| 3768146 |
Strasser de Saad AM, Pesce de Ruiz Holgado AA, Oliver G: D-(+)-lactate dehydrogenase from Lactobacillus murinus. Biotechnol Appl Biochem. 1986 Oct;8(5):370-4.
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. |
2(0,0,0,2) |