| DOI | Resolve DOI: https://doi.org/10.1038/nchembio.352 |
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| Author | Search for: Chan, Jefferson; Search for: Lewis, Andrew R.; Search for: Gilbert, Michel1; Search for: Karwaski, Marie-France1; Search for: Bennet, Andrew J. |
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| Affiliation | - National Research Council of Canada. NRC Institute for Biological Sciences
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| Format | Text, Article |
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| Abstract | We 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. |
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| Publication date | 2010-06-01 |
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| In | |
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| Language | English |
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| Peer reviewed | Yes |
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| NPARC number | 17508456 |
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| Export citation | Export as RIS |
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| Report a correction | Report a correction (opens in a new tab) |
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| Record identifier | bba963ff-3658-4b34-8e52-9111ef6a3296 |
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| Record created | 2011-03-30 |
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| Record modified | 2020-04-17 |
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