Abstract
A d-glucosamine 6-phosphate N-acetyltransferase from Blastocladiella emersonii zoospores was partially purified to a specific activity of 2.41 IU per mg of protein. Its pH optimum was 8.05 and its Km values were 2.4 × 10−4 M d-glucosamine 6-phosphate and 0.38 × 10−4 M Na3S-acetyl coenzyme A.
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