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- W2022728517 abstract "(1) The oxidation of DL -lactate by Escherichia coli NCTC 8196 has been shown to be catalysed by two enzymes, one specific for D -lactate, the other specific for L -lactate. (2) Both enzymes were present during aerobic and anaerobic growth on all media tested. A higher level of both enzymes was produced in cells grown with lactate as growth medium, and the level of L -lactate dehydrogenase ( L -lactate:NAD + oxido-reductase, EC 1.1.1.27) was markedly reduced by growth on glucose, pyruvate or succinate. (3) Heating at 60° for 1.5 min caused almost complete loss of D -lactate dehydrogenase ( D -lactate:NAD + oxidoreductase, EC 1.1.1.28) activity with only slight loss of L -lactate dehydrogenase activity. d-lactate dehydrogenase was inhibited by PCMB, mepacrine and glucose, while L -lactate dehydrogenase was hardly affected. Both enzymes were slightly and equally affected by amytal. (4) The activity of both enzymes was incompletely destroyed by drying extracts as acetone powders. Some stimulation of both activities in the acetone powder was achieved by the addition of methylene blue to the assay system. (9) Some of the D - and L -lactate dehydrogenase activity was particle bound. The particles were of irregular size and were able to oxidize a larger number of carbon compounds, Enzyme activities could be solubilised from the particles by treatment with 1% sodium dodecyl sulphate at pH 10. (6) No lactate racemase (EC 5.1.2.1) activity could be demonstrated." @default.
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- W2022728517 date "1966-01-01" @default.
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- W2022728517 title "D- and L-lactate dehydrogenases in Escherichia coli" @default.
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- W2022728517 doi "https://doi.org/10.1016/s0926-6593(66)80093-0" @default.
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