Properties of ?-lactate dehydrogenase from Lactobacillus bulgaricus: a possible different evolutionary origin for the ?- and ?-lactate dehydrogenases

15 March 1991

journal article
Published by Oxford University Press (OUP) in FEMS Microbiology Letters

Vol. 79 (1) , 89-93
https://doi.org/10.1016/0378-1097(91)90533-g

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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