A direct NMR method for the measurement of competitive kinetic isotope effects

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DOIResolve DOI: http://doi.org/10.1038/nchembio.352
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TypeArticle
Journal titleNature Chemical Biology
Volume6
Issue6
Pages405407; # of pages: 3
AbstractWe present a technique that uses 13C NMR spectroscopy to measure kinetic isotope effects on the second-order rate constant (kcat/Km) for enzyme-catalyzed reactions. Using only milligram quantities of isotopically labeled substrates, precise competitive KIEs can be determined while following the ongoing reaction directly in a NMR spectrometer. Our results for the Vibrio cholerae sialidase–catalyzed hydrolysis of natural substrate analogs support a concerted enzymatic transition state for these reactions.
Publication date
LanguageEnglish
AffiliationNRC Institute for Biological Sciences; National Research Council Canada
Peer reviewedYes
NPARC number17508456
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Record identifierbba963ff-3658-4b34-8e52-9111ef6a3296
Record created2011-03-30
Record modified2016-05-09
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