha2 heterodimer(PAFAH1B3/PAFAH1B3 heterodimer) hydrolyzes AAGPA more efficiently than PAF, but has little hydrolytic activity towards AAGPE (PubMed:10542206). May play a role in male germ cell meiosis during the late pachytenestage and meiotic divisions as well as early spermiogenesis (By similarity). Forms a catalytic dimer which is either homodimer (alpha2/alpha2 homodimer) or heterodimer with PAFAH1B3 (alpha2/alpha1 heterodimer) (PubMed:10542206). Component of the cytosolic (PAF-AH (I)) heterotetrameric enzyme, which is composed of PAFAH1B1 (beta), PAFAH1B2 (alpha2) and PAFAH1B3 (alpha1) subunits (PubMed:10542206). The catalytic activity of the enzyme resides in the alpha1 (PAFAH1B3) and alpha2 (PAFAH1B2) subunits, whereas the beta subunit (PAFAH1B1) has regulatory activity (PubMed:10542206). Trimer formation is not essential for the catalytic activity (PubMed:10542206). Interacts (homodimer form) with PAFAH1B1 (homodimer form); PAFAH1B2 competes with NDEL1 for PAFAH1B1 binding (By similarity). Interacts with VLDLR; this interaction may modulate the Reelin pathway (By similarity).

EXTERNAL LINKS

PAFAH1B2P68402

Platelet-activating factor acetylhydrolase IB subunit alpha2

PAFAH1B2P68402

Molecular Synopsis