Abhydrolase domain-containing protein 4, also known as Lyso-N-acylphosphatidylethanolamine lipase, Alpha/beta-hydrolase 4 and ABHD4, is a protein which belongs to the peptidase S33 family and ABHD4 / ABHD5 subfamily. The alpha/beta hydrolase fold is common to a number of hydrolytic enzymes of widely differing phylogenetic origin and catalytic function. The core of each enzyme is an alpha/beta-sheet (rather than a barrel), containing 8 strands connected by helices. The enzymes are believed to have diverged from a common ancestor, preserving the arrangement of the catalytic residues. All have a catalytic triad, the elements of which are borne on loops, which are the best-conserved structural features of the fold. ABHD4 lysophospholipase selective for N-acyl phosphatidylethanolamine (NAPE). ABHD4 contributes to the biosynthesis of N-acyl ethanolamines, including the endocannabinoid anandamide by hydrolyzing the sn-1 and sn-2 acyl chains from N-acyl phosphatidylethanolamine (NAPE) generating glycerophospho-N-acyl ethanolamine (GP-NAE), an intermediate for N-acyl ethanolamine biosynthesis. ABHD4 hydrolyzes substrates bearing saturated, monounsaturated, polyunsaturated N-acyl chains.
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