Uptake of Branched-Chain Amino Acids by Streptococcus thermophilus
نویسندگان
چکیده
منابع مشابه
Uptake of Branched-Chain Amino Acids by Streptococcus thermophilus.
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 degrees C and at pH 7.0 for the three amino acids leucine, valine, and isoleucine; a second peak existed at pH 5.0 with vali...
متن کاملRegulation of branched-chain amino acid biosynthesis by alpha-acetolactate decarboxylase in Streptococcus thermophilus.
AIMS To demonstrate the presence of an active alpha-acetolactate decarboxylase in Streptococcus thermophilus and to investigate its physiological function. METHODS AND RESULTS Streptococcus thermophilus CNRZ385 contains a gene encoding an alpha-acetolactate decarboxylase. Comparison of the production of alpha-acetolactate and its decarboxylation products, by the parent strain and an alpha-ace...
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Transamination of branched-chain amino acids to (alpha-oxoglutarate, catalyzed by leucine aminotransferase coupled to the glutamate dehydrogenase reaction, is used in an enzymic assay for determination of branched-chain amino acids in serum and tissue homogenates. The coefficients of variation of the method within-day and day-to-day are 2.4 and 6.5%, respectively. Analytical recovery of physiol...
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متن کاملRegulation of protein synthesis by branched-chain amino acids.
Historically, amino acids have been viewed as precursors for protein synthesis as well as metabolic substrates. Recently, a new role for amino acids as regulators of mRNA translation has been identified. In this role, they modulate the phosphorylation state of proteins that represent important control points in translation initiation, including the translational repressor 4E-BP1 and the ribosom...
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ژورنال
عنوان ژورنال: Applied and Environmental Microbiology
سال: 1983
ISSN: 0099-2240,1098-5336
DOI: 10.1128/aem.45.1.136-140.1983