Work

For the record: Fluorescence and 19F NMR evidence that phenylalanine, 3‐L‐fluorophenylalanine and 4‐L‐fluorophenylalanine bind to the L‐leucine specific receptor of Escherichia coli

Year: 2000

Type: article

Abstract: The binding capacity of the L-leucine receptor from Escherichia coli was measured with L-phenylalanine and 4-fluoro-L-phenylalanine as substrates by fluorescence. The apparent dissociation constants (KD) for L-leucine, L-phenylalanine, and 4-fluoro-L-phenylalanine are 0.40, 0.18, and 0.26 respectively. 19F NMR data show protein-induced shifts for the 4-fluoro-L-phenylalanine peak and 3-fluoro-L-phenylalanine when receptor is present. Evidence points to the binding of only the L-isomers of these fluorine analogs.

Source: Protein Science

DOI: 10.1110/ps.9.12.2573

Authors: Linda A. Luck, Colin Johnson

Institution: Clarkson University

Language: English

Topic: Amino Acid Enzymes and Metabolism

Subfield: Biochemistry

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

Funder: American Chemical Society Petroleum Research Fund

OpenAlex ID: W1971360166

FWCI: 0.699

Cites: 13

Cited by: 14

Related to: 10