Publication Type : Journal Article
Thematic Areas : Biotech
Publisher : Journal of Biological Chemistry
Source : Journal of Biological Chemistry, ASBMB, Volume 268, Issue 21, p.15469–15476 (1993)
Url : https://pubmed.ncbi.nlm.nih.gov/8340375/
Campus : Amritapuri
School : School of Biotechnology
Center : Cell Biology
Department : biotechnology
Year : 1993
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.
Cite this Research Publication : Dr. Geetha Kumar and Black, P. N., “Bacterial long-chain fatty acid transport. Identification of amino acid residues within the outer membrane protein FadL required for activity.”, Journal of Biological Chemistry, vol. 268, no. 21, pp. 15469–15476, 1993.