Catalytic antibodies with lipase activity and R or S substrate selectivity.
The specific hydrolysis of unactivated esters bearing an R or S enantiomeric alcohol has been achieved by two separate classes of catalytic antibodies induced to bind either the R or S substrates. The antibodies exhibit rate accelerations (10(3) to 10(5] above background hydrolysis that, coupled with their antipodal specificity, provide a novel set of reagents for use in synthesis.
Janda
K D
KD
Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, CA 92037.
Benkovic
S J
SJ
Lerner
R A
RA
D000818:Animals; D000911:Antibodies, Monoclonal / Q000276:immunology; D000918:Antibody Specificity; D000941:Antigens / Q000276:immunology; D001592:Benzyl Alcohols / Q000378:metabolism; D002384:Catalysis; D004952:Esters / Q000378:metabolism; D006241:Haptens; D006433:Hemocyanins / Q000276:immunology; D006868:Hydrolysis; D007114:Immunization; D007700:Kinetics; D008049:Lipase / Q000378:metabolism*; D051379:Mice; D008805:Mice, Inbred A; D015394:Molecular Structure; D063065:Organophosphonates / Q000276:immunology; D013237:Stereoisomerism; D013379:Substrate Specificity
D000911:Antibodies, Monoclonal; D000941:Antigens; D001592:Benzyl Alcohols; D004952:Esters; D006241:Haptens; D063065:Organophosphonates; D006433:Hemocyanins; C002017:methylphenyl carbinol; D008049:Lipase; C032808:keyhole-limpet hemocyanin