PMID:8340375
| Citation |
Kumar, GB and Black, PN (1993) Bacterial long-chain fatty acid transport. Identification of amino acid residues within the outer membrane protein FadL required for activity. J. Biol. Chem. 268:15469-76 |
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| Abstract |
The outer membrane protein FadL (product of the fadL gene) of Escherichia coli is required for the specific binding and transport of exogenous long-chain fatty acids prior to metabolic utilization. The carboxyl end of FadL has been proposed to play a crucial role by facilitating the transport of long-chain fatty acids. In an attempt to define specific amino acid residues within carboxyl region of FadL essential for activity, a series of deletion and point mutations within the 3' end of the fadL+ gene have been constructed and characterized. These fadL mutants were classified into three categories based on functional properties attributable to the altered FadL proteins: (i) those that had essentially wild-type levels of long-chain fatty acid binding and transport, (ii) those that had wild-type levels of long-chain fatty acid binding but were defective in transport, and (iii) those that were defective for both long-chain fatty acid binding and transport. These findings demonstrate that amino acid residues Phe448, Pro428, Val410, and Ser397 are required for optimal levels of long-chain fatty acid transport and that amino acid residues Pro428 and Val410 are essential for long-chain fatty acid binding. |
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| Keywords |
Amino Acid Sequence; Amino Acids/metabolism; Bacterial Outer Membrane Proteins/chemistry; Bacterial Outer Membrane Proteins/metabolism; Biological Transport; Cell Membrane/metabolism; Escherichia coli/metabolism; Escherichia coli Proteins; Fatty Acid Transport Proteins; Fatty Acids/metabolism; Molecular Sequence Data; Mutagenesis, Site-Directed; Point Mutation; Sequence Deletion; T-Phages/physiology |
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