Abstract
Summary Riboflavin overproducing yeast Pichia guilliermondii grown under iron deficiency produces rather large amounts of ribitol and D-arabinitol. The paper describes the presence of several enzymes involved in the ribitol metabolism such as the ribitol-5-phosphate dehydrogenase and the ribose isomerase as well as the enzymatic synthesis of CDP-ribitol. Ribitol-5-phosphate dehydrogenase was purified about 20-fold. Its enzyme kinetics was estimated. The enzyme activity is sensitive against ammonium ions. In iron-deficient yeast the ribitol-5-phosphate dehydrogenase is derepressed by the factor 3-4 compared with iron-grown cells. In a culture medium containing glucose, ribitol or alanine, the enzyme activity is increased. CDP-ribitol formation from D-ribitol-5-phosphate and CTP suggests the presence of some type of nucleotidyl transferase. The metabolism or ribitol in relation to riboflavin biosynthesis is discussed.
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