Abstract
a new, rapid test system to measure the activity of acetyl-CoA : deacetylcephalosporin C O-acetyltransferase (DAC-acetyltransferase) was established. The reaction product cephalosporin C could be easily analyzed by HPLC. The DAC-acetyltransferase was partially purified by means of fractionated (NH 4) 2SO 4 precipitation, Sephadex G-100 gel chromatography and isoelectric focusing. Molecular weight was determined to be 70 000 ± 5 000 and the p I 4.3 ± 0.2. Besides the two substrates acetyl-CoA and deacetylcephalosporin C, no other factor necessary for the reaction could be found. The enzyme was inhibited by coenzyme A (61%), deacetoxycephalosporin C (57%), penicillin N (14%), 2,6-dihydroxybenzoic acid (27%) and pyruvate (37%) at a concentration of 0.1 mM in each case.
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