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  • Title: D-(+)-lactate dehydrogenase from Lactobacillus murinus.
    Author: Strasser de Saad AM, Pesce de Ruiz Holgado AA, Oliver G.
    Journal: Biotechnol Appl Biochem; 1986 Oct; 8(5):370-4. PubMed ID: 3768146.
    Abstract:
    D-(+)-Lactate dehydrogenase from Lactobacillus murinus was purified 670-fold. The Mr was 140,000 as determined by gel filtration. Maximum enzymatic activity was observed at 25 degrees C and pH 6.0 in 200 mM Na2KPO4 buffer. When the temperature was increased from 60 to 65 degrees C, the enzyme was completely inactive in 5 min. The apparent Km for pyruvate and NADH were 4.7 x 10(-4) and 1 x 10(-5) M, respectively. Pyruvate analogs such as oxalate, oxamate, 2-oxobutyrate, and malonate acted as a competitive inhibitors. L-Lactate and L-malate were noncompetitive inhibitors.
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