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- W2158166139 abstract "Antibody 38C2 efficiently catalyzes deuterium-exchange reactions at the α position of a variety of ketones and aldehydes, including substrates that have a variety of sensitive functional groups. In addition to the regio- and chemoselectivity of these reactions, the catalytic rates (kcat) and rate-enhancement values (kcat/kun) are among the highest values ever observed with catalytic antibodies. Comparison of the substrate range of the catalytic antibody with highly evolved aldolase enzymes, such as rabbit-muscle aldolase, highlights the much broader practical scope of the antibody, which accepts a wide range of substrates. The hydrogen-exchange reaction was used for calibration and mapping of the antibody active site. Isotope-exchange experiments with cycloheptanone reveal that the formation of the Schiff base species (as concluded from the 16O/18O exchange rate at the carbonyl oxygen) is much faster than the formation of the enamine intermediate (as concluded from the H/D exchange rate), and both steps are faster than the antibody-catalyzed aldol addition reaction." @default.
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- W2158166139 date "2002-01-04" @default.
- W2158166139 modified "2023-10-16" @default.
- W2158166139 title "Highly Efficient Antibody-Catalyzed Deuteration of Carbonyl Compounds" @default.
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- W2158166139 doi "https://doi.org/10.1002/1521-3765(20020104)8:1<229::aid-chem229>3.0.co;2-p" @default.
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