Open AccessInhibition of Yeast Phosphatidic‐Acid Synthesis by Free Fatty Acids
Author(s) -
MORIKAWA Minoru,
YAMASHITA Satoshi
Publication year - 1978
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1978.tb12141.x
Subject(s) - acyltransferase , acyltransferases , biochemistry , phosphatidic acid , fatty acid , yeast , chemistry , free fatty acid receptor , biology , enzyme , biosynthesis , polyunsaturated fatty acid , phospholipid , membrane
Particulate preparations obtained from cells of yeast Saccharomyces sake have been shown to possess glycerolphosphate acyltransferase and 1‐acylglycerolphosphate acyltransferase and 1‐acylglycerolphosphate acyltransferase activities. Glycerolphosphate acyltransferase exhibits a high specificity for saturated and monoenoic fatty acyl‐CoA thioesters. When palmitoyl‐CoA is employed as sole acyl group donor, the major lipid product is lysophosphatidic acid. 1‐Acylglycerolphosphate acyltransferase of this yeast species has a rather strict specificity for monoenoic fatty acyl‐CoA thioesters as acyl donor. These two acyltransferases are strongly inhibited in vitro by low concentrations of free fatty acids. 1‐Acylglycerolphosphate acyltransferase is much more susceptible to fatty acid inhibition than glycerolphosphate acyltransferase. The inhibition is dependent not only on the concentration of fatty acid, but also on the length of exposure to fatty acid. Both saturated and unsaturated fatty acids inhibit the acyltransferase activities. The inhibitory effects of fatty acids cannot be ascribed to a nonspecific surfactant action of fatty acids. The present results support the view that free fatty acid serves as a regulator of glycerolipid synthesis.