Lactate dehydrogenases in cyanobacteria.

Abstract:

:NAD-linked lactate dehydrogenases specific for the D- and L-lactate have been demonstrated in a number of strains of unicellular cyanobacteria. The D-lactate dehydrogenase of one strain (Synechococcus 6716) was partially purified and its properties were studied. The enzyme has a molecular weight of ca. 115000-120000, is highly specific, autooxidizable, and susceptible to inhibition by iodoacetamide, oxamate and ATP. The possible physiological functions of the enzyme in the metabolism of the organism were investigated. D-lactate carbon was incorporated in cell material during photosynthetic growth with CO2, but lactate was not used as sole source for carbon for photosynthetic or chemosynthetic development. D-lactate and pyruvate were oxidized aerobically in the dark by resting cell suspensions with the assimilation mainly of the C2 and the C3 carbon atoms. In the oxidation of lactate, acetate was excreted into the medium. No fermentation of glucose was found, but a small amount of D-lactate was detected as a product of endogenous dark metabolism of the cell. All enzymes required for the production of lactate from glucose and from glycogen were found in exponentially growing cells, but the activity of some key enzymes was low or undetectable in old cultures.

journal_name

Arch Microbiol

journal_title

Archives of microbiology

authors

Sanchez JJ,Palleroni NJ,Doudoroff M

doi

10.1007/BF00447300

subject

Has Abstract

pub_date

1975-06-20 00:00:00

pages

57-65

issue

1

eissn

0302-8933

issn

1432-072X

journal_volume

104

pub_type

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