P. Roy Vagelos

TL;DR: Inhibition of β-ketoacyl-acyl carrier protein synthetase by cerulenin was irreversible, and it was associated with the binding of approximately 1 mole of inhibitor per mole of enzyme when inhibition approached 100 %.

TL;DR: Results show the heterogeneity of membranous enzymes with respect to their dependence upon the presence of intact membrane phospholipids, and the similarity in the rate of hydrolysis of phospholips and the rates of inactivation of certain membran Mous enzymes suggests that these enzymes are dependent on phospholipopids whose susceptibility to phospholIPase C hydrolytic is similar to the bulk of membrane phosphols.

TL;DR: The phospholipid biosynthetic enzymes of the cell envelope of Escherichia coli and Salmonella typhimurium had highest specific activities in the cytoplasmic membrane fraction and lowest specific activity in the outer membrane fraction obtained by isopycnic sucrose density gradient centrifugation of the total membrane fraction of lysozyme-EDTA spheroplasts.

TL;DR: The difference in the dependence of the temperature characteristics of various membranous enzymes on membrane fatty acid composition suggests a heterogeneity in the relationship between membran Mous enzymes and membrane phospholipids.

TL;DR: These studies provide a basis for exploring the properties of the fatty acids and phospholipids required for the formation, structure, and function of membranes.