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Hydrolysis of sphingosylphosphocholine by neutral sphingomyelinases
Author(s) -
Miura Yukiko,
Gotoh Eriko,
Nara Futoshi,
Nishijima Masahiro,
Hanada Kentaro
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01523-0
Subject(s) - sphingomyelin , chemistry , substrate (aquarium) , hydrolysis , enzyme , phospholipase , biochemistry , in vitro , phospholipase c , metabolism , mediator , stereochemistry , chromatography , biology , microbiology and biotechnology , membrane , ecology
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.