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For the record: Fluorescence and 19 F NMR evidence that phenylalanine, 3‐L‐fluorophenylalanine and 4‐L‐fluorophenylalanine bind to the L‐leucine specific receptor of Escherichia coli
Author(s) -
Luck Linda A.,
Johnson Colin
Publication year - 2000
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.9.12.2573
Subject(s) - phenylalanine , chemistry , leucine , dissociation constant , escherichia coli , stereochemistry , receptor , amino acid , biochemistry , gene
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.