Acetylation of sphingosine bases and long-chain amines by cell-free preparations of Hansenula ciferri |
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Authors: | Y Barenholz S Gatt |
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Affiliation: | 1. Division of BioTherapeutics, Leiden Academic Centre for Drug Research, Leiden University, Leiden, The Netherlands;2. ISIS Neutron and Muon Source, Science and Technology Facilities Council, Rutherford Appleton Laboratory, Didcot, United Kingdom |
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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. |
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