Peptide aldehyde complexes with wheat serine carboxypeptidase II: Implications for the catalytic mechanism and substrate specificity

Journal of Molecular Biology

Volumn 255, Issue 5, 1996, Pages 714-725

  Bullock, Timothy L ^a,c   Breddam, Klaus ^b   Remington, S James ^a  

^a UNIVERSITY OF OREGON   (United States)

^b CARLSBERG LABORATORY   (Denmark)

^c MEDICAL RESEARCH COUNCIL   (United Kingdom)

Author keywords

Carboxypeptidase; Cryocrystallography; Enzyme mechanisms; Microbial peptidase inhibitors; Protein crystallography

Indexed keywords

ALDEHYDE; ANTIPAIN; ARGININE; CHYMOSTATIN; OXYGEN; SERINE; SERINE CARBOXYPEPTIDASE;

ARTICLE; COVALENT BOND; ENZYME ACTIVE SITE; ENZYME MECHANISM; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; GEOMETRY; HYDROGEN BOND; HYDROPHOBICITY; MOLECULAR MODEL; NONHUMAN; PRIORITY JOURNAL; STEREOCHEMISTRY; STEREOISOMERISM; WHEAT; X RAY CRYSTALLOGRAPHY;

TRITICUM SPP.;

EID: 0029912405     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1996.0058     Document Type: Article

References (44)

1. Aoyagi, T., Takeuchi, T., Matsuzaki, A., Kawamura, K., Kondo, S., Hamada, M. & Umezawa, H. (1969). Leupeptins, new protease inhibitors from Actinomyces. J. Antibiot. 22, 283-286.
2. Baker, E. N. & Hubbard, R. E. (1984). Hydrogen bonding in globular proteins. Prog. Biophys. Molec. Biol. 44, 97-179.
3. Bidlingmeyer, B. A., Cohen, S. A. & Tarvin, T. L. (1984). Rapid analysis of amino acids using pre-column derivatization. J. Chromatog. 336, 93-104.
4. Brayer, G. D., Delbaere, L. T. J., James, M. N. G., Bauer, C.-A. & Thompson, R. C. (1979). Crystallographic and kinetic investigations of the covalent complex formed by a specific tetrapeptide aldehyde and the serine protease from Streptomyces griseus. Proc. Natl Acad. Sci. USA, 76, 96-100.
5. Breddam, K. (1985). Enzymatic properties of malt carboxypeptidase II in hydrolysis and aminolysis reactions. Carlsberg Res. Commun. 50, 309-323.
6. Breddam, K. (1986). Serine carboxypeptidases. A review. Carlsberg Res. Commun. 51, 83-128.
7. Breddam, K., Sorensen, S. B. & Svendsen, I. (1987). Primary structure and enzymatic properties of carboxypeptidase II from wheat bran. Carlsberg Res. Commun. 52, 297-311.
8. Bullock, T. L., Branchaud, B. & Remington, S. J. (1994). Structure of the complex of 1-benzylsuccinate with wheat serine carboxypeptidase II at 2.0 A resolution. Biochemistry, 33, 11127-11134.
9. Burley S. K. & Petsko, G. A. (1985). Aromatic-aromatic interaction, a mechanism of protein structure stabilization. Science, 229, 23-28.
10. Carter, P. & Wells, J. A. (1988). Dissecting the catalytic triad of a serine protease. Nature, 332, 564-568.
11. Chen, R., Gorenstein, D. G., Kennedy W. P., Lowe, G., Nurse, D. & Schultz, R. M. (1979). Evidence for hemiacetal formation between N-acyl-L-phenylalanyls and alpha-chymotrypsin by cross-saturation nuclear magnetic resonance spectroscopy Biochemistry, 18, 921-926.
12. Delbaere, L. T. J. & Brayer, G. D. (1980). Structure of the complex formed between the bacterial-produced inhibitor chymostatin and the serine enzyme Streptomyces griseus protease A. J. Mol. Biol. 139, 45-51.
13. Delbaere, L. T. J. & Brayer, G. D. (1985). The 1.8 A structure of the complex between chymostatin and Streptomyces griseus protease A. A model for serine protease catalytic tetrahedral intermediates. J. Mol. Biol. 183, 89-103.
14. Douglas, K. T., Nakagawa, Y. & Kaiser, E. T. (1976). Mechanistic studies of carboxypeptidase Y. Kinetic detection of an acyl-enzyme intermediate in trimethylacetate esterase reaction. J. Am. Chem. Soc. 98, 8231-8236.
15. Endrizzi, J. E., Breddam, K. & Remington, S. J. (1994). 2.8 Å structure of yeast serine carboxypeptidase. Biochemistry, 33, 11106-11120.
16. Fowler, P. W. & Moore, G. J. (1988). Calculation of the magnitude and orientation of electrostatic interactions between small aromatic rings in peptides and proteins, implications for angiotensin II. Biochem. Biophys. Res. Commun. 153, 1296-1300.
17. Hayashi, R., Moore, S. & Stein, W. H. (1973). Serine at the active center of yeast carboxypeptidase. J. Biol. Chem. 248, 8366-8369.
18. Hayashi, R., Bai, Y. & Hata, T. (1975). Evidence for an essential histidine in carboxypeptidase Y. Reaction with the chloromethyl ketone derivative of benzyl-oxycarbonyl-L-phenylalanine. J. Biol. Chem. 250, 5221-5226.
19. Henderson, R. (1970). Structure of crystalline alpha-chymotrypsin. IV The structure of indoleacryloyl-alpha-chymotrypsin and its relevance to the hydrolytic mechanism of the enzyme. J. Mol. Biol. 54, 341-354.
20. Howard, A. J., Nielsen, C. & Xuong, N. H. (1985). Software for a diffractometer with multiwire area detector. Methods Enzymol. 114, 452-471.
21. Jones, T. A. (1978). A graphics model building and refinement system for macromolecules. J. Appl. Crystallog. 11, 268-272.
22. Kennedy W. P. & Shultz, R. M. (1979). Mechanism of association of a specific aldehyde "transition-state analogue" to the active site of alpha-chymotrypsin. Biochemistry, 18, 349-356.
23. Liao, D.-I. & Remington, S. J. (1990). Structure of wheat serine carboxypeptidase II at 3.5 A resolution. J. Biol. Chem. 265, 6528-6531.
24. Liao, D.-I., Breddam, K., Sweet, R. M., Bullock, T. & Remington, S. J. (1992). Refined atomic model of wheat serine carboxypeptidase II at 2.2 A resolution. Biochemistry, 31, 9796-9812.
25. Martin, B. M., Oliver, R. W. A., Johanssen, J. T. & Viswanatha, T. (1980). The carboxypeptidase Y catalyzed hydrolysis of indoleacryloylimidazole. Carlsberg Res. Commun. 45, 69-70.
26. Mortensen, U. H., Remington, S. J. & Breddam, K. (1994). Site-directed mutagenesis on (serine) carboxypeptidase Y A hydrogen bond network stabilizes the transition state by interaction with the C-terminal carboxylate group of the substrate. Biochemistry, 33, 508-517.
27. Ollis, D. L., Cheah, E., Cygler, M., Dijkstra, B., Frolow, F., Franken, S. M., Harel, M., Remington, S. J., Silman, I., Schrag, J., Sussman, J. L., Verschueren, K. H. G. & Goldman, A. (1992). The a/β hydrolase fold. Protein Eng. 5, 197-211.
28. Ortiz, C., Tellier, C., Williams, H., Stolowich, N. J. & Scott, I. A. (1991). Diasteriotopic covalent binding of the natural inhibitor leupeptin to trypsin, detection of two interconverting hemiacetals by solution and solid-state NMR spectroscopy Biochemistry, 30, 10026-10034.
29. Remington, S. J. & Breddam, K. (1994). Carboxypeptidases C and D. Methods Enzymol. 244, 231-248.
30. Schechter, I. & Berger, A. (1967). On the size of the active site of proteases. I. Papain. Biochem. Biophys. Res. Commun. 27, 157-162.
31. Segal, D. M., Cohen, G. H., Davies, D. R., Powers, J. C. & Wilcox, P E. (1971). The stereochemistry of substrate binding to chymotrypsin A. Cold Spring Harbor Symp. Quant. Biol. 36, 85-80.
32. Stein, R. L. & Strimpler, A. M. (1987). Slow-binding inhibition of chymotrypsin and cathepsin G by the peptide aldehyde chymostatin. Biochemistry, 26: 2611-2616.
33. Suda, H., Aoyagi, T., Hamada, M., Takeuchi, T. & Umezawa, H. (1972). Antipain, a new protease inhibitor isolated from actinomycetes. J. Antibiot. 25, 263-266.
34. Tatsuta, K., Mikami, N., Fujimoto, K., Umezawa, S., Umezawa, H. & Aoyagi, T. (1973). The structure of chymostatin, a chymotrypsin inhibitor. J. Antibiot. 26, 625-646.
35. Teng, T. Y. (1990). Mounting of crystals for macromolecular crystallography in a free-standing thin film. J. Appl. Crystallog. 23, 387-391.
36. Thompson, R. C. (1973). Use of peptide aldehydes to generate transition-state analogs of elastase. Biochemistry, 12, 47-51.
37. Tomkinson, N. P., Galpin, I. J. & Beynon, R. J. (1992). Synthetic analogues of chymostatin. Inhibition of chymotrypsin and Streptomyces griseus proteinase A. Biochem. J. 286, 475-480.
38. Tronrud, D. E., Ten Eyck, L. F. & Matthews, B. W. (1987). An efficient general-purpose least-squares refinement program for macromolecular structures. Acta Crystallog. sect. A, 43, 489-503.
39. Umezawa, H. (1976). Structures and activities of protease inhibitors of microbial origin. Methods Enzymol. 45, 678-695.
40. Umezawa, H., Aoyagi, T., Morishima, H., Kunimoto, S., Matsuzaki, M., Hamada, M. & Takeuchi, T. (1970). Chymostatin, a new chymotrypsin inhibitor produced by actinomycetes. J. Antibiot. 23, 425-427.
41. Umezawa, S., Tatsuta, K., Fujimoto, K., Tsuchiwa, T., Umezawa, H. & Naganawa, H. (1972). Structure of antipain, a new Sakaguchi-positive product of Streptomyces. J. Antibiot. 25, 267-270.
42. Umezawa, H., Aoyagi, T., Okura, A., Morishima, H., Takeuchi, T. & Okami, Y. (1973). Elastatinal, a new elastase inhibitor produced by actinomycetes. J. Antibiot. 26, 787-789.
43. Westerick, J. & Wolfendon, R. (1972). Aldehydes as inhibitors of papain. J. Biol. Chem. 247, 8195-8198.
44. Wilson, K. P., Liao, D., Bullock, T., Remington, S. J. & Breddam, K. (1990). Crystallization of serine carboxypeptidases. J. Mol. Biol. 221, 301-303.