Fluorescence and F-19 NMR evidence that phenylalanine, 3-L-fluorophenylalanine and 4-L-fluorophenylalanine bind to the L-leucine specific receptor ofEscherichia coli

Citation
La. Luck et C. Johnson, Fluorescence and F-19 NMR evidence that phenylalanine, 3-L-fluorophenylalanine and 4-L-fluorophenylalanine bind to the L-leucine specific receptor ofEscherichia coli, PROTEIN SCI, 9(12), 2000, pp. 2573-2576
Citations number
13
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Biochemistry & Biophysics
Journal title
PROTEIN SCIENCE
ISSN journal
0961-8368 → ACNP
Volume
9
Issue
12
Year of publication
2000
Pages
2573 - 2576
Database
ISI
SICI code
0961-8368(200012)9:12<2573:FAFNET>2.0.ZU;2-V
Abstract
The binding capacity of the L-leucine receptor from Escherichia coli was me asured with L-phenylalanine and 4-fluoro-L-phenylalanine as substrates by f luorescence. The apparent dissociation constants (K-D) for L-leucine, L-phe nylalanine, and 4-fluoro-L-phenylalanine are 0.40. 0.18. and 0.26 respectiv ely. F-19 NMR data show protein-induced shifts for the 4-fluoro-L-phenylala nine peak and 3-fluoro-L-phenylalanine when receptor is present. Evidence p oints to the binding of only the L-isomers of these fluorine analogs.