Abstract
Enzymes make complex life possible. With very few exceptions, each of the tens of thousands of chemical reactions that sustain living systems takes place quickly and smoothly through the action of a specific enzyme. The high rates and selectivities of enzymes make them ideal catalysts for in vitro processes, as well, and they are being utilized increasingly in research, industry, and medicine.
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References
E. A. Kabat, “Structural Concepts in Immunology and Immunochemistry,” Holt, Reinhart and Winston, New York, 1976.
D. Pressman and A. Grossberg, “The Structural Basis of Antibody Specificity,” Benjamin, New York, 1968
A. Nisonoff, J. Hopper and S. Spring, “The Antibody Molecule,” Academic Press, New York, (1975).
L. Pauling, Chemical achievement and hope for the future, Amer. Sci. 36:51 (1948).
W. P. Jencks, “Catalysis in Chemistry and Enzymology,” McGraw Hill, New York, p.288 (1969).
R. Wolfenden, Transition state analog inhibitors and enzyme catalysis, Ann. Rev. Biophys. Bioeng. 5:271 (1976).
G. E. Lienhard, Enzymatic catalysis and transition-state theory, Science 180:149 (1973).
J. Sauer, Diels-Alder reactions: New preparative aspects, Angew. Chem., Int. Ed. Engl. 5:211 (1966); Diels-Alder reactions: The reaction mechanism, ibid. 6:16 (1967).
A. Wassermann, “Diels-Alder Reactions”, Elsevier Publ. Co.; Amsterdam, (1965).
M. I. Page and W. P. Jencks, Entropic contributions to rate accelerations in enzymic and intramolecular reactions and the chelate effect, Proc. Nat. Acad. Sci. USA 68:1678 (1971).
W. P. Jencks, Binding energy, specificity, and enzymic catalysis: The Circe effect, Adv. Enzymol. 43:219 (1975).
D. Hilvert, K. W. Hill, K. D. Nared, and M.-T. M. Auditor, Antibody catalysis of a Diels-Alder reaction, J. Am. Chem. Soc. 111:9261 (1989).
F. K. Brown and K. N. Houk, The STO-3G transition structure of the Diels-Alder reaction, Tetrahedron Lett. 25:4609 (1984).
F. E. Ziegler, The thermal aliphatic Claisen rearrangement, Chem. Rev. 88:1423 (1988).
R. P. Lutz, Catalysis of the Cope and Claisen rearrangements, Chem. Rev. 84:205 (1984).
P. R. Andrews, E. N. Cain, E. Rizzardo, and G. D. Smith, Rearrangement of chorismate to prephenate. Use of chorismate mutase inhibitors to define the transition state structure, Biochemistry 16:4848 (1977).
H. S.-I. Chao and G. A. Berchtold, Inhibition of chorismate mutase activity of chorismate mutase-prephenate dehydrogenase from Aerobacter aerogenes, Biochemistry 21:2778 (1982).
S. G. Sogo, T. S. Widlanski, J. H. Hoare, C. E. Grimshaw, G. A. Berchthold, and J. R. Knowles, Stereochemistry of the rearrangement of chorismate to prephenate: Chorismate mutase involves a chair transition state, J. Am. Chem. Soc. 106:2701 (1984).
P. A. Bartlett and C. R. Johnson, An inhibitor of chorismate mutase resembling the transition-state conformation, J. Am. Chem. Soc. 107:7792 (1985).
D. Hilvert, S. H. Carpenter, K. D. Nared, and M.-T. M. Auditor, Catalysis of concerted reactions by antibodies: The Claisen rearrangement, Proc. Natl. Acad. Sci. USA 85:4953 (1988).
D. Y. Jackson, J. W. Jacobs, R. Sugasawara, S. H. Reich, P. A. Bartlett, and P. G. Schultz, An antibody-catalyzed Claisen rearrangement, J. Am. Chem. Soc. 110:4841 (1988).
D. Hilvert and K. D. Nared, Stereospecific Claisen rearrangement catalyzed by an antibody, J. Am. Chem. Soc. 110:5593 (1988).
A. Tramontano, K. D. Janda, and R. A. Lerner, Catalytic antibodies, Science 234:1566 (1986).
S. J. Pollack, J. W. Jacobs, and P. G. Schultz, Selective chemical catalysis by an antibody, Science 234:1570 (1986).
A. Tramontano, A. A. Ammann, and R. A. Lerner, Antibody catalysis approaching the activity of enzymes, J. Am. Chem. Soc. 110:2282 (1988).
K. D. Janda, S. J. Benkovic, and R. A. Lerner, Catalytic antibodies with lipase activity and R or S substrate selectivity, Science 244:437 (1989).
K. D. Janda, D. Schloeder, S. J. Benkovic, and R. A. Lerner, Induction of an antibody that catalyzes the hydrolysis of an amide bond, Science 241:1188 (1988)
B. L. Iverson, and R. A. Lerner, Sequence-specific peptide cleavage catalyzed by an antibody, Science. 243:1184 (1989).
S. Paul, D. J. Volle, C. M. Beach, D. J. Johnson, M. J. Powell, R. J. Massey, Catalytic hydrolysis of vasoactive intestinal peptide by human autoantibody, Science. 244:1158 (1989).
S. J. Benkovic, A. D. Napper, and R. A. Lerner, Catalysis of a stereospecific bimolecular amide synthesis by an antibody, Proc. Natl. Acad. Sci. USA 85:5355 (1988).
A. Balan, B. P. Doctor, B. S. Green, M. Torten, and H. Ziffer, Antibody combining sites as templates for selective organic chemical reactions, J. Chem. Soc., Chem. Commun. 106 (1988).
A. G. Cochran, R. Sugasawara, and P. G. Schultz, Photosensitized cleavage of a thymine dimer by an antibody, J. Am. Chem. Soc. 110:7888 (1988).
K. M. Shokat, C.J. Leumann, R. Sugasawara, and P. G. Schultz, An antibody-mediated redox reaction, Angew. Chem. Int. Ed. Engl. 27:1172 (1988).
N. Janjic and A. Tramontano, Antibody-catalyzed redox reaction, J. Am. Chem. Soc. 111:9109 (1989).
K. M. Shokat, C. J. Leumann, R. Sugasawara, and P. G. Schultz, A new strategy for the generation of catalytic antibodies, Nature (London) 338:269 (1989).
W. D. Huse, L. Sastry, S. A. Iverson, A. S. Kang, M. Alting-Mees, D. R. Burton, S. J. Benkovic, and R. A. Lerner, Generation of a large combinatorial library of the immunoglobulin repertoire in phage lambda, Science 246:1275 (1989).
S. J. Pollack, G. R. Nakayama, and P. G. Schultz, Introduction of nucleophiles and spectroscopic probes into antibody combining sites, Science 242:1038 (1988).
A. Skerra and A. Plückthun, Assembly of a functional immunoglobulin Fv fragment in Escherichia coli, Science 240:1038 (1988).
M. Better, C. P. Chang, R. R. Robinson, and A. H. Horwitz, Escherichia coli secretion of an active chimeric antibody fragment, Science 240:1041 (1988).
A. H. Horwitz, C. P. Chang, M. Better, K. E. Hellstrom, and R. R. Robinson, Secretion of functional antibody and Fab fragment from yeast cells, Proc. Natl. Acad. Sci. USA 85:8678 (1988).
J. R. Carlson, A new means of inducibly inactivating a cellular protein, Mol. Cell. Biol. 8:2638 (1988).
S. Roberts, J. C. Cheetham, and A. R. Rees, Generation of an antibody with enhanced affinity and specificity for its antigen by protein engineering, Nature (London) 328:731 (1987).
E. Baldwin, and P. G. Schultz, Generation of a catalytic antibody by site-directed mutagenesis, Science 245:1104 (1989).
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Hilvert, D. (1990). Catalytic Antibodies: Perspectives and Prospects. In: Baldwin, T.O., Raushel, F.M., Scott, A.I. (eds) Chemical Aspects of Enzyme Biotechnology. Industry-University Cooperative Chemistry Program Symposia. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-9637-7_10
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DOI: https://doi.org/10.1007/978-1-4757-9637-7_10
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