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Comparative studies of lactic acid dehydrogenases in lactic acid bacteria

โœ Scribed by R. Hensel; U. Mayr; K. O. Stetter; O. Kandler

Publisher
Springer
Year
1977
Tongue
English
Weight
976 KB
Volume
112
Category
Article
ISSN
0302-8933

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โœฆ Synopsis

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 efficiency 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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