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  • Title: Resolution and reconstitution of the phosphatidate-synthesizing system of rat-liver microsomes.
    Author: Yamashita S, Hosaka K, Numa S.
    Journal: Proc Natl Acad Sci U S A; 1972 Nov; 69(11):3490-2. PubMed ID: 4508337.
    Abstract:
    The phosphatidate-synthesizing system of rat-liver microsomes was resolved into two component enzymes, glycerolphosphate acyltransferase and 1-acylglycerolphosphate acyltransferase. The resolution is effected by sucrose density gradient centrifugation in the presence of a nonionic detergent, Triton X-100. Combination of both enzymes results in reconstitution of the phosphatidate-synthesizing system. These results establish that two distinct enzymes, glycerolphosphate acyltransferase and 1-acylglycerolphosphate acyltransferase, are required for synthesis of phosphatidic acid from sn-glycerol 3-phosphate.Furthermore, the 1-acylglycerolphosphate acyltransferase preparation efficiently uses unsaturated (or saturated) fatty acyl-CoA as acyl donor. Our previous studies showed that the glycerolphosphate acyltransferase preparation catalyzes formation of 1-acylglycerol 3-phosphate, using preferentially saturated fatty acyl-CoA as acyl donor. These findings indicate that the reconstituted system is capable of yielding phosphatidic acid with an asymmetric fatty acid distribution.
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