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pubmed-article:11822454pubmed:abstractTextAntibody 38C2 efficiently catalyzes deuterium-exchange reactions at the alpha 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.lld:pubmed
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pubmed-article:11822454pubmed:dateRevised2009-8-4lld:pubmed
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pubmed-article:11822454pubmed:articleTitleHighly efficient antibody-catalyzed deuteration of carbonyl compounds.lld:pubmed
pubmed-article:11822454pubmed:affiliationDepartment of Chemistry and Institute of Catalysis Science and Technology, Technion-Israel Institute of Technology Technion City, Haifa.lld:pubmed
pubmed-article:11822454pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:11822454pubmed:publicationTypeComparative Studylld:pubmed
pubmed-article:11822454pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed