Inhibitors can activate proteases to catalyze the synthesis and hydrolysis of peptides

Biochemistry

Volumn 45, Issue 49, 2006, Pages 14567-14572

  Schechter, Israel ^a   Ziv, Etty ^a  

^a WEIZMANN INSTITUTE OF SCIENCE   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; BIOSYNTHESIS; CATALYSIS; CHEMICAL BONDS; HYDROLYSIS; PROTEINS;

INHIBITORS; INTERMEDIATE MOLECULES; PEPTIDE BONDS; PEPTIDES;

ENZYME INHIBITION;

ACYL GROUP; ADENOSINE TRIPHOSPHATE; CATHEPSIN S; FUNCTIONAL GROUP; PAPAIN; PEPTIDE; PROTEINASE; PROTEINASE INHIBITOR; THIOESTER; TRYPSIN;

ARTICLE; CATALYSIS; CHEMICAL BOND; DEGRADATION; ENERGY; ENZYME ACTIVATION; ENZYME INHIBITOR COMPLEX; ENZYME SUBSTRATE; PEPTIDE SYNTHESIS; PRIORITY JOURNAL; PROTEIN HYDROLYSIS;

BINDING, COMPETITIVE; DIPEPTIDES; ENZYME ACTIVATION; HYDROLYSIS; KINETICS; PAPAIN; PEPTIDE HYDROLASES; PEPTIDES; PROTEASE INHIBITORS; TRYPSIN;

EID: 33845382503     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi061910h     Document Type: Article

References (24)

1. Schechter, I., and Berger, A. (1967) On the size of the active site in proteases. I. Papain, Biochem. Biophys. Res. Commun. 27, 157-162.
2. Schechter, I., and Berger, A. (1968) On the size of the active site of proteases. III. Mapping the active site of papain: Specific peptide inhibitors of papain, Biochem. Biophys. Res. Commun. 32, 898-902.
3. Berger, A., and Schechter, I. (1970) Mapping the active site of papain with the aid of peptide substrates and inhibitors, Philos. Trans. R. Soc. London, Ser. B 257, 249-264.
4. Schechter, I. (2005) Mapping of the active site of proteases in the 1960s and rational design of inhibitors/drugs in the 1990s, Curr. Protein Pept. Sci. 6, 501-512.
5. Drenth, J., Jansonius, J. N., Koekoek, R., and Wolthers, B. G. (1971) The structure of papain, Adv. Protein Chem. 25, 79-115.
6. Drenth, J., Kalk, K. H., and Swen, H. M. (1976) Binding of chloromethyl ketone substrate analogues to crystalline papain, Biochemistry 15, 3731-3738.
7. Berger, A., Schechter, I., Benderly, H. A., and Kurn, N. (1971) Enzyme-inhibitor interaction as a model for biological recognition, in 10th European Peptide Symposium, pp 290-309, North-Holland Publishing Company, Amsterdam.
8. Wolthers, B. G., and Kalk, K. H. (1970) Binding of competitive (product) inhibitors to papain in the active and inactive state, Biochim. Biophys. Acta 198, 556-568.
9. Blumberg, S., Schechter, I., and Berger, A. (1970) The purification of papain by affinity chromatography, Eur. J. Biochem. 15, 92-102.
10. Smolarsky, M. (1978) Mechanism of action of papain: Aryldehydroalanines as spectroscopic probes of acyl enzyme formation, Biochemistry 17, 4606-4615.
11. Smolarsky, M. (1980) Mechanism of papain catalysis: Studies of active site acylation and deacylation by the stopped-flow technique, Biochemistry 19, 478-484.
12. Zur, M. (1975) Mapping the active site of a serine protease-trypsin, Ph.D. Thesis, The Weizmann Institute of Science, Rehovot, Israel.
13. Schechter, I., and Berger, A. (1966) Peptides of L- and D-alanine. Synthesis and optical rotations, Biochemistry 5, 3362-3370.
14. Schechter, I., and Berger, A. (1966) The hydrolysis of diastereoisomers of alanine peptides by carboxypeptidase A and aminopeptidase, Biochemistry 5, 3371-3375.
15. Fruton, J. S. (1949) The synthesis of peptides, Adv. Protein Chem. 5, 1-82.
16. Borsook, H. (1953) Peptide bond formation, Adv. Protein Chem. 8, 127-174.
17. Fruton, J. S. (1982) Proteinase-catalyzed synthesis of peptide bonds, Adv. Enzymol. 53, 239-306.
18. Blow, D. M., and Steitz, T. A. (1970) X-ray diffraction studies of enzymes, Annu. Rev. Biochem. 39, 63-100.
19. Johnson, L. N., Phillips, D. C., and Rupley, J. A. (1968) The activity of lysozyme: An interim review of crystallographic and chemical evidence, Brookhaven Symp. Biol. 21, 120-138.
20. Lipscomb, W. N., Hartsuck, J. A., Reeke, G. N., Quiocho, F., Bethge, P. A., Ludwig, M. L., Steitz, T. A., Muirhead, H., and Coppola, J. C. (1968) The structure of carboxypeptidase A. VII. The 2.0-Å resolution studies of the enzyme and of its complex with glycyltyrosine, and mechanistic deductions, Brookhaven Symp. Biol. 21, 24-90.
21. Behrens, O. K., and Bergmann, M. (1939) Cosubstrates in proteolysis, J. Biol. Chem. 129, 587-602.
22. Warren, E. H., Vigneron, N. J., Gavin, M. A., Coulie, P. G., Stroonbant, V., Dalet, A., Tycodi, S. S., Xuereb, S. M., Mito, J. K., Riddell, S. R., and Van den Eynde, B. J. (2006) An antigen produced by splicing of noncontiguous peptides in the reverse order, Science 313, 1444-1447.
23. Hershko, A., Heller, H., Elias, S., and Ciechanover, A. (1983) Components of ubiquitin-protein ligase system, J. Biol. Chem. 258, 8206-8214.
24. Volpe, J. J., and Vegelos, P. R. (1973) Saturated fatty acid biosynthesis and its regulation, Annu. Rev. Biochem. 42, 21-60.