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Abstract
Saccharopine-dehydrogenase, an enzyme of lysine biosynthesis via amino-adipate pathway could be demonstrated in Phycomyces blakesleeanus . The functionality of enzyme activity and volume of extracts is linear up to 0.5 ml extract. Between 20° and 40 °C the curve of enzyme activity is also linear. In in vitro tests the pH optimum of enzyme activity could be measured at pH 6.8. The Michaelis-Menten-constants were determined in extracts purified by fractionated ammonium sulfate precipitation (50-70%). The Km constant of saccharopine-dehydrogenase from Phycomyces blakesleeanus was for lysine 1.34 mM, a-ketoglutarate 0,23 mM, and for the coenzyme NADH 120µM. The significance of these enzyme data for the biosynthesis of lysine in the fungus was discussed.
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