Role of Phe120 in the activity and structure of bovine pancreatic ribonuclease A

Journal of Biochemistry

Volumn 124, Issue 2, 1998, Pages 410-416

  Tanimizu, Naoki ^a   Ueno, Hiroshi ^a   Hayashi, Rikimaru ^a  

^a KYOTO UNIVERSITY   (Japan)

Author keywords

Carboxymethylation of histidine; Catalytic histidine residues; Catalytic role of phenylalanine; RNase A

Indexed keywords

ALANINE; GLUTAMIC ACID; HISTIDINE; LEUCINE; PANCREAS ENZYME; PHENYLALANINE; RIBONUCLEASE A; TRYPTOPHAN;

ARTICLE; CONFORMATIONAL TRANSITION; ENZYME ACTIVITY; ENZYME PHOSPHORYLATION; HYDROLYSIS; MICHAELIS MENTEN KINETICS; NONHUMAN; PH; SITE DIRECTED MUTAGENESIS;

EID: 0031656619     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022127     Document Type: Article

References (29)

1. Gundlach, H.G., Stein, W.H., and Moore, S. (1959) The nature of the amino acid residues involved in the inactivation of ribonuclease by iodoacetate. J. Biol. Chem. 234, 1754-1760
2. Crestfield, A.M., Stein, W.H., and Moore, S. (1963) Alkylation and identification of the histidine residues at the active site of ribonuclease. J. Biol. Chem. 238, 2413-2420
3. Richards, F.M. and Wychoff, H.W. (1971) Bovine pancreatic ribonuclease in The Enzymes (Boyer, P.D., ed.) Vol. 4, pp. 647-806, Academic Press, New York
4. Blackburn, P. and Moore, S. (1982) Bovine pancreatic ribonuclease A in The Enzymes (Boyer, P.D., ed.) Vol. 15, pp. 317-443, Academic Press, New York
5. Laity, J.H., Shimotakahara, S., and Scheraga, H.A. (1993) Expression of wild-type and mutant bovine pancreatic ribonuclease A in Escherichia coli. Proc. Natl. Acad. Sci. USA 90, 615-619
6. Schlutz, D.A. and Baldwin, R.L. (1992) Cis proline mutants of ribonuclease A. I. Thermal stability. Protein Sci. 1, 910-916
7. Schultz, D.A. and Baldwin, R.L. (1992) Cis proline mutants of ribonuclease A. II. Elimination of the slow-folding forms by mutation. Protein Sci. 1, 917-924
8. Thompson, J.E. and Raines, R.T. (1994) Value of general acid-base catalysis to ribonuclease A. J. Am. Chem. Soc. 116, 5467-5468
9. Boix, E., Nogues, M.V., Schein, C.H., Benner, S.A., and Cuchillo, C.M. (1994) Reverse transphosphorylation by ribonuclease A needs an intact p2-binding site. Point mutation at Lys7 and Arg10 alter the catalytic properties of the enzyme. J. Biol. Chem. 269, 2529-2534
10. delCardayre, S.B. and Raines, R.T. (1994) Structural determinants of enzymatic processivity. Biochemistry 33, 6031-6037
11. Nambiar, K.P., Stackhouse, J., Presnell, S.R., and Benner, S.A. (1987) Expression of bovine pancreatic ribonuclease A in Escherichia coli. Eur. J. Biochem. 163, 67-71
12. Vasantha, N. and Filpula, D. (1989) Expression of bovine pancreatic ribonuclease A coded by a synthetic gene in Bacillus subtilis. Gene 76, 53-60
13. Studier, F.W., Rosenberg, A.H., Dunn, J.J., and Dubendroff, J.W. (1990) Use of T7 polymerase to directed expression of cloned genes in Methods Enzymology (Goeddel, D.V., eds.) Vol. 185, pp. 60-89, Academic Press, New York
14. Schein, C.H., Boix, E., Haugg, M., Holliger, K.P., Hemmi, S., Frank, G., and Schwalbe, H. (1992) Secretion of mammalian ribonucleases from Escherichia coli using the signal sequence of murine spleen ribonuclease. Biochem. J. 283, 137-144
15. Eberhardt, E.S., Wittmayer, P.K., Templer, B.M., and Raines, R.T. (1996) Contribution of a tyrosine side chain to ribonuclease A catalysis and stability. Protein Sci. 5, 1697-1703
16. Doumen, J., Gonciarz, M., Zegers, I., Loris, R., Wyns, L., and Steyaert, J. (1996) A catalytic function for the structurally conserved residue Phe100 of ribonuclease T1. Protein Sci. 5, 1523-1530
17. Zegers, I., Maes, D., Dao-thi, I.M., Poortman, F., Palmer, R., and Wayns, L. (1994) The structures of RNase A complexed with 3′-CMP and d(CpA): Active site conformation and conserved water molecules. Protein Sci. 3, 2322-2339
18. Lin, M.C., Gutte, B., Caldi, D.G., Moore, S., and Merrifield, R.B. (1972) Reactivation of des(119-124) ribonuclease A by mixture with synthetic COOH-terminal peptides; the role of phenylalanine-120. J. Biol. Chem. 247, 4768-4774
19. Hayashi, R., Moore, S., and Merrifield, R.B. (1973) Preparation of pancreatic ribonuclease 1-114 and 1-115 and their reactivation by mixture with synthetic COOH-terminal peptides. J. Biol. Chem. 248, 3889-3892
20. deMel, V.S.J., Doscher, M.S., Glinn, M.A., Martin, P.D., Ram, M.L., and Edwards, B.F.P. (1994) Structural investigation of catalytically modified F120L and F120Y semisynthetic ribonucleases. Protein Sci. 3, 39-50
21. Deng, W.P. and Nickoloff, J.A. (1992) Site-directed mutagenesis of virtually any plasmid by eliminating a unique site. Anal. Biochem. 200, 81-88
22. Smith, P.K., Krohn, R.I., Hermanson, G.T., Mallia, A.K., Gartner, F.H., Provenzano, M.D., Fujimoto, E.K., Goeke, N.M., Olson, B.J., and Klenk, D.C. (1985) Measurement of protein using bicinchonic acid. Anal. Biochem. 150, 76-85
23. Rosario, E.J. and Hammes, G.G. (1969) Kinetic and equilibrium studies of the ribonuclease-catalyzed hydrolysis of uridine 2′,3′-cyclic phosphate. Biochemistry 8, 1884-1889
24. Eftink, M.R. and Biltonen, R.L. (1983) Energetics of ribonuclease A catalysis. 1. pH, ionic strength, and solvent isotope dependence of the hydrolysis of cytidine cyclic 2′,3′-phosphate. Biochemistry 22, 5123-5134
25. Jackson, D., Burnier, J., Quan, C., Stanley, M., Tom, J., and Wells, J.A. (1994) A designed peptide ligase for total synthesis of ribonuclease A with unnatural catalytic residues. Science 266, 243-247
26. Galzi, J., Bertrand, D., Devillers-Thiery, A., Revah, F., Bertrand, S., and Changeux, J. (1991) Allosteric transitions of the acetylcholine receptor probed at the amino acid level with a photolabile cholinergic ligand. FEBS Lett. 294, 198-202
27. Sine, S.M., Quiram, P., Papanikolaou, F., Kreienkamp, H., and Taylor, P. (1992) Conserved tyrosines in the alpha subunit of the acetylcholine receptor stabilize quaternary ammonium groups of agonists and curariform antagonists. J. Biol. Chem. 269, 8808-8816
28. a and contribution to protein stability. J. Mol. Biol. 224, 759-770
29. Coulter, C.L. (1973) Structural chemistry of cyclic nucleotides. II. Crystal and molecular structure of sodium cytidine 2′,3′-cyclic phosphate. J. Am. Chem. Soc. 95, 570-575