Structural highlights
Function
[LYPL1_HUMAN] Does not exhibit phospholipase nor triacylglycerol lipase activity, able to hydrolyze only short chain substrates due to its shallow active site.[1]
Publication Abstract from PubMed
Sequence homology indicates the existence of three human cytosolic acyl protein thioesterases, including APT1 that is known to depalmitoylate H- and N-Ras. The lysophospholipase-like 1 (LYPLAL1) protein is predicted to be related to APT1 and might also function as a potential triacylglycerol lipase involved in obesity. However, its role remained unclear. The 1.7 A crystal structure of LYPLAL1 reveals a fold very similar to APT1, but features a shape of the active site that precludes binding of long-chain substrates. Biochemical data demonstrate that LYPLAL1 exhibits neither phospholipase nor triacylglycerol lipase activity, but rather accepts short-chain substrates. Furthermore, extensive screening efforts using chemical array technique revealed a first small molecule inhibitor of LYPLAL1.
Crystal structure of the predicted phospholipase LYPLAL1 reveals unexpected functional plasticity in spite of close relationship to acyl protein thioesterases.,Burger M, Zimmermann TJ, Kondoh Y, Stege P, Watanabe N, Osada H, Waldmann H, Vetter IR J Lipid Res. 2011 Nov 3. PMID:22052940[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Burger M, Zimmermann TJ, Kondoh Y, Stege P, Watanabe N, Osada H, Waldmann H, Vetter IR. Crystal structure of the predicted phospholipase LYPLAL1 reveals unexpected functional plasticity in spite of close relationship to acyl protein thioesterases. J Lipid Res. 2011 Nov 3. PMID:22052940 doi:10.1194/jlr.M019851
- ↑ Burger M, Zimmermann TJ, Kondoh Y, Stege P, Watanabe N, Osada H, Waldmann H, Vetter IR. Crystal structure of the predicted phospholipase LYPLAL1 reveals unexpected functional plasticity in spite of close relationship to acyl protein thioesterases. J Lipid Res. 2011 Nov 3. PMID:22052940 doi:10.1194/jlr.M019851
