Abstract
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.
| Original language | English |
|---|---|
| Pages (from-to) | 676-680 |
| Number of pages | 5 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 35 |
| Issue number | 5 |
| DOIs | |
| State | Published - 6 Jun 1969 |
| Externally published | Yes |
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