Abstract
The stability, pH-dependence and kinetic properties of the Mn2+ and FDP-activated NAD-dependent lactic acid dehydrogenases from Lactobacillus casei ssp. casei (ATCC 393) and L. curvatus (DSM) 20010) were studied after the enzymes were purified to homogeneity by affinity chromatography. Both enzymes are virtually unidirectional, catalysing efficiently only the reduction of pyruvate. They are similar with respect to the effector requirement and pH-optimum. They differ, however, in their electrophoretic mobility, heat stability, pH-dependence of the Mn2+ requirement and several kinetic properties. It is suggested that most of these differences are caused by differences of the negative charges in the vicinity of the FDP-binding site or the site responsible for the interaction of the subunits of the enzymatically active oligomeres.
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Abbreviations
- l-LDH:
-
l-Lactic acid dehydrogenase
- FDP:
-
Fructose-1,6-bisphosphate
- DTE:
-
Dithioerythrol
References
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In the case of the L. casei-LDH the shape of the NADH saturation curve is not changed by omitting the effectors FDP and Mn 2+. The K M under these conditions is 3 fold higher (10.10 −5 M).
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Hensel, R., Mayr, U., Stetter, K.O. et al. Comparative studies of lactic acid dehydrogenases in lactic acid bacteria. Arch. Microbiol. 112, 81–93 (1977). https://doi.org/10.1007/BF00446658
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DOI: https://doi.org/10.1007/BF00446658