Identification of mouse palmitoyl-coenzyme A Δ9-desaturase

Studies on palmitoyl-coenzyme A synthetase.

The purification and properties of microsomal palmitoyl-coenzyme A synthetase.

The isolation and purification of palmitoyl-CoA synthetase from rat liver microsomes is described. Several methods suitable for enzyme assay are described. The general properties and kinetic parameters of the purified enzyme were determined and are discussed in relationship to microsomal fatty acid activation.

Inhibition of glucose 6-phosphate dehydrogenase by palmitoyl coenzyme A.

Low concentrations of palmitoyl coenzyme A inhibit yeast glucose-6-P dehydrogenase (TAKETA, K., AND POGELL, B. M. (1966) J. Biol. Chem. 241, 720). This inhibition is prevented or reversed by bovine serum albumin, mycobacterial polysaccharides, or alkylated cyclodextrins. Sephadex chromatography and sucrose density gradient centrifugation show that palmitoyl-CoA inhibits by dissociating the tetr...

Inhibition of stearoyl coenzyme A desaturase by sterculate in mouse liver microsomes.

17. REFERENCES ENQELMAN, D. M. (1970) J. Mol. Biol. 47, 115-117 STEM, J. M., TOURTELLOTTE, M. E., REINEBT, J. C., MCETEANEY, R. N., AND RADER, R. L. (1969) P~oc. Nat. Acad. Sci. U. S. A. 63, 104 MELCHIOR, D. L., MOROWITZ, H. J., STURTEVANT, J. M., AND TSONQ, T. Y. (1970) B&him. Biophya. Acta 219, 114-122 LADBROOKE, B. D., WILLIAMS, R. M., AND CHAPMAN, D. (1968) B&him. hiophya. Acta 150, 333-340...

Regulation of the activity of acetyl coenzyme A carboxylase by palmitoyl coenzyme A and citrate.

Pahnitoyl-CoA (100 PM), in the presence of albumin (24 mg per ml), inhibited the incorporation of [14C]citrate into fatty acids in a cytosol fraction of chick liver and inhibited the activity of acetyl-CoA carboxylase purified from chick liver. Under similar incubation conditions, pahnitoyl-CoA (ZOO PM) did not inhibit fatty acid synthetase, ATP-citrate lyase, malic enzyme, NADP-linked isocitra...