D-Lactate dehydrogenase

Recombinant D-lactate dehydrogenase (EC 1.1.1.28) is purified from a modified E. coli strain. D-Lactate dehydrogenase is an enzyme that catalyzes specifically the reduction of D(+) lactate to pyruvate with concomitant oxidation of NAD⁺ to NADH. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-OH group of donor with NAD⁺ or NADP⁺ as acceptor. The systematic name of this enzyme is D-lactate:NAD+ oxidoreductase. This enzyme has been identified mainly in lower organisms and, e.g. in lactic acid bacteria, where it plays a key role in anaerobic energy metabolism. In fact, very few D-specific enzymes have been identified in vertebrates. In rare instances, accumulation of D-lactate has been reported in patients with shortbowel syndrome leading to severe lactic acidosis. The quality of several food products are correlated to its content of D-lactic acid. The enzyme is provided in 3.2 M ammonium sulphate.

Activity: 8900 U/ml

Temperature and pH optimum/stability: The optimum pH and temperature are 7.0 and 37 °C, respectively.