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  • Title: Properties of D-lactate dehydrogenase from Lactobacillus bulgaricus: a possible different evolutionary origin for the D- and L-lactate dehydrogenases.
    Author: Le Bras G, Garel JR.
    Journal: FEMS Microbiol Lett; 1991 Mar 15; 63(1):89-93. PubMed ID: 2044942.
    Abstract:
    The NAD-dependent D-lactate dehydrogenase from Lactobacillus bulgaricus has been purified to homogeneity. This enzyme was a dimer made of two identical chains of molecular mass 37,000. Saturation by either substrate was hyperbolic, with Km values of 50 microM for NADH and 1 mM for pyruvate. The specific activity was 2200 units/mg and was not affected by the presence of fructose-1,6-bisphosphate, Mn2+ ions, ATP or ADP. The amino-terminal sequence determined on 50 residues showed no significant homology with known lactate dehydrogenases, suggesting that the D-lactate dehydrogenase from L. bulgaricus could not be evolutionarily related to the family of NAD-dependent L-lactate dehydrogenases.
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