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 Microbioljournal_title
Archives of microbiologyauthors
Sanchez JJ,Palleroni NJ,Doudoroff Mdoi
10.1007/BF00447300subject
Has Abstractpub_date
1975-06-20 00:00:00pages
57-65issue
1eissn
0302-8933issn
1432-072Xjournal_volume
104pub_type
杂志文章abstract::A novel actinomycete, strain PA1-10T, isolated from the leaf of Phyllanthus amarus collected from Bangkok, Thailand, was characterized taxonomically using a polyphasic approach. This strain contained the characteristics consistent with those of members of the genus Nonomuraea. It formed short rugose spore chain on aer...
journal_title:Archives of microbiology
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abstract::L-(+)-lactate dehydrogenase (LDH) from Staphylococcus epidermidis ATCC 14990 was purified by affinity chromatography. The purified enzyme was specifically activated by fructose-1,6-diphosphate (FDP). The concentration of FDP required for 50% maximal activity was about 0.15 mM. The enzyme activity was inhibited by aden...
journal_title:Archives of microbiology
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journal_title:Archives of microbiology
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abstract::We describe a convenient method for the in vivo construction of large plasmids that possess a multitude of restriction sites. A large (23 kbases) circular self-replicating plasmid carrying a partial LEU2-d gene was cotransformed with a circular non-replicating plasmid carrying the entire LEU2 gene. In vivo recombinati...
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journal_title:Archives of microbiology
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journal_title:Archives of microbiology
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