Journal of Lipid Research, Vol. 15, 1-10, January 1974
Copyright © 1974 by Lipid Research, Inc.
Metabolism of sulfoquinovosyl diglyceride in Chlorella pyrenoidosa by sulfoquinovosyl monoglyceride:fatty acyl CoA acyltransferase and sulfoquinovosyl glyceride:fatty acyl ester hydrolase pathways
M. G. Wolfersberger and Ronald A. Pieringer
Department of Biochemistry, Temple University School of Medicine, Philadelphia, Pennsylvania 19140
Cell-free preparations of Chlorella pyrenoidosa catalyze the transfer of the fatty acyl moiety of fatty acyl CoA derivatives to sulfoquinovosyl monoglyceride to form sulfoquinovosyl diglyceride. This reaction is stimulated by Triton X-100 concentrations of up to 0.6 mg/ml and has a pH optimum of 7.7. Similar Chlorella preparations catalyze the stepwise removal of both fatty acyl groups from sulfoquinovosyl diglyceride to form sulfoquinovosyl monoglyceride and then sulfoquinovosyl glycerol. This reaction is inhibited by both calcium and magnesium. The nonionic surfactant Triton X-100 inhibits the enzymatic deacylation at concentrations of less than 0.5 mg/ml but stimulates it at higher concentrations. The pH optimum for the deacylation of sulfoquinovosyl glycerides is 8.2, with little activity observed below pH 8. The enzymatic activities for both the transacylation and deacylation reactions are associated with a 30,000 g particulate fraction of Chlorella. Sulfoquinovosyl glycerol was found not to be an acceptor of the fatty acyl moiety of fatty acyl CoA derivatives. Methods are described for the preparation of sulfoquinovosyl monoglyceride, sulfoquinovose, and 3-sulfo-1,2-propanediol.
Supplementary key words algae • fatty acyl CoA • lipase • sulfolipid • sulfoquinovose • sulfoquinovosyl glycerol • sulfoquinovosyl monoglyceride • 3-sulfo-1,2-propanediol
Submitted on October 27, 1972
Revised on June 12, 1973
Accepted on August 28, 1973
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