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. 1970 Jul;66(3):1008–1015. doi: 10.1073/pnas.66.3.1008

Relationship of a Membrane-Bound D-(-)-Lactic Dehydrogenase to Amino Acid Transport in Isolated Bacterial Membrane Preparations

H R Kaback 1,*, L S Milner 1
PMCID: PMC283151  PMID: 4316677

Abstract

The conversion of D-lactate to pyruvate in isolated membrane preparations of E. coli ML 308-225 markedly stimulates the transport of proline, glutamic acid, aspartic acid, aspargine, tryptophan, lysine, serine, alanine, and glycine. The uptake of histidine, phenylalanine, tyrosine, leucine, isoleucine, and valine by the membranes is also markedly stimulated by this conversion, although these amino acids are taken up much less effectively than those mentioned previously. The uptake of arginine, methionine, cystine, and cysteine is enhanced only about twofold in the presence of D-(-)-lactate, and these amino acids are not concentrated well by the membranes. With the exception of glutamate, asparate, asparagine, and methionine, which are converted to other metabolites to varying extents in the intramembranal pool, each of the other amino acids was recovered from the membranes as the unchanged amino acid. Succinate, L-(+)-lactate, D,L-α-hydroxybutyrate, and DPNH partially replace D-(-)-lactate but are less effective.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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