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• W2740985112 endingPage "83" @default.
• W2740985112 startingPage "43" @default.
• W2740985112 abstract "Enzyme isotope effects, or the kinetic effects of “heavy” enzymes, refer to the effect of isotopically labeled protein residues on the enzyme's activity or physical properties. These effects are increasingly employed in the examination of the possible contributions of protein dynamics to enzyme catalysis. One hypothesis assumed that isotopic substitution of all 12C, 14N, and nonexchangeable 1H by 13C, 15N, and 2H, would slow down protein picosecond to femtosecond dynamics without any effect on the system's electrostatics following the Born–Oppenheimer approximation. It was suggested that reduced reaction rates reported for several “heavy” enzymes accords with that hypothesis. However, numerous deviations from the predictions of that hypothesis were also reported. Current studies also attempt to test the role of individual residues by site-specific labeling or by labeling a pattern of residues on activity. It appears that in several systems the protein's fast dynamics are indeed reduced in “heavy” enzymes in a way that reduces the probability of barrier crossing of its chemical step. Other observations, however, indicated that slower protein dynamics are electrostatically altered in isotopically labeled enzymes. Interestingly, these effects appear to be system dependent, thus it might be premature to suggest a general role of “heavy” enzymes’ effect on catalysis." @default.
• W2740985112 created "2017-08-08" @default.
• W2740985112 creator A5010894256 @default.
• W2740985112 creator A5040981658 @default.
• W2740985112 creator A5042711695 @default.
• W2740985112 date "2017-01-01" @default.
• W2740985112 modified "2023-10-11" @default.
• W2740985112 title "Measurement of Enzyme Isotope Effects" @default.
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• W2740985112 doi "https://doi.org/10.1016/bs.mie.2017.06.033" @default.
• W2740985112 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28911779" @default.
• W2740985112 hasPublicationYear "2017" @default.
• W2740985112 type Work @default.

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