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J Biol Chem, Vol. 273, Issue 10, 5468-5477, March 6, 1998
From the Howard Hughes Medical Institute, Departments of Medicine
and Biochemistry, and Regional Primate Research Center, University
of Washington, Seattle, Washington 98195-7370
We report the molecular cloning and expression of
a phosphatidic acid-preferring phospholipase A1 from
bovine testis. The open reading frame encoded an 875-amino acid protein
with a calculated molecular mass of 97,576 daltons and a pI of 5.61. The sequence included a region similar to a lipase consensus sequence
containing the putative active site serine and also included a
potential, coiled-coil-forming region. Expression of the open reading
frame in COS1 cells resulted in a 20-44-fold increase in phosphatidic acid phospholipase A1 activity over that of control cells.
Mutation of the putative active site serine (amino acid 540)
demonstrated that it was essential for this increase in enzyme
activity. Northern blot analysis revealed at least five different
messages with the highest overall message levels in mature testis, but
detectable message in all tissues examined. Two possible alternately
spliced regions in the open reading frame also were identified.
Finally, a search of the data base identified six related proteins: a
potential counterpart of the phospholipase A1 in
Caenorhabditis elegans, two putative lipases in yeast, and
three proteins separately encoded by the Drosophila retinal
degeneration B gene and its mouse and human homologues.
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