title: The expanding superfamily of phospholipase A(2) enzymes: classification and characterization.
abstract: The phospholipase A(2) (PLA(2)) superfamily consists of a broad range of enzymes defined by their ability to catalyze the hydrolysis of the middle (sn-2) ester bond of substrate phospholipids. The hydrolysis products of this reaction, free fatty acid and lysophospholipid, have many important downstream roles, and are derived from the activity of a diverse and growing superfamily of PLA(2) enzymes. This review updates the classification of the various PLA(2)'s now described in the literature. Four criteria have been employed to classify these proteins into one of the 11 Groups (I-XI) of PLA(2)'s. First, the enzyme must catalyze the hydrolysis of the sn-2 ester bond of a natural phospholipid substrate, such as long fatty acid chain phospholipids, platelet activating factor, or short fatty acid chain oxidized phospholipids. Second, the complete amino acid sequence of the mature protein must be known. Third, each PLA(2) Group should include all of those enzymes that have readily identifiable sequence homology. If more than one homologous PLA(2) gene exists within a species, then each paralog should be assigned a Subgroup letter, as in the case of Groups IVA, IVB, and IVC PLA(2). Homologs from different species should be classified within the same Subgroup wherever such assignments are possible as is the case with zebra fish and human Group IVA PLA(2) orthologs. The current classification scheme does allow for historical exceptions of the highly homologous Groups I, II, V, and X PLA(2)'s. Fourth, catalytically active splice variants of the same gene are classified as the same Group and Subgroup, but distinguished using Arabic numbers, such as for Group VIA-1 PLA(2) and VIA-2 PLA(2)'s. These four criteria have led to the expansion or realignment of Groups VI, VII and VIII, as well as the addition of Group XI PLA(2) from plants.
authors.affiliation: Department of Chemistry and Biochemistry, MC 0601, Revelle College and School of Medicine, University of California, San Diego, La Jolla, CA 92093-0601, USA.
authors.forename: D A
authors.initials: DA
authors.lastname: Six
authors.forename: E A
authors.initials: EA
authors.lastname: Dennis
mesh_terms: D000818:Animals; D001665:Binding Sites; D003600:Cytosol / Q000201:enzymology; D006639:Histidine / Q000737:chemistry; D006801:Humans; D008969:Molecular Sequence Data; D010741:Phospholipases A / Q000737:chemistry / Q000145:classification* / Q000235:genetics; D010743:Phospholipids / Q000737:chemistry; D017385:Sequence Homology; D012694:Serine / Q000737:chemistry; D013045:Species Specificity
chemical_list: D010743:Phospholipids; D012694:Serine; D006639:Histidine; D010741:Phospholipases A