Antibody-catalysed peptide nitroanilide hydrolysis using a new type of hapten

Biocatalysis and Biotransformation

Volumn 16, Issue 4, 1998, Pages 307-316

  Yomtova, V M ^a   Kyurkchiev, S D ^b   Slavcheva, N N ^a   Ivanov, I P ^c  

^a INSTITUTE OF ORGANIC CHEMISTRY   (Bulgaria)

^b BULGARIAN ACADEMY OF SCIENCES   (Bulgaria)

^c UNIVERSITY OF SOFIA   (Bulgaria)

Author keywords

Abzyme; Nitroanilide hydrolysis; Peptide aldehyde hapten; Substrate specificity

Indexed keywords

ANILIDE; BOVINE SERUM ALBUMIN; HAPTEN; MONOCLONAL ANTIBODY; PEPTIDE; SEMICARBAZONE; TRYPSIN;

ARTICLE; CATALYSIS; CONTROLLED STUDY; ENZYME SPECIFICITY; HYDROLYSIS; IMMUNIZATION; PROTEIN DEGRADATION;

BOVINAE;

EID: 0032413754     PISSN: 10242422     EISSN: None     Source Type: Journal    
DOI: 10.3109/10242429809003624     Document Type: Article

References (36)

1. Asboth, B. and Polgar, L. (1983) Transition-state stabilization at the oxyanion binding sites of serine and thiol proteinases: Hydrolysis of thiono and oxygen esters. Biochemistry, 22, 117-122.
2. Atassi, M.Z., Kazim, A.L. and Sakata, S. (1981) High yield coupling of peptides to protein carriers. Biochimica Biophysica Acta, 670, 300-302.
3. Bajusz, S., Barabas, E., Tolnay, P., Szell, E. and Bagdy, D. (1978) Inhibition of thrombin and trypsin by tripeptide aldehydes. International Journal of Pep title and Protein Research, 12, 217-221.
4. Bizzozero, S.A. and Zweifel, B.O. (1975) The importance of the conformation of the tetrahedral intermediate for the α-chymotrypsin-catalyzed hydrolysis of peptide substrates. FEBS Letters, 59, 105-108.
5. Blackburn, G.M. and Deng, S. (1993) Catalytic antibodies for the hydrolysis of unactivated peptides. Biochemical Society Transactions, 21, 1102-1107.
6. Charbonnier, J.-B., Carpenter, E., Gigant, B., Gollinelli-Pimpeau, B., Esshar, Z., Green, B.S. and Knossow, M. (1995) Crystal structure of the complex of a catalytic antibody Fab fragment with a transition state analog: structural similarities in esterase-like catalytic antibodies. Proceedings of the National Academy of Sciences USA, 92, 11721-11725.
7. Gibian, H. and Schröder, E. (1961) Synthesen von arginin-haltigen peptiden. Annalen der Chemie, 642, 145-162.
8. Guo, J., Huang, W. and Scanlan, T. (1994) Kinetic and mechanistic characterization of an efficient hydrolytic antibody: evidence for the formation of an acyl intermediate. Journal of the American Chemical Society, 116, 6062-6069.
9. Iverson, B.L. and Lerner, R.A. (1989) Sequence specific peptide cleavage catalyzed by an antibody. Science, 243, 1184-1188.
10. Janda, K.D., Schloeder, D., Bencovic, S.J. and Lerner, R.A. (1988) Induction of an antibody that catalyzes the hydrolysis of an amide bond. Science, 241, 1188-1191.
11. Janda, K.D., Bencovic, S.J., McLeod, D.A., Schloeder, D.M. and Lerner, R.A. (1991) Substrate attenuation: an approach to improve antibody catalysis. Tetrahedron, 47, 2503-2506.
12. Jencks, W.P. (1969) In Catalysis in Chemistry and Enzymology, McGraw-Hill, NY.
13. Kennedy, W.P. and Schultz, R.M. (1979). Mechanism of association of a specific aldehyde "Transition-State Analogue" to the active site of α-chymotrypsin. Biochemistry, 18, 349-356.
14. Kirby, A.J. (1996) Enzyme mechanisms, models and mimics. Angewandte Chemie (Int. Edn in English) 35, 706-723.
15. Kitazume, T., Lin, J.T., Yamamoto, T. and Yamazaki, T. (1991) Stereoselective synthesis of fluorinated materials catalyzed by an antibody. Journal of the American Chemical Society 113, 2123-2126.
16. Köhler, G. and Milstein, C. (1975) Continuous cultures of fused cells secreting antibody of predefined specificity. Nature, 256, 495-497.
17. Lewis, C.A. Jr. and Wolfend, R. (1977) Thiochemiacetal formation by inhibitory aldehydes at the active site of papain. Biochemistry, 16, 4890-4895.
18. Lowry, O.H., Rosebrough, N.J., Farr, A.L. and Randall, R.J. (1951) Protein measurement with the folin phenol reagent. The Journal Biological Chemistry, 193, 265-275.
19. MacBeath, G. and Hilvert, D. (1996) Hydrolytic antibodies: variations on a theme, Chem. Biol., 3, 433-445.
20. Martin, M.T., Napper, A.D., Schultz, P.G. and Rees, A.R. (1991) Mechanistic studies of tyrosine-dependant catalytic antibody Biochemistry, 30, 9757-9761.
21. McConnell, R.M., Barnes, G.E., Hoyng, C.F. and Gunn, J.M. (1990) New leupeptin analogues: synthesis and inhibition data. Journal of Medicinal Chemistry, 33, 86-93.
22. Oritz, C., Tellier, C., Williams, H., Stolowich, N.J. and Scott, A.I. (1991) Diastereotopic covalent binding of the natual inhibitor leupeptin to trypsin: detection of two interconverting hemiacetals by solution and solid-state NMR spectroscopy Biochemistry, 30, 10026-10034.
23. Patel, A.H., Ahsan, A., Suthar, B.P. and Schultz, R.M. (1983) Transition-state affinity chromatography of trypsin-like proteinases with dipeptidyl argininal ligands. Biochimica Biophysica Acta, 748, 321-330.
24. L fragment J. Biol. Chem. 270, 15257-15261.
25. Paul, S., Volle, D.J., Beach, C.M., Johnson, D.R., Powell, M.J. and Massey, R.J. (1989) Catalytic hydrolysis of vasoactive intestinal peptide by human autoantibody. Science, 244, 1158-1162.
26. Penninckx, M. and Gigot, D. (1979) Synthesis of a peptide form of N-δ-(phosphonoacetyl)-L-ornithine. J. Biol. Chem., 254(14), 6392-6396.
27. Pollack, S.J., Jacobs, J.W. and Schultz, P.G. (1986) Selective chemical catalysis by an antibody. Science, 234, 1570-157.
28. Schultz, R.M., Varma-Nelson, P., Oritz, R., Kozlowski, K.A., Orawski, A.T., Pagast, P. and Frankfater, A. (1989) 1507 Active and inactive forms of the transition-state analog protease inhibitor leupeptin: explanation of the observed slow binding of leupeptin to cathepsin B and papain. The Journal of Biological Chemistry, 264, 1497-1507.
29. 13C NMR spectroscopy of "Transition-State Analogue" complexes of N-acetyl-L-phenylalanina and α-chymotrypsin. Journal of the American Chemical Society, 106, 4272-4273.
30. Shimizu, B., Saito, A., Ito, A. and Tokawa, K. (1972) Synthetic studies of leupeptins and their analogs. Journal of Antibiotics, 25(9), 515-523.
31. Taira, K. and Gorenstein, D.G. (1987) Stereoelectronic effects in serine proteases: ab initio molecular orbital calculations. Bulletin of the Chemical Society of Japan, 60, 3625-3632.
32. Tawfik, D.S., Zemel, R.R., Arad-Yellin, R., Green, B.S. and Eshhar, Z. (1990) A simple method of selecting catalytic monoclonal antibodies that exhibit turnover and specificity. Biochemistry, 29, 9916-9921.
33. Thomas, N.R. (1994) Hapten design for the generation of catalytic antibodies. Applied Biochemistry and Biotechnology, 47, 345-370.
34. Thompson, R.C. (1973) Use of peptide aldehydes to generate transition-state analogs of elastase. Biochemistry, 12, 47-51.
35. Tramontano, A., Janda, K.D. and Lerner, R.A. (1986), Catalytic antibodies. Science 234, 1566-1570.
36. Wells, J.A. and Estell, D.A. (1988) Subtilisin - an enzyme designed to be engineered. Trends in Biochemical Sciences, 13, 291-297.