[17] assay of fatty acid synthase using a bicyclic dione as substrate
AH Ullman, HB White III - Methods in enzymology, 1981 - Elsevier
Publisher Summary This chapter discusses the assay of fatty acid synthase using a bicyclic
dione as substrate. Fatty acid synthase is detected by assaying the β-ketoacyl-ACP
rcductase component of the enzyme complex (I). The NADPH-dependent reduction of the
non-physiological substratc, cis-decalin-1, 4-dione, by the β-ketoacyl-ACP reductase is
monitored spectrophotometrically at 340 nm. It is found that since carbonyl reduction is a
nonrate-limiting reaction in the synthesis of fatty acids, the assay of reductase is significantly …
dione as substrate. Fatty acid synthase is detected by assaying the β-ketoacyl-ACP
rcductase component of the enzyme complex (I). The NADPH-dependent reduction of the
non-physiological substratc, cis-decalin-1, 4-dione, by the β-ketoacyl-ACP reductase is
monitored spectrophotometrically at 340 nm. It is found that since carbonyl reduction is a
nonrate-limiting reaction in the synthesis of fatty acids, the assay of reductase is significantly …