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Sphingomyelinases: enzymology and membrane activity
Author(s) -
Goñi Félix M,
Alonso Alicia
Publication year - 2002
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(02)03482-8
Subject(s) - sphingomyelin , ceramide , sphingomyelin phosphodiesterase , membrane , enzyme , chemistry , acid sphingomyelinase , biochemistry , phospholipase , phospholipase a2 , biophysics , biology , apoptosis
This paper reviews our present knowledge of sphingomyelinases as enzymes, and as enzymes acting on a membrane constituent lipid, sphingomyelin. Six types of sphingomyelinases are considered, namely acidic, secretory, Mg 2+ ‐dependent neutral, Mg 2+ ‐independent neutral, alkaline, and bacterial enzymes with both phospholipase C and sphingomyelinase activity. Sphingomyelinase assay methods and specific inhibitors are reviewed. Kinetic and mechanistic studies are summarized, a kinetic model and a general‐base catalytic mechanism are proposed. Sphingomyelinase–membrane interactions are considered from the point of view of the influence of lipids on the enzyme activity. Moreover, effects of sphingomyelinase activity on membrane architecture (increased membrane permeability, membrane aggregation and fusion) are described. Finally, a number of open questions on the above topics are enunciated.