ArticleProceedings of the National Academy of Sciences of the United States of America1993
A genetic approach to the generation of antibodies with enhanced catalytic activities.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 54 citations in OpenAlex.
- Computational design of catalytic dyads and oxyanion holes for ester hydrolysis.Journal of the American Chemical Society · 2012Article
- Bringing biological solutions to chemical problems.Proceedings of the National Academy of Sciences of the United States of America · 1998Article
- In vivo versus in vitro screening or selection for catalytic activity in enzymes and abzymes.Molecular biotechnology · 1997Review
- On the failure of de novo-designed peptides as biocatalysts.Proceedings of the National Academy of Sciences of the United States of America · 1996Review
- Expression studies of catalytic antibodies.Proceedings of the National Academy of Sciences of the United States of America · 1995Article
- Selection of catalytic antibodies for a biosynthetic reaction from a combinatorial cDNA library by complementation of an auxotrophic Escherichia coli: antibodies for orotate decarboxylation.Proceedings of the National Academy of Sciences of the United States of America · 1994Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
A hydrolytic catalytic antibody, generated against a nitrophenyl phosphonate transition state analogue, has been cloned and expressed in Escherichia coli for use as a model system to demonstrate the feasibility of using genetic selections to enhance catalytic activity. Conditions were found that permit the secretion of active recombinant antibody into the periplasm of a strain of E. coli deficient in the biotin biosynthetic genes (delta bio-gal). A number of substrates were synthesized that, upon hydrolysis by the antibody, yield free biotin, which is required for cell growth. The substrates and selections can be used to identify mutants of the antibody with altered activities. This approach should be generalizable to a wide number of hydrolytic reactions including the selective cleavage of peptide, polysaccharide, phosphodiester, and ester bonds.
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