Probing the transition states of four glucoside hydrolyses with 13C kinetic isotope effects measured at natural abundance by NMR spectroscopy.
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Advances in kinetic isotope effect measurement techniques for enzyme mechanism studyEnzymatic transition states, transition-state analogs, dynamics, thermodynamics, and lifetimesMechanistic studies of 1-aminocyclopropane-1-carboxylate deaminase: characterization of an unusual pyridoxal 5'-phosphate-dependent reaction.Free energy study of the catalytic mechanism of Trypanosoma cruzi trans-sialidase. From the Michaelis complex to the covalent intermediate.Dissecting the mechanisms of a class of chemical glycosylation using primary ¹³C kinetic isotope effectsMechanistic evidence for a front-side, SNi-type reaction in a retaining glycosyltransferase.Sensitive and Accurate 13C Kinetic Isotope Effect Measurements Enabled by Polarization Transfer.A potent bicyclic inhibitor of a family 27 alpha-galactosidase.
P2860
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P2860
Probing the transition states of four glucoside hydrolyses with 13C kinetic isotope effects measured at natural abundance by NMR spectroscopy.
description
2004 nî lūn-bûn
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name
Probing the transition states ...... abundance by NMR spectroscopy.
@en
Probing the transition states ...... abundance by NMR spectroscopy.
@nl
type
label
Probing the transition states ...... abundance by NMR spectroscopy.
@en
Probing the transition states ...... abundance by NMR spectroscopy.
@nl
prefLabel
Probing the transition states ...... abundance by NMR spectroscopy.
@en
Probing the transition states ...... abundance by NMR spectroscopy.
@nl
P2093
P356
P1476
Probing the transition states ...... abundance by NMR spectroscopy.
@en
P2093
Alex D Bain
Jason K Lee
Paul J Berti
P304
P356
10.1021/JA0394028
P407
P577
2004-03-01T00:00:00Z