ACETYLATION OF SPHINGOSINE BASES AND LONG-CHAIN AMINES BY CELL-FREE PREPARATIONS OF HANSENULA CIFERRI

A cell-free preparation of the yeast, Hansenula ciferri catalyzed the transfer of the acetyl group of acetyl coenzyme-A to the sphinosine bases at both their amino and hydroxyl groups. The enzyme also transferred acetyl groups to the hydroxyls of the N-acetylated sphingosine bases as well as to the amino groups of primary amines of ten or more carbon atoms. A mixture of acetate, ATP and coenzyme-A could be employed instead of acetyl CoA. The reaction had an optimal pH at about 7.8 and was inhibited by free coenzyme-A. © 1969.