Contribution of the carbohydrate moiety to conformational stability of the carboxypeptidase Y: High pressure study

European Journal of Biochemistry

Volumn 262, Issue 2, 1999, Pages 475-483

  Dumoulin, Mireille ^c   Ueno, Hiroshi ^c   Hayashi, Rikimaru ^b   Balny, Claude ^a  

^a CNRS   (France)

^b KYOTO UNIVERSITY   (Japan)

^c NONE

Author keywords

Carboxypeptidase Y; Fluorescence spectrometry; High pressure; Protein denaturation; Unglycosylation

Indexed keywords

CARBOHYDRATE; CARBOXYPEPTIDASE C;

ARTICLE; CARBOHYDRATE ANALYSIS; CONFORMATIONAL TRANSITION; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME DENATURATION; ENZYME STABILITY; ENZYME STRUCTURE; NONHUMAN; PRESSURE; PRIORITY JOURNAL; SACCHAROMYCES CEREVISIAE; STRUCTURE ANALYSIS;

CARBOXYPEPTIDASE C; CARBOXYPEPTIDASES; CATALYSIS; ENZYME STABILITY; MODELS, MOLECULAR; PRESSURE; PROTEIN CONFORMATION; SPECTROMETRY, FLUORESCENCE; TEMPERATURE; THERMODYNAMICS;

EID: 0001625030     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00397.x     Document Type: Article

References (40)

1. 1. Hayashi, R. (1976) Carboxypeptidase Y. Methods Enzymol 45, 568-587.
2. 2. Hata, T., Hayashi, R. & Doi, E. (1967) Purification of yeast proteinases. Part III. Isolation and physicochemical properties of yeast proteinase A and C. Agric. Biol. Chem. 31, 357-367.
3. 3. Aribara, S., Hayashi, R. & Hata, T. (1971) Physical and chemical properties of yeast proteinase C. Agric. Biol. Chem. 35, 658-666.
4. 4. Endrizzi, J.A., Breddam, K. & Remington, S.J. (1994) 2.8-Å Structure of yeast serine carboxypeptidase. Biochemistry 33, 11106-11120.
5. 5. Hasilik, A. & Tanner, W. (1978) Biosynthesis of the vacuolar yeast glycoprotein Carboxypeptidase Y. Conversion of precursor into the enzyme. Eur. J. Biochem. 85, 599-608.
6. 6. Hashimoto, C., Cohen, R.E., Zhang, W.-J. & Ballou, C.E. (1981) Carbohydrate chains on yeast Carboxypeptidase Y are phosphorylated. Proc. Natl Acad. Sci. USA 78, 2244-2248.
7. 7. Trimble, R.B., Maley, F. & Chu, F.K. (1983) Glycoprotein biosynthesis in yeast. J. Biol. Chem. 258, 2562-2567.
8. 8. Winther, J.R., Stevens, T.H. & Kielland-Brandt, M.C. (1991) Yeast carboxypeptidase Y requires glycosylation for efficient intracellular transport, but not for vacuolar sorting, in vivo stability, or activity. Eur. J. Biochem. 197, 681-689.
9. 9. Chu, F.K. & Maley, F. (1982) Stabilization of the structure and activity of yeast carboxypeptidase Y by its high-mannose oligosaccharide chains. Arch. Biochem. Biophys. 214, 134-139.
10. 10. Mozhaev, V.V., Heremans, K., Frank, J., Masson, P. & Balny, C. (1996) High pressure effects on protein structure and function. Proteins 24, 81-91.
11. 11. Bridgman, P.W. (1912) Water in the liquid and fine solid forms under pressure. Proc. Am. Acad. Arts Sci. 47, 441-558.
12. 12. Hamaguchi, K. (1992) Physico-chemical properties of amino acid side chains. In The Protein Molecule. Conformation, Stability and Folding (Hamaguchi, K., ed), pp. 1-19. Japan Scientific Society Press, Tokyo.
13. 13. Ruan, K., Lange, R., Bec, N. & Balny, C. (1997) A stable partly denatured state of trypsin induced by high hydrostatic pressure. Biochem. Biophys. Res. Commun. 239, 150-154.
14. 14. Cléry, C., Renault, F. & Masson, P. (1995) Pressure-induced molten globule state of cholinesterase. FEBS Lett. 370, 212-214.
15. 15. Kunugi, S., Yanagi, Y., Kitayaki, M., Tanaka, N. & Uehara-Kunugi, Y. (1997) Effects of high-pressure on the activity and spectroscopic properties of carboxypeptidase Y. Bull. Chem. Soc. Jpn. 70, 1459-1463.
16. 16. Hayashi, R., Kinsho, T. & Ueno, H. (1998) Combined application of sub-zero temperature and high pressure on biological materials. In High Pressure Food Science, Bioscience and Chemistry (Isaacs, N.S., ed.), pp. 166-174. Royal Society of Chemistry, England.
17. 17. Jung, G., Ueno, H., Hayashi, R. & Liao, T.-H. (1995) Identification of the catalytic histidine residue participating in the charge-relay system of carboxypeptidase Y. Protein Sci. 4, 2433-2435.
18. 18. Shimizu, H., Ueno, H. & Hayashi, R. (1999) Role of carbohydrate moiety in carboxypeptidase Y: structural study of mutant enzyme lacking carbohydrate moiety. Biosci. Biotechnol. Biochem. in press.
19. 19. Neumann, R.C., Kauzmann, W. & Zipp, A. (1973) Pressure dependence of weak acid ionization in aqueous buffers. J. Phys. Chem. 77, 2687-26911.
20. 20. Morishita, M., Tanaka, T. & Kawai, S. (1997) High pressure optical cell and its pump for spectrophotometer. In High Pressure Bioscience and Technology (Suzuki, A. & Hayashi, R., eds), pp. 187-194. San-ei Shuppan Co., Kyoto, Japan (in Japanese).
21. 21. Bec, N., Villa, A., Tortora, P., Mozhaev, V.V., Balny, C. & Lange, R. (1996) Enhanced stability of carboxypeptidase from Sulfolobus solfataricus at high pressure. Biotechnol. Lett. 18, 482-488.
22. 22. Lange, R., Frank, J., Saldana, J.-L. & Balny, C. (1996) Fourth derivative UV-spectroscopy of proteins under high pressure. I. Factors affecting the fourth derivative spectrum of the aromatic amino acids. Eur. Biophys. J. 24, 277-283.
23. 23. Gibson, R.E. & Loeffler, O.H. (1941) Pressure-volume-temperature relations in solutions. V. The energy-volume coefficients of the carbon tetrachloride, water and ethylene glycol. J. Am. Chem. Soc. 63, 898-906.
24. 24. Silva, J.L., Miles, E.V. & Weber, G. (1986) Pressure dissociation and conformational drift of the β-dimer of tryptophan synthase. Biochemistry 25, 5780-5786.
25. 25. Balny, C., Travers, F., Barman, T. & Douzou, P. (1987) Thermodynamics of the two-step formation of horseradish peroxidase coumpound I. Eur. Biophys. J. 14, 375-383.
26. 26. Hawley, S.A. (1971) Reversible pressure-temperature denaturation of chymotrypsinogen. Biochemistry 10, 2436-2442.
27. 27. Taniguchi, Y. & Suzuki, K. (1983) Pressure inactivation of α-chymotrypsin. J. Phys. Chem. 87, 5185-5193.
28. 28. Masson, P. & Cléry, C. (1996) Pressure-induced molten globule states of proteins. In High Pressure Bioscience and Biotechnology (Hayashi, R. & Balny, C., eds), pp. 114-126. Elsevier Science B.V., the Netherlands.
29. 29. Ptitsyn, O.B. (1995) Molten globule and protein folding. Adv. Prot. Chem. 47, 83-229.
30. 30. Mombelli, E., Bec, N., Tortora, P., Balny, C. & Lange, R. (1996) Pressure and temperature control of a thermophilic carboxypeptidase from Sulfolobus solfataricus. Food Biotech. 10, 131-142.
31. 31. Winther, J.R. & Sørensen, P. (1991) Propeptide of carboxypeptidase Y provides a chaperone-like function as well as inhibition of the enzyme activity. Proc. Natl Acad. Sci. USA 88, 9330-9334.
32. 32. Sørensen, P., Winther, J.R., Kaarsholm, N.C. & Poulsen, F.M. (1993) The pro region required for folding of carboxypeptidase Y is a partially folded domain with little regular structural core. Biochemistry 32, 12160-12166.
33. 33. Mer, G., Hietter, H. & Lefèvre, J.-F. (1996) Stabilization of protein by glycosylation examined by NMR analysis of a fucosylated proteinase inhibitor. Nat. Struct. Biol. 3, 45-53.
34. 34. Wang, F.-F.C. & Hirs, C.H.W. (1977) Influence of the heterosaccharides in porcine pancreatic ribonuclease on the conformation and stability of the protein. J. Biol. Chem. 23, 8358-8364.
35. 35. Hetch, H.J., Kaliz, H.M., Hendle, J., Schmid, R.D. & Schomburg, D. (1993) Crystal structure of glucose oxidase from Aspergilus niger refined at 2.3 Å resolution. J. Mol. Biol. 229, 153-172.
36. 36. Dwek, R.A. (1995) Glycobiology: more function for oligosaccharides. Science 269, 1234-1235.
37. 37. Masson, P. (1992) Pressure denaturation of proteins. In High Pressure and Biotechnology (Balny, C., Hayashi, R., Heremans, K. & Masson, P., eds), Vol. 224, pp. 89-99. John Libbey Eurotext, France.
38. 38. Joao, H.C. & Dwek, R.A. (1993) Effects of glycosylation on protein structure and dynamics in ribonuclease B and some of its individual glycoforms. Eur. J. Biochem. 218, 239-244.
39. 39. Rudd, P.M., Joao, H.C., Coghill, E., Fiten, P., Saunders, M.R., Opedenakker, G. & Dwek, R.A. (1994) Glycoforms modify the dynamic stability and functional activity of an enzyme. Biochemistry 33, 17-22.
40. 40. Tams, J.W. & Welinder, K.G. (1998) Glycosylation and thermodynamic versus kinetic stability of horseradish peroxydase. FEBS Lett. 421, 234-236.