The yeast Candida dbicans is able to utilize L-lysine as the sole nitrogen and carbon source accompanied by intracellular accumulation of a-aminoadipate-J-semialdehyde. A novel yeast amino acid dehydrogenase catalysing the oxidative deamination of the &-group of L-lysine was found in this yeast. The enzyme, L-lysine 8-dehydrogenase, is strongly induced in cells grown on L-lysine as the sole nitrogen source. The enzyme is specific for both L-lysine and NADP+. The K,,, values were determined to be 0.87 mM for L-lysine and 0-071 mM for NADP+. An apparent M, of 87000 was estimated by gel filtration. The enzyme has maximum activity at pH 9-5 and a temperature optimum of 32 "C under our assay conditions
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