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- W2162222799 abstract "ABSTRACT Amino acid uptake by Rhizobium leguminosarum is dominated by two ABC transporters, the general amino acid permease (Aap) and the branched-chain amino acid permease (Bra Rl ). Characterization of the solute specificity of Bra Rl shows it to be the second general amino acid permease of R. leguminosarum . Although Bra Rl has high sequence identity to members of the family of hydrophobic amino acid transporters (HAAT), it transports a broad range of solutes, including acidic and basic polar amino acids ( l- glutamate, l -arginine, and l -histidine), in addition to neutral amino acids ( l- alanine and l -leucine). While amino and carboxyl groups are required for transport, solutes do not have to be α-amino acids. Consistent with this, Bra Rl is the first ABC transporter to be shown to transport γ-aminobutyric acid (GABA). All previously identified bacterial GABA transporters are secondary carriers of the amino acid-polyamine-organocation (APC) superfamily. Also, transport by Bra Rl does not appear to be stereospecific as d amino acids cause significant inhibition of uptake of l -glutamate and l -leucine. Unlike all other solutes tested, l -alanine uptake is not dependent on solute binding protein BraC Rl . Therefore, a second, unidentified solute binding protein may interact with the BraDEFG Rl membrane complex during l -alanine uptake. Overall, the data indicate that Bra Rl is a general amino acid permease of the HAAT family. Furthermore, Bra Rl has the broadest solute specificity of any characterized bacterial amino acid transporter." @default.
- W2162222799 created "2016-06-24" @default.
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- W2162222799 date "2002-08-01" @default.
- W2162222799 modified "2023-09-25" @default.
- W2162222799 title "<i>Rhizobium leguminosarum</i> Has a Second General Amino Acid Permease with Unusually Broad Substrate Specificity and High Similarity to Branched-Chain Amino Acid Transporters (Bra/LIV) of the ABC Family" @default.
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- W2162222799 doi "https://doi.org/10.1128/jb.184.15.4071-4080.2002" @default.
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