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Transport of branched-chain amino acids in Corynebacterium glutamicum

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Abstract

The transport of branched-chain amino acids was characterized in intact cells of Corynebacterium glutamicum ATCC 13032. Uptake and accumulation of these amino acids occur via a common specific carrier with slightly different affiniteis for each substrate (K m[Ile]=5.4 μM, K m[Leu]=9.0 μM, K m[Val]=9.5 μM). The maximal uptake rates for all three substrates were very similar (0.94–1.30 nmol/mg dw · min). The optimum of amino acid uptake was at pH 8.5 and the activation energy was determined to be 80 kJ/mol. The transport activity showed a marked dependence on the presence of Na+ ions and on the membrane potential, but was independent of an existing proton gradient. It is concluded, that uptake of branched-chain amino acid transport proceeds via a secondary active Na+-coupled symport mechanism.

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Abbreviations

CCCP:

Carboxyl cyanide m-chlorophenylhydrazone

dw:

dry weight

MES:

2[N-morpholino]ethanesulfonic acid

mon:

monensin

nig:

nigericin

TPP:

tetraphenylphosphonium bromide

Tris:

tris[hydroxymethyl]aminomethane

val:

valinomycin

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Ebbighausen, H., Weil, B. & Krämer, R. Transport of branched-chain amino acids in Corynebacterium glutamicum . Arch. Microbiol. 151, 238–244 (1989). https://doi.org/10.1007/BF00413136

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  • DOI: https://doi.org/10.1007/BF00413136

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