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  • Title: Specificity of lysophospholipase D.
    Author: Wykle RL, Kraemer WF, Schremmer JM.
    Journal: Biochim Biophys Acta; 1980 Jul 14; 619(1):58-67. PubMed ID: 7417469.
    Abstract:
    The specificity of lysophospholipase D (1-alkyl-sn-glycero-3-phosphoethanolamine ethanolaminehydrolase, EC 3.1.4.39; also works on choline analogs) for 1-alkyl- and 1-acyl-linked substrates was examined using rat liver microsomes. The microsomes were treated with diisopropylphosphorofluoridate to inhibit the hydrolysis of acyl chains from the acyl-linked compounds (1-palmitoyl-sn-glycero-3-phosphocholine and 1-palmitoyl-sn-glycero-3-phosphoethanolamine) and were treated with p-bromophenacyl bromide to block acylation of the compounds tested. In the presence of the inhibitors, 1-alkyl-sn-glycero-3-phosphocholine and 1-alkyl-sn-glycero-3-phosphoethanolamine were hydrolyzed extensively by lysophospholipase D but the corresponding 1-acyl-linked analogs were only negligibly hydrolyzed. Lysophospholipase D therefore appears to be specific for the ether-linked compounds. 1-Alk-1-'-enyl-sn-glycero-3-phosphoethanolamine (lyso plasmalogen) was also tested as a substrate, but a plasmalogenase in the rat liver microsomes rapidly hydrolyzed the compound and we were unable to determine whether it is a substrate for lysophospholipase D. Alkyl-linked substrates containing long-chain acyl groups at the 2-position are not hydrolyzed by the enzymes. We tested 1-alkyl-2-acetoyl-sn-glycero-3-phosphocholine and 1-alkyl-2-acetoyl-sn-glycero-3-phosphoethanolamine to determine if the less bulky, more hydrophilic acetate group would permit hydrolysis by lysophospholipase D; the derivatives did not appear to be attacked, except after hydrolysis of the acetate group. However, in the absence of inhibitors, the acetate groups were rapidly hydrolyzed by microsomal preparations.
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