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Observing enzyme ternary transition state analogue complexes by 19F NMR spectroscopyElectronic supplementary information (ESI) available: Supporting Figures, HQSC NMR spectra, LC-MS/MS data and X-ray diffraction refinement data are described. See DOI: 10.1039/c7sc04204c
Erscheinungsjahr
2017-11
Quelle
EZB Electronic Journals Library
Beschreibungen/Notizen
Ternary transition state analogue (TSA) complexes probing the isomerization of β-
d
-glucose 1-phosphate (G1P) into
d
-glucose 6-phosphate (G6P) catalyzed by catalytically active, fluorinated (5-fluorotryptophan), β-phosphoglucomutase (βPGM) have been observed directly by
19
F NMR spectroscopy. In these complexes MgF
3
−
and AlF
4
−
are surrogates for the transferring phosphate. However, the relevance of these metal fluorides as TSA complexes has been queried. The 1D
19
F spectrum of a ternary TSA complex presented a molar equivalence between fluorinated enzyme, metal fluoride and non-isomerizable fluoromethylenephosphonate substrate analogue. Ring flips of the 5-fluoroindole ring remote from the active site were observed by both
19
F NMR and X-ray crystallography, but did not perturb function. This data unequivocally demonstrates that the concentration of the metal fluoride complexes is equivalent to the concentration of enzyme and ligand in the TSA complex in aqueous solution.
Ternary transition state analogue (TSA) complexes probing the isomerization of β-
d
-glucose 1-phosphate (G1P) into
d
-glucose 6-phosphate (G6P) catalyzed by catalytically active, fluorinated (5-fluorotryptophan), β-phosphoglucomutase (βPGM) have been observed directly by
19
F NMR spectroscopy.
Sprache
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Identifikatoren
ISSN: 2041-6520
eISSN: 2041-6539
DOI: 10.1039/c7sc04204c
Titel-ID: cdi_rsc_primary_c7sc04204c
Format
–
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