The lipase gene family.
Development of the lipase gene family spans the change in science that witnessed the birth of contemporary techniques of molecular biology. Amino acid sequencing of enzymes gave way to cDNA cloning and gene organization, augmented by in vitro expression systems and crystallization. This review traces the origins and highlights the functional significance of the lipase gene family, overlaid on the background of this technical revolution. The gene family initially consisted of three mammalian lipases [pancreatic lipase (PL), lipoprotein lipase, and hepatic lipase] based on amino acid sequence similarity and gene organization. Family size increased when several proteins were subsequently added based on amino acid homology, including PL-related proteins 1 and 2, phosphatidylserine phospholipase A1, and endothelial lipase. The physiological function of each of the members is discussed as well as the region responsible for lipase properties such as enzymatic activity, substrate binding, heparin binding, and cofactor interaction. Crystallization of several lipase gene family members established that the family belongs to a superfamily of enzymes, which includes esterases and thioesterases. This superfamily is related by tertiary structure, rather than amino acid sequence, and represents one of the most populous families found in nature.
Wong
Howard
H
Lipid Research Laboratory, West Los Angeles Veterans Affairs Healthcare Center and Department of Medicine, University of California, Los Angeles, CA, USA. wongh@ucla.edu
Schotz
Michael C
MC
D000818:Animals; D003460:Crystallization; D019143:Evolution, Molecular; D008049:Lipase / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism*; D005810:Multigene Family; D011487:Protein Conformation; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship
D008049:Lipase