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. 1964 Jul;88(1):25–30. doi: 10.1128/jb.88.1.25-30.1964

LACTIC DEHYDROGENASES OF PSEUDOMONAS NATRIEGENS

Hazel Walker 1, R G Eagon 1
PMCID: PMC277251  PMID: 14197895

Abstract

Walker, Hazel (University of Georgia, Athens), and R. G. Eagon. Lactic dehydrogenases of Pseudomonas natriegens. J. Bacteriol. 88:25–30. 1964.—Lactic dehydrogenases specific for d- and l-lactate were demonstrated in Pseudomonas natriegens. The l-lactic dehydrogenase showed considerable heat stability, and 40% of the activity remained in extracts after heating at 60 C for 10 min. An essential thiol group for enzyme activity was noted. The results of these experiments were consistent with the view that lactate was dehydrogenated initially by a flavin cofactor and that electrons were transported through a complete terminal oxidase system to oxygen. The intracellular site of these lactic dehydrogenases was shown to be the cell membrane. It was suggested that the main physiological role of these lactic dehydrogenases is that of lactate utilization.

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Selected References

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