Antibody-Catalyzed Rearrangement of the Peptide Bond
- 30 October 1992
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 258 (5083), 803-805
- https://doi.org/10.1126/science.1439788
Abstract
The generation of antibodies from a bifunctional cyclic phosphinate transition-state analog provided agents capable of efficiently catalyzing both steps of the overall conversion of a substrate containing an asparaginyl-glycyl sequence through a succinimide intermediate to the products aspartyl-glycyl and the rearranged isoaspartyl-glycyl sequence. This reaction provides a potential means in addition to amide cleavage for the deactivation of protein or peptide biological functions in vivo.Keywords
This publication has 13 references indexed in Scilit:
- At the Crossroads of Chemistry and Immunology: Catalytic AntibodiesScience, 1991
- Nonenzymatic Deamidation of Asparaginyl and Glutaminyl Residues in ProteinCritical Reviews in Biochemistry and Molecular Biology, 1991
- Stereospecific hydrolysis of alkyl esters by antibodiesJournal of the American Chemical Society, 1989
- Catalytic Antibodies with Lipase Activity and R or S Substrate SelectivityScience, 1989
- Tertiary Structure Is a Principal Determinant to Protein DeamidationScience, 1988
- Propensity for spontaneous succinimide formation from aspartyl and asparaginyl residues in cellular proteinsInternational Journal of Peptide and Protein Research, 1987
- A Stereospecific Cyclization Catalyzed by an AntibodyScience, 1987
- The Mechanism of Irreversible Enzyme Inactivation at 100°CScience, 1985
- Molecular basis for the accumulation of acidic isozymes of triosephosphate isomerase on agingMechanisms of Ageing and Development, 1981
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970