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 sialidaseĝ€"catalyzed hydrolysis of natural substrate analogs support a concerted enzymatic transition state for these reactions.
Original language | English (US) |
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Pages (from-to) | 405-407 |
Number of pages | 3 |
Journal | Nature chemical biology |
Volume | 6 |
Issue number | 6 |
DOIs | |
State | Published - Jun 2010 |
Externally published | Yes |
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology