Observing enzyme ternary transition state analogue complexes by ¹⁹F NMR spectroscopy.

ABSTRACT: 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 ¹⁹F NMR spectroscopy. In these complexes MgF₃^- and AlF₄^- are surrogates for the transferring phosphate. However, the relevance of these metal fluorides as TSA complexes has been queried. The 1D ¹⁹F 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

SUBMITTER: Ampaw A 

PROVIDER: S-EPMC5863612 | biostudies-literature | 2017 Dec

REPOSITORIES: biostudies-literature