| Literature DB >> 20418878 |
Jefferson Chan1, Andrew R Lewis, Michel Gilbert, Marie-France Karwaski, Andrew J Bennet.
Abstract
We present a technique that uses (13)C NMR spectroscopy to measure kinetic isotope effects on the second-order rate constant (k(cat)/K(m)) 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.Entities:
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Year: 2010 PMID: 20418878 DOI: 10.1038/nchembio.352
Source DB: PubMed Journal: Nat Chem Biol ISSN: 1552-4450 Impact factor: 15.040