Reminiscence of phospholipase B in Penicillium notatum

Since the phospholipase B (PLB) was reported as a deacylase of both lecithin and lysolecithin yielding fatty acids and glycerophosphocholine (GPC), there was a question as to whether it is a single enzyme or a mixture of a phospholipase A(2) (PLA(2)) and a lysophospholipase (LPL). We purified the PLB in Penicillium notatum and showed that it catalyzed deacylation of sn-1 and sn-2 fatty acids of 1,2-diacylphospholipids and also sn-1 or sn-2 fatty acids of 1- or 2-monoacylphospholipids (lysophospholipids). Further, it also has a monoacyllipase activity. The purified PLB is a glycoprotein with m.w. of 91,300. The sugar moiety is M-9 only and the protein moiety consists of 603 amino acids. PLB, different from PLA(2), shows other enzymatic activities, such as transacylase, lipase and acylesterase. PLB activity is influenced by various substances, e.g. detergents, deoxycholate, diethylether, Fe3+, and endogenous protease. Therefore, PLB might have broader roles than PLA(2) in vivo. The database shows an extensive sequence similarity between P. notatum PLB and fungal PLB, cPLA(2) and patatin, suggesting a homologous relationship. The catalytic triad of cPLA(2), Ser, Asp and Arg, is also present in P. notatum PLB. Other related PLBs, PLB/Lipases are discussed.