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. 1983 Jan;45(1):136–140. doi: 10.1128/aem.45.1.136-140.1983

Uptake of Branched-Chain Amino Acids by Streptococcus thermophilus

K M Akpemado 1, P A Bracquart 1
PMCID: PMC242243  PMID: 16346160

Abstract

The transport of branched-chain amino acids in Streptococcus thermophilus was energy dependent. The metabolic inhibitors of glycolysis and ATPase enzymes were active, but the proton-conducting uncouplers were not. Transport was optimal at temperatures of between 30 and 45°C and at pH 7.0 for the three amino acids leucine, valine, and isoleucine; a second peak existed at pH 5.0 with valine and isoleucine. By competition and kinetics studies, the branched-chain amino acids were found to share at least a common transport system.

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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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