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Title

Phosphatidate phosphohydrolase catalyzes the hydrolysis of ceramide 1- phosphate, lysophosphatidate, and sphingosine 1-phosphate

AuthorsWaggoner, David W.; Gómez-Muñoz, Antonio; Brindley, David N.
Issue Date1996
PublisherAmerican Society for Biochemistry and Molecular Biology
CitationJournal of Biological Chemistry 271(28): 16506-16509 (1996)
AbstractA Mg2+-independent phosphatidate phosphohydrolase was purified from rat liver plasma membranes in two distinct forms, an anionic protein and a cationic protein. Both forms of the enzyme dephosphorylated phosphatidate, ceramide 1-phosphate, lysophosphatidate, and sphingosine 1-phosphate. When assayed at a constant molar ratio of lipid to Triton X-100 of 1:500, the apparent K(m) values of the anionic phosphohydrolase for the lipid substrates was 3.5, 1.9, 0.4, and 4.0 μM, respectively. The relative catalytic efficiency of the enzyme for phosphatidate, ceramide 1-phosphate, lysophosphatidate, and sphingosine 1-phosphate was 0.16, 0.14, 0.48, and 0.04 liter (min · mg)-1, respectively. The hydrolysis of phosphatidate was inhibited competitively by ceramide 1-phosphate, lysophosphatidate, and sphingosine 1-phosphate. The K((i)(app)) values were 5.5, 5.9, and 4.0 μM, respectively. The hydrolysis of phosphatidate by the phosphohydrolase conformed to a surface dilution kinetic model. It is concluded that the enzyme is a lipid phosphomonoesterase that could modify the balance of phosphatidate, ceramide 1-phosphate, lysophosphatidate, and sphingosine 1- phosphate relative to diacylglycerol, ceramide, monoacylglycerol, and sphingosine, respectively. The enzyme could thus play an important role in regulating cell activation and signal transduction.
URIhttp://hdl.handle.net/10261/79107
DOI10.1074/jbc.271.28.16506
Identifiersdoi: 10.1074/jbc.271.28.16506
issn: 0021-9258
e-issn: 1083-351X
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