The yeast is able to utilize l-lysine as the sole nitrogen and carbon source accompanied by intracellular accumulation of α-aminoadipate-δ-semialdehyde. A novel yeast amino acid dehydrogenase catalysing the oxidative deamination of the ε-group of l-lysine was found in this yeast. The enzyme, l-lysine ε-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.


Article metrics loading...

Loading full text...

Full text loading...


Most cited this month Most Cited RSS feed

This is a required field
Please enter a valid email address
Approval was a Success
Invalid data
An Error Occurred
Approval was partially successful, following selected items could not be processed due to error