| Literature DB >> 9241427 |
Abstract
Ten years have passed since the initial reports that antibodies could be programmed to have enzymatic activity by immunization with a transition-site analog. Much of the research over the last decade has focused on defining the scope and generality of antibody catalysis; however, during the past two years the first few crystal structures of catalytic antibody transition-state analogs have been reported. This review analyzes four such structures of catalytic antibodies that catalyze markedly different reactions, including ester hydrolysis, sulfide oxidation, and a pericyclic rearrangement. Structure-function relations for these catalysts are discussed and compared to the structure and function of natural enzymes, as well as the chemistry that occurs in solution.Entities:
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Year: 1997 PMID: 9241427 DOI: 10.1146/annurev.biophys.26.1.461
Source DB: PubMed Journal: Annu Rev Biophys Biomol Struct ISSN: 1056-8700