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Volumn 54, Issue 8, 1998, Pages 766-774

The contribution of noncatalytic phosphate-binding subsites to the mechanism of bovine pancreatic ribonuclease A

Author keywords

Binding sites; Catalysis; Enzyme kinetics; Ribonuclease; RNA

Indexed keywords

AMINO ACID; PANCREAS ENZYME; PHOSPHATE; RIBONUCLEASE A;

EID: 0031671322     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s000180050205     Document Type: Article
Times cited : (46)

References (47)
  • 3
    • 0002598414 scopus 로고
    • Type II restriction enzymes
    • Linn S. M., Lloyd R. S. and Roberts R. J. (eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • Roberts R. J. and Halford S. E. (1993) Type II restriction enzymes. In: Nucleases, pp. 35-88, Linn S. M., Lloyd R. S. and Roberts R. J. (eds), Cold Spring Harbor Laboratory Press, Cold Spring Harbor
    • (1993) Nucleases , pp. 35-88
    • Roberts, R.J.1    Halford, S.E.2
  • 4
    • 77956909282 scopus 로고
    • Bovine pancreatic ribonuclease
    • Boyer P. D. (ed.), Academic Press, New York
    • Richards F. M. and Wyckoff H. W. (1971) Bovine pancreatic ribonuclease. In: The Enzymes. vol. 4, pp. 647-806, Boyer P. D. (ed.), Academic Press, New York
    • (1971) The Enzymes , vol.4 , pp. 647-806
    • Richards, F.M.1    Wyckoff, H.W.2
  • 5
    • 0002447609 scopus 로고    scopus 로고
    • Barnase and Barstar
    • D'Alessio G. and Riordan J. F. (eds), Academic Press, San Diego
    • Hartley R. W. (1997) Barnase and Barstar. In: Ribonucleases: Structures and Functions, pp. 51-100, D'Alessio G. and Riordan J. F. (eds), Academic Press, San Diego
    • (1997) Ribonucleases: Structures and Functions , pp. 51-100
    • Hartley, R.W.1
  • 6
    • 0026751045 scopus 로고
    • Barnase has subsites that give rise to large rate enhancements
    • Day A.G., Parsonage D., Ebel S., Brown T. and Fersht A.R. (1992) Barnase has subsites that give rise to large rate enhancements. Biochemistry 31: 6390-6395
    • (1992) Biochemistry , vol.31 , pp. 6390-6395
    • Day, A.G.1    Parsonage, D.2    Ebel, S.3    Brown, T.4    Fersht, A.R.5
  • 7
    • 0028287089 scopus 로고
    • Subsite binding in an RNase-structure of a barnase tetranucleotide complex at 1.76-angstrom resolution
    • Buckle A. M. and Fersht A. R. (1994) Subsite binding in an RNase-structure of a barnase tetranucleotide complex at 1.76-angstrom resolution. Biochemistry 33: 1644-1653
    • (1994) Biochemistry , vol.33 , pp. 1644-1653
    • Buckle, A.M.1    Fersht, A.R.2
  • 8
    • 0000512084 scopus 로고
    • Enzymatic characterization of onconase, a novel ribonuclease with antitumor activity
    • Ardelt W., Lee IL-S., Randolph G., Viera A., Mikulski S. M. and Shogen K. (1994) Enzymatic characterization of onconase, a novel ribonuclease with antitumor activity. Protein Sci. 3 (Suppl. 1): 137
    • (1994) Protein Sci. , vol.3 , Issue.1 SUPPL. , pp. 137
    • Ardelt, W.1    Lee, I.L.-S.2    Randolph, G.3    Viera, A.4    Mikulski, S.M.5    Shogen, K.6
  • 9
    • 0025809312 scopus 로고
    • Comparative base specificity, stability and lectin activity of two lectins from eggs of Rana catesbeiana and R. japonica and liver ribonuclease from R. catesbeiana
    • Tokyo
    • Okabe Y., Katayama N., Iwana M., Watanabe H., Ohgi K., Irie M. et al. (1991) Comparative base specificity, stability and lectin activity of two lectins from eggs of Rana catesbeiana and R. japonica and liver ribonuclease from R. catesbeiana. J. Biochem. (Tokyo) 109: 786-790
    • (1991) J. Biochem. , vol.109 , pp. 786-790
    • Okabe, Y.1    Katayama, N.2    Iwana, M.3    Watanabe, H.4    Ohgi, K.5    Irie, M.6
  • 11
    • 0029871341 scopus 로고    scopus 로고
    • Role of the N terminus in RNase A homologues: Differences in catalytic activity, ribonuclease inhibitor interaction and cytotoxicity
    • Boix E., Wu Y. N., Vasandani V. M., Saxena S. K., Ardelt W., Ladner J. et al. (1996) Role of the N terminus in RNase A homologues: differences in catalytic activity, ribonuclease inhibitor interaction and cytotoxicity. J. Mol. Biol. 257: 992-1007
    • (1996) J. Mol. Biol. , vol.257 , pp. 992-1007
    • Boix, E.1    Wu, Y.N.2    Vasandani, V.M.3    Saxena, S.K.4    Ardelt, W.5    Ladner, J.6
  • 12
    • 0026724926 scopus 로고
    • Eosinophil-derived neurotoxin and human liver ribonuclease: Identity of structure and linkage of neurotoxicity to nuclease activity
    • Sorrentino S., Glitz D. G., Hamann K. J., Loegering D. A., Checkel J. L. and Gleich G. J. (1992) Eosinophil-derived neurotoxin and human liver ribonuclease: identity of structure and linkage of neurotoxicity to nuclease activity. J. Biol. Chem. 267: 14859-14865
    • (1992) J. Biol. Chem. , vol.267 , pp. 14859-14865
    • Sorrentino, S.1    Glitz, D.G.2    Hamann, K.J.3    Loegering, D.A.4    Checkel, J.L.5    Gleich, G.J.6
  • 13
    • 0030602895 scopus 로고    scopus 로고
    • X-ray crystallographic structure of recombinant eosinophil-derived neurotoxin at 1.83 Å resolution
    • Mosiman S. C., Newton D. L., Youle R. J. and James M. N. G. (1996) X-ray crystallographic structure of recombinant eosinophil-derived neurotoxin at 1.83 Å resolution. J. Mol. Biol. 260: 540-542
    • (1996) J. Mol. Biol. , vol.260 , pp. 540-542
    • Mosiman, S.C.1    Newton, D.L.2    Youle, R.J.3    James, M.N.G.4
  • 14
    • 0023003622 scopus 로고
    • Ribonuclease activity associated with human eosinophil-derived neurotoxin and eosinophil cationic protein
    • Slifman N. R., Loegering D. A., McKean D. J. and Gleich G. J. (1986) Ribonuclease activity associated with human eosinophil-derived neurotoxin and eosinophil cationic protein. J. Immunol. 137: 2913-2917
    • (1986) J. Immunol. , vol.137 , pp. 2913-2917
    • Slifman, N.R.1    Loegering, D.A.2    McKean, D.J.3    Gleich, G.J.4
  • 15
    • 0025826167 scopus 로고
    • Ribonuclease activity and substrate preference of human eosinophil cationic protein (ECP)
    • Sorrentino S. and Glitz D. G. (1991) Ribonuclease activity and substrate preference of human eosinophil cationic protein (ECP). FEBS Lett. 288: 23-26
    • (1991) FEBS Lett. , vol.288 , pp. 23-26
    • Sorrentino, S.1    Glitz, D.G.2
  • 16
  • 17
    • 0024427333 scopus 로고
    • Presence of a basic amino acid residue at either position 66 or 122 is a condition for enzymic activity in the ribonuclease superfamily
    • Beintema J.J. (1989) Presence of a basic amino acid residue at either position 66 or 122 is a condition for enzymic activity in the ribonuclease superfamily. FEBS Lett. 254: 1-4
    • (1989) FEBS Lett. , vol.254 , pp. 1-4
    • Beintema, J.J.1
  • 18
    • 0026264573 scopus 로고
    • Structure and function of ribonuclease A binding subsites
    • Tipton K. F. (ed.), Portland Press, London
    • Parés X., Nogués M. V., de Llorens R. and Cuchillo C. M. (1991) Structure and function of ribonuclease A binding subsites. In: Essays in Biochemistry, vol. 26, pp. 89-103, Tipton K. F. (ed.), Portland Press, London
    • (1991) Essays in Biochemistry , vol.26 , pp. 89-103
    • Parés, X.1    Nogués, M.V.2    De Llorens, R.3    Cuchillo, C.M.4
  • 19
    • 0028806062 scopus 로고
    • Bovine pancreatic ribonuclease A as a model of an enzyme with multiple substrate binding sites
    • Nogués M. V., Vilanova M. and Cuchillo C.M. (1995) Bovine pancreatic ribonuclease A as a model of an enzyme with multiple substrate binding sites. Biochim. Biophys. Acta 1253: 16-24
    • (1995) Biochim. Biophys. Acta , vol.1253 , pp. 16-24
    • Nogués, M.V.1    Vilanova, M.2    Cuchillo, C.M.3
  • 20
    • 0002450219 scopus 로고    scopus 로고
    • Pancreatic ribonucleases
    • D'Alessio G. and Riordan J. F. (eds), Academic Press, San Diego
    • Cuchillo C. M., Vilanova M. and Nogués M.V. (1997) Pancreatic ribonucleases. In: Ribonucleases: Structures and Functions, pp. 272-304, D'Alessio G. and Riordan J. F. (eds), Academic Press, San Diego
    • (1997) Ribonucleases: Structures and Functions , pp. 272-304
    • Cuchillo, C.M.1    Vilanova, M.2    Nogués, M.V.3
  • 21
    • 0001970541 scopus 로고    scopus 로고
    • Crystallographic studies of ribonuclease complexes
    • D'Alessio G. and Riordan J. F. (eds), Academic Press, San Diego
    • Gilliland G. L. (1997) Crystallographic studies of ribonuclease complexes. In: Ribonucleases: Structures and Functions, pp. 306-341, D'Alessio G. and Riordan J. F. (eds), Academic Press, San Diego
    • (1997) Ribonucleases: Structures and Functions , pp. 306-341
    • Gilliland, G.L.1
  • 22
    • 0022515682 scopus 로고
    • The mechanism of binding of a polynucleotide chain to pancreatic ribonuclease
    • McPherson A., Brayer G., Cascio D. and Williams R. (1986) The mechanism of binding of a polynucleotide chain to pancreatic ribonuclease. Science 232: 765-768
    • (1986) Science , vol.232 , pp. 765-768
    • McPherson, A.1    Brayer, G.2    Cascio, D.3    Williams, R.4
  • 25
    • 0021196092 scopus 로고
    • Kinetic studies in the cleavage of oligouridylic acids and poly U by bovine pancreatic ribonuclease A
    • Tokyo
    • Irie M., Mikami F., Monma K., Ohgi K.,. Watanabe H., Yamaguchi R. et al. (1984) Kinetic studies in the cleavage of oligouridylic acids and poly U by bovine pancreatic ribonuclease A. J. Biochem. (Tokyo) 96: 89-96
    • (1984) J. Biochem. , vol.96 , pp. 89-96
    • Irie, M.1    Mikami, F.2    Monma, K.3    Ohgi, K.4    Watanabe, H.5    Yamaguchi, R.6
  • 26
    • 0029868324 scopus 로고    scopus 로고
    • The role of non-catalytic binding subsites in the endonuclease activity of bovine pancreatic ribonuclease A
    • Moussaoui M., Guasch A., Boix E., Cuchillo C. M. and Nogués M. V. (1996) The role of non-catalytic binding subsites in the endonuclease activity of bovine pancreatic ribonuclease A. J. Biol. Chem. 271: 4687-4692
    • (1996) J. Biol. Chem. , vol.271 , pp. 4687-4692
    • Moussaoui, M.1    Guasch, A.2    Boix, E.3    Cuchillo, C.M.4    Nogués, M.V.5
  • 27
    • 0019002795 scopus 로고
    • The reaction of bovine pancreatic ribonuclease A with 6-chloropurine riboside 5′-monophosphate: Evidence on the existence of a phosphate-binding subsite
    • Parés X., Llorens R., Arús C. and Cuchillo C. M. (1980) The reaction of bovine pancreatic ribonuclease A with 6-chloropurine riboside 5′-monophosphate: evidence on the existence of a phosphate-binding subsite. Eur. J. Biochem. 105: 571-579
    • (1980) Eur. J. Biochem. , vol.105 , pp. 571-579
    • Parés, X.1    Llorens, R.2    Arús, C.3    Cuchillo, C.M.4
  • 29
    • 0020494580 scopus 로고
    • Evidence on the existence of a purine ligand induced conformational change in the active site of bovine pancreatic ribonuclease A studied by proton nuclear magnetic resonance spectroscopy
    • Arús C., Paolillo L., Llorens R., Napolitano R. and Cuchillo C. M. (1982) Evidence on the existence of a purine ligand induced conformational change in the active site of bovine pancreatic ribonuclease A studied by proton nuclear magnetic resonance spectroscopy. Biochemistry 21: 4290-4297
    • (1982) Biochemistry , vol.21 , pp. 4290-4297
    • Arús, C.1    Paolillo, L.2    Llorens, R.3    Napolitano, R.4    Cuchillo, C.M.5
  • 30
    • 0024027310 scopus 로고
    • 1H-n.m.r. studies on the specificity of the interaction between bovine pancreatic ribonuclease A and dideoxynucleoside monophosphates
    • 1H-n.m.r. studies on the specificity of the interaction between bovine pancreatic ribonuclease A and dideoxynucleoside monophosphates. Int. J. Peptide Protein Res. 31: 537-543
    • (1988) Int. J. Peptide Protein Res. , vol.31 , pp. 537-543
    • Alonso, J.1    Paolillo, L.2    D'Auria, G.3    Nogués, M.V.4    Cuchillo, C.M.5
  • 33
    • 0027504354 scopus 로고
    • The amino acid sequence of human ribonuclease 4, a highly conserved ribonuclease that cleaves specifically on the 3′ side of uridine
    • Zhou H. M. and Strydom D. J. (1993) The amino acid sequence of human ribonuclease 4, a highly conserved ribonuclease that cleaves specifically on the 3′ side of uridine. Eur. J. Biochem. 217: 401-410
    • (1993) Eur. J. Biochem. , vol.217 , pp. 401-410
    • Zhou, H.M.1    Strydom, D.J.2
  • 34
    • 0022829368 scopus 로고
    • Isolation and characterization of a human colon carcinoma-secreted enzyme with pancreatic ribonuclease-like activity
    • Shapiro R., Fett J. W., Strydom D. J. and Vallee B. L. (1986) Isolation and characterization of a human colon carcinoma-secreted enzyme with pancreatic ribonuclease-like activity. Biochemistry 25: 3527-3532
    • (1986) Biochemistry , vol.25 , pp. 3527-3532
    • Shapiro, R.1    Fett, J.W.2    Strydom, D.J.3    Vallee, B.L.4
  • 35
    • 0028029452 scopus 로고
    • Structure of ribonuclease A derivative II at 2.1 Å resolution
    • Boqué L., Coll M. G., Vilanova M, Cuchillo C. M. and Fita I. (1994) Structure of ribonuclease A derivative II at 2.1 Å resolution. J. Biol. Chem. 269: 19707-19712
    • (1994) J. Biol. Chem. , vol.269 , pp. 19707-19712
    • Boqué, L.1    Coll, M.G.2    Vilanova, M.3    Cuchillo, C.M.4    Fita, I.5
  • 36
    • 0030917539 scopus 로고    scopus 로고
    • Crystal structures of ribonuclease A complexes with 5′-diphosphoadenosine 3′-phosphate and 5′-diphosphoadenosine 2′-phosphate at 1.7 Å resolution
    • Leonidas D. D., Shapiro R., Irons L. I., Russo N. and Acharya K. R. (1997) Crystal structures of ribonuclease A complexes with 5′-diphosphoadenosine 3′-phosphate and 5′-diphosphoadenosine 2′-phosphate at 1.7 Å resolution. Biochemistry 36: 5578-5588
    • (1997) Biochemistry , vol.36 , pp. 5578-5588
    • Leonidas, D.D.1    Shapiro, R.2    Irons, L.I.3    Russo, N.4    Acharya, K.R.5
  • 37
    • 0028040762 scopus 로고
    • Reverse transphosphorylation by ribonuclease A needs an intact p2-binding site
    • Boix E., Nogués M. V., Schein C. H., Benner S. A. and Cuchillo C. M. (1994) Reverse transphosphorylation by ribonuclease A needs an intact p2-binding site. J. Biol. Chem. 269: 2529-2534
    • (1994) J. Biol. Chem. , vol.269 , pp. 2529-2534
    • Boix, E.1    Nogués, M.V.2    Schein, C.H.3    Benner, S.A.4    Cuchillo, C.M.5
  • 38
    • 0017822280 scopus 로고
    • Studies on the binding of adenylyl-3′,5′-cytidine to ribonuclease
    • Mitsui Y., Urata Y., Torii K. and Irie M. (1978) Studies on the binding of adenylyl-3′,5′-cytidine to ribonuclease. Biochim. Biophys. Acta 535: 299-308
    • (1978) Biochim. Biophys. Acta , vol.535 , pp. 299-308
    • Mitsui, Y.1    Urata, Y.2    Torii, K.3    Irie, M.4
  • 39
    • 0014579415 scopus 로고
    • Interaction of uridine 2′(3′),5′-diphosphate with ribonuclease A and carboxymethylribonuclease A
    • Tokyo
    • Sawada F. and Irie M. (1969) Interaction of uridine 2′(3′),5′-diphosphate with ribonuclease A and carboxymethylribonuclease A. J. Biochem. (Tokyo) 66: 415-418
    • (1969) J. Biochem. , vol.66 , pp. 415-418
    • Sawada, F.1    Irie, M.2
  • 40
    • 0015989555 scopus 로고
    • A steady-state kinetic study of the ribonuclease A catalyzed hydrolysis of uridine-2′:3′(cyclic)-5′-diphosphate
    • Li J. R. and Walz G. F. (1974) A steady-state kinetic study of the ribonuclease A catalyzed hydrolysis of uridine-2′:3′(cyclic)-5′-diphosphate. Arch. Biochem. Biophys. 161: 227-233
    • (1974) Arch. Biochem. Biophys. , vol.161 , pp. 227-233
    • Li, J.R.1    Walz, G.F.2
  • 42
    • 0024639235 scopus 로고
    • Chemical and computer graphics studies on the topography of the ribonuclease A active site cleft. A model of the enzyme pentanucleotide substrate complex
    • de Llorens R., Arús C., Parés X. and Cuchillo C. M. (1989) Chemical and computer graphics studies on the topography of the ribonuclease A active site cleft. A model of the enzyme pentanucleotide substrate complex. Protein Eng. 2: 417-429
    • (1989) Protein Eng. , vol.2 , pp. 417-429
    • De Llorens, R.1    Arús, C.2    Parés, X.3    Cuchillo, C.M.4
  • 43
    • 0028262928 scopus 로고
    • Crystal structure of human angiogenin reveals the structural basis for its functional divergence from ribonuclease
    • Acharya K. R., Shapiro R., Allen S. C., Riordan J. F. and Vallee B.L. (1994) Crystal structure of human angiogenin reveals the structural basis for its functional divergence from ribonuclease. Proc. Natl. Acad. Sci. USA 91: 2915-2919
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2915-2919
    • Acharya, K.R.1    Shapiro, R.2    Allen, S.C.3    Riordan, J.F.4    Vallee, B.L.5
  • 44
    • 0002702165 scopus 로고    scopus 로고
    • Structure and function of angiogenin
    • D'Alessio G. and Riordan J. F. (eds), Academic Press, San Diego
    • Riordan J.F. (1997) Structure and function of angiogenin. In: Ribonucleases: Structures and Functions, pp. 446-489, D'Alessio G. and Riordan J. F. (eds), Academic Press, San Diego
    • (1997) Ribonucleases: Structures and Functions , pp. 446-489
    • Riordan, J.F.1
  • 45
    • 0001987910 scopus 로고    scopus 로고
    • Evolution of vertebrate ribonucleases: Ribonuclease a superfamily
    • D'Alessio G. and Riordan J. F. (eds), Academic Press, San Diego
    • Beintema J. J., Breukelman H. F., Carsana A. and Furia A. (1997) Evolution of vertebrate ribonucleases: ribonuclease A superfamily. In: Ribonucleases: Structures and Functions, pp. 245-269, D'Alessio G. and Riordan J. F. (eds), Academic Press, San Diego
    • (1997) Ribonucleases: Structures and Functions , pp. 245-269
    • Beintema, J.J.1    Breukelman, H.F.2    Carsana, A.3    Furia, A.4
  • 46
    • 0024291642 scopus 로고
    • Structure of phosphate-free ribonuclease A refined at 1.26 Å
    • Wlodaver A., Svensson L. A., Sjolin L. and Gilliland G. L. (1988) Structure of phosphate-free ribonuclease A refined at 1.26 Å. Biochemistry 27: 2705-2717
    • (1988) Biochemistry , vol.27 , pp. 2705-2717
    • Wlodaver, A.1    Svensson, L.A.2    Sjolin, L.3    Gilliland, G.L.4


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