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• W2078632150 abstract "Sphingosylphosphocholine (SPC), the N-deacylated form of sphingomyelin (SM), is a naturally occurring lipid mediator. However, little is known about the metabolism of SPC. We here report an in vitro assay system for SPC-phospholipase C (PLC). Using this assay system, we demonstrated that nSMase1 and nSMase2, human neutral sphingomyelinases (SMases), are capable of hydrolyzing SPC efficiently under detergent-free conditions. Bacterial and plasmodial neutral SMases also showed SPC-PLC activity. The substrate specificity of neutral SMases that hydrolyze SM, SPC, and monoradyl glycerophosphocholine, but not diradyl glycerophosphocholine, suggested that a hydrogen-bond donor at the C-2 or sn-2 position in the substrate is required for recognition by the enzymes." @default.
• W2078632150 created "2016-06-24" @default.
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• W2078632150 date "2004-01-07" @default.
• W2078632150 modified "2023-10-14" @default.
• W2078632150 title "Hydrolysis of sphingosylphosphocholine by neutral sphingomyelinases" @default.
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• W2078632150 doi "https://doi.org/10.1016/s0014-5793(03)01523-0" @default.
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