1887

Abstract

The yeast is able to utilize l-lysine as the sole nitrogen and carbon source accompanied by intracellular accumulation of a-aminoadipate-d-semialdehyde. A novel yeast amino acid dehydrogenase catalysing the oxidative deamination of the e-group of l-lysine was found in this yeast. The enzyme, l-lysine e-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 values were determined to be 0.87 mM for l-lysine and 0071 mM for NADP. An apparent 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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/content/journal/micro/10.1099/00221287-137-3-711
1991-03-01
2021-05-17
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