Role of S'1 loop residues in the substrate specificities of pepsin A and chymosin

Biochemistry

Volumn 43, Issue 48, 2004, Pages 15122-15130

  Kageyama, Takashi ^a  

^a KYOTO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ENZYMES; MUTAGENESIS; PROTEINS; YEAST;

AROMATIC RESIDUES; MONKEY CHYMOSIN;

HYDROPHOBICITY;

CHYMOSIN; GLUTATHIONE TRANSFERASE; HYBRID PROTEIN; MUTANT PROTEIN; PEPSIN A;

AMINO ACID SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENZYME SPECIFICITY; ENZYME SUBSTRATE; HYDROGEN BOND; HYDROPHOBICITY; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS; YEAST;

AMINO ACID SEQUENCE; ANIMALS; CATTLE; CEBIDAE; CHYMOSIN; HUMANS; HYDROLYSIS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OLIGOPEPTIDES; PEPSIN A; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SUBSTRATE SPECIFICITY;

MAMMALIA; VECTORS;

EID: 10044263144     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi048440g     Document Type: Article

References (49)

1. Tang, J., Sepulveda, P., Marciniszyn, J., Jr., Chen, K. C., Huang, W. Y., Tao, N., Liu, D., and Lanier, J. P. (1973) Amino acid sequence of porcine pepsin, Proc. Natl. Acad. Sci. U.S.A. 70, 3437-3439.
2. Foltmann, B. (1981) Gastric proteinases-Structure, function, evolution, and mechanism of action. Essays Biochem. 17, 52-84.
3. Kageyama, T. (2002) Pepsinogens, progastricsins, and prochymosins: Structure, function, evolution, and development, Cell. Mol Life Sci. 59, 288-306.
4. Fruton, J. S. (2002) A history of pepsin and related enzymes, Q. Rev. Biol. 77, 127-147.
5. Kageyama, T., Tanabe, K., and Koiwai, O. (1991) Development-dependent expression of isozymogens of monkey pepsinogens and structural differences between them. Eur. J. Biochem, 202, 205-215.
6. Foltmann, B. (1992) Chymosin: A short review on foetal and neonatal gastric proteases, Scand. J. Clin. Lab. Invest. 52 (Suppl 210), 65-79.
7. Kageyama, T., Ichinose, M., Tsukada-Kato, S., Omata, M., Narita, Y., Moriyama, A., and Yonezawa, S. (2000) Molecular cloning of neonate/infant- specific pepsinogens from rat stomach mucosa and their expressional change during development, Biochem. Biophys. Res. Commun. 267, 806-812.
8. Fruton, J. S. (1970) The specificity and mechanism of pepsin action, Adv. Enzymol. Relat. Areas Mol. Biol. 33, 401-443.
9. Davies, D. R. (1990) The structure and function of the aspartic proteinases, Annu. Rev. Biophys. Biophys. Chem. 19, 189-215.
10. Dunn, B. M. (2002) Structure and mechanism of the pepsin-like family of aspartic peptidases, Chem. Rev. 102, 4431-4458.
11. Sampath-Kumar, P. S., and Fruton, J. S. (1974) Studies on the extended active sites of acid proteinases, Proc. Natl. Acad. Sci. U.S.A. 71, 1070-1072.
12. Powers, J. C., Harley, A. D., and Myers, D. V. (1977) Subsite specificity of porcine pepsin, Adv. Exp. Med. Biol. 95, 141-157.
13. Dunn, B. M., Jimenez, M., Parten, B. F., Valler, M. J., Rolph, C. E., and Kay, J. (1986) A systematic series of synthetic chromophoric substrates for aspartic proteinases, Biochem. J. 237, 899-906.
14. 2)-Phe-Arg-Leu, by selected aspartic proteinases: Evidence for specific interactions in subsites S3 and S2. Biochim. Biophys. Acta 913, 122-130.
15. Dunn, B. M., and Hung, S. (2000) The two sides of enzyme-substrate specificity: Lessons from the aspartic proteinases, Biochim. Biophys. Acta 1477, 231-240.
16. Andreeva, N. S., Zdanov, A. S., Gustchina, A. E., and Fedorov, A. A. (1984) Structure of ethanol-inhibited porcine pepsin at 2 Å resolution and binding of the methyl ester of phenylalanyldiiodotyrosine to the enzyme, J. Biol. Chem. 259, 11353-11365.
17. Sielecki, A. R., Fedorov, A. A., Boodhoo, A., Andreeva, N. S., and James, M. N. (1990) Molecular and crystal structures of monoclinic porcine pepsin refined at 1.8 Å resolution, J. Mol. Biol. 214, 143-170.
18. Abad-Zapatero, C., Rydel, T. J., and Erickson, J. (1990) Revised 2.3 Å structure of porcine pepsin: Evidence for a flexible subdomain, Proteins 8, 62-81.
19. Cooper, J. B., Khan, G., Taylor, G., Tickle, I. J., and Blundell, T. L. (1990) X-ray analyses of aspartic proteinases. II. Three-dimensional structure of the hexagonal crystal form of porcine pepsin at 2.3 Å resolution, J. Mol. Biol. 214, 199-222.
20. Newman, M., Safro, M., Frazao, C., Khan, G., Zdanov, A., Tickle, I. J., Blundell, T. L., and Andreeva, N. (1991) X-ray analyses of aspartic proteinases. IV. Structure and refinement at 2.2 Å resolution of bovine chymosin, J. Mol. Biol. 221, 1295-1309.
21. Lin, X. L., Wong, R. N., and Tang, J. (1989) Synthesis, purification, and active site mutagenesis of recombinant porcine pepsinogen, J. Biol. Chem. 264, 4482-4489.
22. Suzuki, J., Sasaki, K., Sasao, Y., Hamu, A., Kawasaki, H., Nishiyama, M., Horinouchi, S., and Beppu, T. (1989) Alteration of catalytic properties of chymosin by site-directed mutagenesis, Protein Eng. 2, 563-569.
23. Shintani, T., Nomura, K., and Ichishima, E. (1997) Engineering of porcine pepsin. Alteration of S1 substrate specificity of pepsin to those of fungal aspartic proteinases by site-directed mutagenesis, J. Biol. Chem. 272, 18855-18861.
24. Williams, M. G., Wilsher, J., Nugent, P., Mills, A., Dhanaraj, V., Fabry, M., Sedlácek, J., Uusitalo, J. M., Penttila, M. E., Pitts, J. E., and Blundell, T. L. (1997) Mutagenesis, biochemical characterization, and X-ray structural analysis of point mutants of bovine chymosin, Protein Eng. 10, 991-997.
25. Okoniewska, M., Tanaka, T., and Yada, R. Y. (1999) The role of the flap residue, threonine 77, in the activation and catalytic activity of pepsin A, Protein Eng. 12, 55-61.
26. Okoniewska, M., Tanaka, T., and Yada, R. Y. (2000) The pepsin residue glycine-76 contributes to active-site loop flexibility and participates in catalysis, Biochem. J. 349, 169-177.
27. Kageyama, T. (1995) Procathepsin E and cathepsin E, Methods Enzymol. 248, 120-136.
28. Kageyama, T., Ichinose, M., and Yonezawa, S. (1995) Processing of the precursors to neurotensin and other bioactive peptides by cathepsin E, J. Biol. Chem. 270, 19135-19140.
29. Kageyama, T., and Takahashi, K. (1980) Isolation of an activation intermediate and determination of the amino acid sequence of the activation segment of human pepsinogen A. J. Biochem. 88, 571-582.
30. Kageyama, T. (2000) New world monkey pepsinogens A and C, and prochymosins, Purification, characterization of enzymatic properties, cDNA cloning, and molecular evolution. J. Biochem. 127, 761-770.
31. Stephenson, S. L., and Kenny, A. J. (1987) Metabolism of neuropeptides. Hydrolysis of the angiotensins, bradykinin, substance P, and oxytocin by pig kidney microvillar membranes, Biochem. J. 241, 237-247.
32. Stearns, T., Ma, H., and Botstein, D. (1990) Manipulating yeast genome using plasmid vectors, Methods Enzymol. 185, 280-297.
33. Kageyama, T., and Takahashi, K. (1980) Monkey pepsinogens and pepsins. IV. The amino acid sequence of the activation peptide segment of Japanese monkey pepsinogen, J. Biochem. 88, 9-16.
34. Fujinaga, M., Cherney, M. M., Tarasova, N. I., Bartlett, P. A., Hanson, J. E., and James, M. N. (2000) Structural study of the complex between human pepsin and a phosphorus-containing peptidic-transition-state analogue. Acta Crystallogr., Sect. D 56 (Part 3), 272-279.
35. Groves, M. R., Dhanaraj, V., Badasso, M., Nugent, P., Pitts, J. E., Hoover, D. J., and Blundell, T. L. (1998) A 2.3 Å resolution structure of chymosin complexed with a reduced bond inhibitor shows that the active site β-hairpin flap is rearranged when compared with the native crystal structure, Protein Eng. 11, 833-840.
36. Gilliland, G. L., Winborne, E. L., Nachman, J., and Wlodawer, A. (1990) The three-dimensional structure of recombinant bovine chymosin at 2.3 Å resolution. Proteins 8, 82-101.
37. Anson, M. L., and Mirsky, A. E. (1932) The estimation of pepsin with hemoglobin, J. Gen. Physiol. 16, 59-63.
38. Foltmann, B. (1970) Prochymosin and chymosin, Methods Enzymol. 19, 421-436.
39. Gustchina, E., Rumsh, L., Ginodman, L., Majer, P., and Andreeva, N. (1996) Post X-ray crystallographic studies of chymosin: The existence of two structural forms and the regulation of activity by the interaction with the histidine-proline cluster of κ-casein, FEBS Lett. 379, 60-62.
40. Guillou, H., Miranda, G., and Pelissier, J. P. (1991) Hydrolysis of β-casein by gastric proteases. I. Comparison of proteolytic action of bovine chymosin and pepsin A. Int. J. Pept. Protein Res. 37, 494-501.
41. s1- casein, J. Dairy Res. 60, 401-412.
42. s1-caseins A and F, J. Dairy Res. 65, 233-241.
43. Strop, P., Sedlacek, J., Stys, J., Kaderabkova, Z., Blaha, I., Pavlickova, L., Pohl, J., Fabry, M., Kostka, V., Newman, M., Frazao, C., Shearer, A., Tickle, I. J., and Blundell, T. L. (1990) Engineering enzyme subsite specificity: Preparation, kinetic characterization, and X-ray analysis at 2.0 Å resolution of Val111Phe site-mutated calf chymosin, Biochemistry 29, 9863-9871.
44. Galea, C. A., Dalrymple, B. P., Kuypers, R., and Blakeley, R. (2000) Modification of the substrate specificity of porcine pepsin for the enzymatic production of bovine hide gelatin. Protein Sci. 9, 1947-1959.
45. Lin, Y., Fusek, M., Lin, X., Hartsuck, J. A., Kezdy, F. J., and Tang, J. (1992) pH dependence of kinetic parameters of pepsin, rhizopuspepsin, and their active-site hydrogen bond mutants, J. Biol. Chem. 267, 18413-18418.
46. Pitts, J. E., Dhanaraj, V., Dealwis, C. G., Mantafounis, D., Nugent, P., Orprayoon, P., Cooper, J. B., Newman, M., and Blundell, T. L. (1992) Multidisciplinary cycles for protein engineering: Site-directed mutagenesis and X-ray structural studies of aspartic proteinases, Scand. J. Clin. Lab. Invest. 52 (Suppl 210), 39-50.
47. Pitts, J. E., Uusitalo, J. M., Mantafounis, D., Nugent, P. G., Quinn, D. D., Orprayoon, P., and Penttila, M. E. (1993) Expression and characterisation of chymosin pH optima mutants produced in Trichoderma reesei, J. Biotechnol. 28, 69-83.
48. Örd, T., Kolmer, M., Villems, R., and Saarma, M. (1990) Structure of the human genomic region homologous to the bovine prochymosin-encoding gene, Gene 91, 241-246.
49. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227, 680-685.