Acyl-protein thioesterase 1 is an enzyme that in humans is encoded by the LYPLA1gene.[1][2]
Lysophospholipases are enzymes that act on biological membranes to regulate the multifunctional lysophospholipids. The protein encoded by this gene hydrolyzes lysophosphatidylcholine in both monomeric and micellar forms. The use of alternate polyadenylation sites has been found for this gene. There are alternatively spliced transcript variants described for this gene but the full length nature is not known yet.[2]
References
↑Wang A, Yang HC, Friedman P, Johnson CA, Dennis EA (Apr 1999). "A specific human lysophospholipase: cDNA cloning, tissue distribution and kinetic characterization". Biochim Biophys Acta. 1437 (2): 157–69. doi:10.1016/s1388-1981(99)00012-8. PMID10064899.
Bohn E, Gerke V, Kresse H, et al. (1992). "Annexin II inhibits calcium-dependent phospholipase A1 and lysophospholipase but not triacyl glycerol lipase activities of rat liver hepatic lipase". FEBS Lett. 296 (3): 237–40. doi:10.1016/0014-5793(92)80294-Q. PMID1531641.
Andersson B, Wentland MA, Ricafrente JY, et al. (1996). "A "double adaptor" method for improved shotgun library construction". Anal. Biochem. 236 (1): 107–13. doi:10.1006/abio.1996.0138. PMID8619474.
Wang A, Johnson CA, Jones Y, et al. (2000). "Subcellular localization and PKC-dependent regulation of the human lysophospholipase A/acyl-protein thioesterase in WISH cells". Biochim. Biophys. Acta. 1484 (2–3): 207–14. doi:10.1016/s1388-1981(00)00020-2. PMID10760470.
Devedjiev Y, Dauter Z, Kuznetsov SR, et al. (2001). "Crystal structure of the human acyl protein thioesterase I from a single X-ray data set to 1.5 A.". Structure. 8 (11): 1137–46. doi:10.1016/S0969-2126(00)00529-3. PMID11080636.
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. doi:10.1038/nature04209. PMID16189514.