Regulation of high-affinity leucine transport in escherichia coli
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چکیده
منابع مشابه
Regulation of leucine transport and binding proteins in Escherichia coli.
The branched-chain amino acids are transported into the bacteria Escherichia coli by two types of transport systems, a high affinity transport system (LIV-I) which requires periplasmic binding proteins and a low affinity membrane bound system (LIV-11). The LIV-I system is sensitive to osmotic shock while the LIV-I1 system can be observed in membrane vesicle preparations (Kaback, ’71). Berger an...
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The major component of leucine uptake in Escherichia coli K-12 is a common system for l-leucine, l-isoleucine, and l-valine (LIV-I) with a Michaelis constant (K(m)) value of 0.2 muM (LIV-I system). The LIV-binding protein appears to be associated with this system. It now appears that the LIV-I transport system and LIV-binding protein also serve for the entry of l-alanine, l-threonine, and possi...
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Leucine is transported into E. coli cells by high-affinity transport systems (LIV-I and leucine-specific systems) which are sensitive to osmotic shock and require periplasmic binding proteins. In addition leucine is transported by a low-affinity system ( LIV-11) which is membrane bound and retained in membrane vesicle preparations. The LIV-I system serves for threonine and alanine in addition t...
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I,-Arabinosr is transported into Escherichia coli via two independent transport systems, a system possessing relatively low affinity for arabinose, the araE system, and a system of higher affinity for arabinose, t)he araFG system. In the work reported here we demonstrate that insert,ion of the Mu-Zac bacteriophage isolated by Casadaban 8r Cohen (1979) permits a reliable measurement’ of the expr...
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ژورنال
عنوان ژورنال: Journal of Supramolecular Structure
سال: 1980
ISSN: 0091-7419,1547-9366
DOI: 10.1002/jss.400140410