L-Malate dehydrogenase (EC 1.1.1.37), Escherichia coli

Recombinant L-malate dehydrogenase (EC 1.1.1.37) is purified from a modified E. coli strain. Malate dehydrogenase is an enzyme of the citric acid cycle that catalyzes the conversion of malate into oxaloacetate (using NAD+), which is a reversible reaction. This enzyme is also involved in gluconeogenesis, the synthesis of glucose from smaller molecules. Pyruvate in the mitochondria is acted upon by pyruvate carboxylase to form oxaloacetate, a citric acid cycle intermediate. In order to get the oxaloacetate out of the mitochondria, malate dehydrogenase reduces it to malate, and it then traverses the inner mitochondrial membrane. Once in the cytosol, the malate is oxidized back to oxaloacetate by cytosolic malate dehydrogenase. The enzyme is provided in 3.2 M ammonium sulphate. Activity: 4000 U/ml Temperature and pH optimum/stability: The optimum pH and temperature are 7.5 and 25°C, respectively. Shipping Conditions: Room Temperature. Storage Conditions: 2 °C to 8 °C. Features: >95% pure (SDS-PAGE). b3236, Malate dehydrogenase