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• W2024182486 endingPage "111" @default.
• W2024182486 startingPage "109" @default.
• W2024182486 abstract "LIV-I, a high-affinity system that transports neutral, branched-chain amino acids into Escherichia coli, has two components, LivG and LivF, that are homologous to the cystic fibrosis (CF) transmembrane conductance regulator (CFTR). CF-associated mutations of human CFTR were introduced into corresponding regions of LivG, and their effects on leucine transport could be grouped into three classes. Mutations were found that (i) abolished LIV-I--directed transport, (ii) retained about a quarter of wild-type activity at the Michaelis-Menten constant (KM), and (iii) had minimal activity at the KM. A mutation equivalent to a benign polymorphism had no effect on transport. The correlation of these mutational phenotypes in LivG and CFTR suggests that the LIV-I prokaryotic transporter is functionally similar to the CF protein and that this similarity can be exploited to clarify the properties of the nucleotide-binding fold in this superfamily of proteins." @default.
• W2024182486 created "2016-06-24" @default.
• W2024182486 creator A5030999547 @default.
• W2024182486 creator A5042005444 @default.
• W2024182486 creator A5049973089 @default.
• W2024182486 creator A5068242165 @default.
• W2024182486 date "1991-10-04" @default.
• W2024182486 modified "2023-10-18" @default.
• W2024182486 title "A bacterial system for investigating transport effects of cystic fibrosis--associated mutations" @default.
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• W2024182486 doi "https://doi.org/10.1126/science.1718037" @default.
• W2024182486 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/1718037" @default.
• W2024182486 hasPublicationYear "1991" @default.
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