Comparative studies of lactic acid dehydrogenases in lactic acid bacteria. I. Purification and kinetics of the allosteric L-lactic acid dehydrogenase from Lactobacillus casei ssp. casei and Lactobacillus curvatus.

Archives of microbiology ·Vol. 112 ·No. 1 ·1977-02-04 ·Pages 81-93

Hensel R, Mayr U, Stetter KO, Kandler O

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 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.

MeSH Terms

Allosteric Regulation Cations, Divalent Chromatography, Affinity Drug Stability Enzyme Activation Fructosephosphates Hydrogen-Ion Concentration Kinetics L-Lactate Dehydrogenase/isolation & purification Lactobacillus/enzymology Lactobacillus casei/enzymology Manganese NAD Pyruvates/metabolism

Chemicals

Cations, Divalent Fructosephosphates Pyruvates NAD Manganese L-Lactate Dehydrogenase

Authors & Affiliations

4 authors, click to expand affiliations / ORCID

Hensel R

Mayr U

Stetter K O

Kandler O

References (19)

19 references, click to expand

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Article Info

Journal

Archives of microbiology

Abbr.

Arch Microbiol

ISSN

0302-8933

DOI

10.1007/BF00446658

Published

1977-02-04

Pages

81-93

Language

English

Region

Germany

NLM ID

0410427

Subset

External Links

PubMed source DOI: 10.1007/BF00446658 View journal details

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Comparative studies of lactic acid dehydrogenases in lactic acid bacteria. I. Purification and kinetics of the allosteric L-lactic acid dehydrogenase from Lactobacillus casei ssp. casei and Lactobacillus curvatus.

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