ArticleProceedings of the National Academy of Sciences of the United States of America2009
An aspartate and a water molecule mediate efficient acid-base catalysis in a tailored antibody pocket.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 23 citations in OpenAlex.
- Comprehensive Characterization of a Novel Broad-Host-Range LyticAntibiotics (Basel, Switzerland) · 2026Article
- NMR-guided directed evolution.Nature · 2022Article
- Protein Flexibility and Stiffness Enable Efficient Enzymatic Catalysis.Journal of the American Chemical Society · 2019Article
- Aromatic interactions at the ligand-protein interface: Implications for the development of docking scoring functions.Chemical biology & drug design · 2018Article
- Synthetic, Switchable Enzymes.Journal of molecular microbiology and biotechnology · 2017Review
- Computational strategies for the design of new enzymatic functions.Archives of biochemistry and biophysics · 2015Review
- BIOPHYSICS. Response to Comments on "Extreme electric fields power catalysis in the active site of ketosteroid isomerase".Science (New York, N.Y.) · 2015Article
- Catalytic efficiency of designed catalytic proteins.Current opinion in structural biology · 2014Review
- A single mutation in a regulatory protein produces evolvable allosterically regulated catalyst of nonnatural reaction.Angewandte Chemie (International ed. in English) · 2013Article
- Bridging the gaps in design methodologies by evolutionary optimization of the stability and proficiency of designed Kemp eliminase KE59.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Challenges and advances in validating enzyme design proposals: the case of kemp eliminase catalysis.Biochemistry · 2011Article
- Exploring challenges in rational enzyme design by simulating the catalysis in artificial kemp eliminase.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
Design of catalysts featuring multiple functional groups is a desirable, yet formidable goal. Antibody 13G5, which accelerates the cleavage of unactivated benzisoxazoles, is one of few artificial enzymes that harness an acid and a base to achieve efficient proton transfer. X-ray structures of the Fab-hapten complexes of wild-type 13G5 and active-site variants now afford detailed insights into its mechanism. The parent antibody preorganizes Asp(H35) and Glu(L34) to abstract a proton from substrate and to orient a water molecule for leaving group stabilization, respectively. Remodeling the environment of the hydrogen bond donor with a compensatory network of ordered waters, as seen in the Glu(L34) to alanine mutant, leads to an impressive 10(9)-fold rate acceleration over the nonenzymatic reaction with acetate, illustrating the utility of buried water molecules in bifunctional catalysis. Generalization of these design principles may aid in creation of catalysts for other important chemical transformations.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.