메뉴 건너뛰기




Volumn 11, Issue 3, 2000, Pages 408-413

Sulfur shuffle: Modulating enzymatic activity by thiol-disulfide interchange

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; CATALYST ACTIVITY; CHAINS; ENZYME ACTIVITY; HYDROGEN BONDS; RNA; SULFUR;

EID: 0034071454     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc990142m     Document Type: Article
Times cited : (16)

References (36)
  • 1
    • 0014288823 scopus 로고
    • Binding of phosphate ligands to ribonuclease A
    • Anderson, D. G., Hammes, G. C., and Walz, F. G. J. (1968) Binding of Phosphate Ligands to Ribonuclease A. Biochemistry 7, 1637-1645.
    • (1968) Biochemistry , vol.7 , pp. 1637-1645
    • Anderson, D.G.1    Hammes, G.C.2    Walz, F.G.J.3
  • 3
    • 0020110250 scopus 로고
    • Activity staining of nucleolytic enzymes after SDS-PAGE: Use of aqueous isopropanol to remove detergent from gels
    • Blank, A., Sugiyama, R. H., and Dekker, C. A. (1982) Activity staining of nucleolytic enzymes after SDS-PAGE: use of aqueous isopropanol to remove detergent from gels. Anal. Biochem. 120, 267-275.
    • (1982) Anal. Biochem. , vol.120 , pp. 267-275
    • Blank, A.1    Sugiyama, R.H.2    Dekker, C.A.3
  • 5
    • 0011194467 scopus 로고
    • A new approach toward the inhibition of ribonucleases: A water-stable ribonucleoside-technetium chelate
    • Chen, Y.-C. J., and Janda, K. D. (1992) A new approach toward the inhibition of ribonucleases: a water-stable ribonucleoside-technetium chelate. J. Am. Chem. Soc. 114, 1488-1489.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 1488-1489
    • Chen, Y.-C.J.1    Janda, K.D.2
  • 6
    • 0018735516 scopus 로고
    • Statistical analysis of enzyme kinetic data
    • Cleland, W. W. (1979) Statistical analysis of enzyme kinetic data. Methods Enzymol. 63, 103-138.
    • (1979) Methods Enzymol. , vol.63 , pp. 103-138
    • Cleland, W.W.1
  • 7
    • 0032845707 scopus 로고    scopus 로고
    • Energetics of substrate binding, catalysis, and product release
    • Cleland, W. W., and Northrop, D. B. (1999) Energetics of substrate binding, catalysis, and product release. Methods Enzymol. 308, 3-27.
    • (1999) Methods Enzymol. , vol.308 , pp. 3-27
    • Cleland, W.W.1    Northrop, D.B.2
  • 9
    • 0028275049 scopus 로고
    • Structural determinants of enzymatic processivity
    • delCardayré, S. B., and Raines, R. T. (1994) Structural Determinants of Enzymatic Processivity. Biochemistry 33, 6032-6037.
    • (1994) Biochemistry , vol.33 , pp. 6032-6037
    • DelCardayré, S.B.1    Raines, R.T.2
  • 10
    • 0029032586 scopus 로고
    • Engineering ribonuclease a: Production, purification, and characterization of wild-type enzyme and mutants at Gln11
    • delCardayré, S. B., Ribó, M., Yokel, E. M., Quirk, D. J., Rutter, W. J., and Raines, R. T. (1995) Engineering ribonuclease A: production, purification, and characterization of wild-type enzyme and mutants at Gln11. Protein Eng. 8, 261-273.
    • (1995) Protein Eng. , vol.8 , pp. 261-273
    • DelCardayré, S.B.1    Ribó, M.2    Yokel, E.M.3    Quirk, D.J.4    Rutter, W.J.5    Raines, R.T.6
  • 11
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • Ellman, G. L. (1959) Tissue sulfhydryl groups. Arch. Biochem. Biophys. 82, 70-77.
    • (1959) Arch. Biochem. Biophys. , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 13
    • 0029057710 scopus 로고
    • Reversible introduction of thiol compounds into proteins by use of activated mixed disulfides
    • Faulstich, H., and Heintz, D. (1995) Reversible introduction of thiol compounds into proteins by use of activated mixed disulfides. Methods Enzymol. 251, 357-366.
    • (1995) Methods Enzymol. , vol.251 , pp. 357-366
    • Faulstich, H.1    Heintz, D.2
  • 14
    • 0029119934 scopus 로고
    • Examining the structural and chemical flexibility of the active site base, Lys-258, of Eschericia coli aspartate aminotransferase by replacement with unnatural amino acids
    • Gloss, L. M., and Kirsch, J. F. (1995) Examining the structural and chemical flexibility of the active site base, Lys-258, of Eschericia coli aspartate aminotransferase by replacement with unnatural amino acids. Biochemistry 34, 12323-12332.
    • (1995) Biochemistry , vol.34 , pp. 12323-12332
    • Gloss, L.M.1    Kirsch, J.F.2
  • 15
    • 0029002917 scopus 로고
    • Effects of chemical modification on the binding activities of P-selectin mutants
    • Hollenbaugh, D., Aruffo, A., and Senter, P. D. (1995) Effects of Chemical Modification on the Binding Activities of P-Selectin Mutants. Biochemistry 34, 5678-5684.
    • (1995) Biochemistry , vol.34 , pp. 5678-5684
    • Hollenbaugh, D.1    Aruffo, A.2    Senter, P.D.3
  • 16
    • 0023146180 scopus 로고
    • Reaction of (Bromoacetamido)-nucleoside affinity labels with ribonuclease A: Evidence for steric control of reaction specificity and alkylation rate
    • Hummel, C. F., Pincus, M. R., Brandt-Rauf, P. W., Frei, G. M., and Carty, R. P. (1987) Reaction of (Bromoacetamido)-nucleoside Affinity Labels with Ribonuclease A: Evidence for Steric Control of Reaction Specificity and Alkylation Rate. Biochemistry 26, 135-146.
    • (1987) Biochemistry , vol.26 , pp. 135-146
    • Hummel, C.F.1    Pincus, M.R.2    Brandt-Rauf, P.W.3    Frei, G.M.4    Carty, R.P.5
  • 18
    • 0027512825 scopus 로고
    • Ribonuclease S-peptide as a carrier in fusion proteins
    • Kim, J.-S., and Raines, R. T. (1993) Ribonuclease S-peptide as a carrier in fusion proteins. Protein Sci. 2, 248-356.
    • (1993) Protein Sci. , vol.2 , pp. 248-356
    • Kim, J.-S.1    Raines, R.T.2
  • 19
    • 0000846047 scopus 로고
    • Phosphoryl tristriazole-a new phosphorylating reagent
    • Kraszewski, A., and Stawinski, J. (1980) Phosphoryl tristriazole-a new phosphorylating reagent. Tetrahedron Lett. 21, 2935-2936.
    • (1980) Tetrahedron Lett. , vol.21 , pp. 2935-2936
    • Kraszewski, A.1    Stawinski, J.2
  • 20
    • 0033543235 scopus 로고    scopus 로고
    • Toward rational design of ribonuclease inhibitors: High-resolution crystal strcuture of a ribonuclease A complex with a potent 3′,5′-pyrophosphate-linked dinucleotide inhibitor
    • Leonidas, D. D., Shapiro, R., Irons, L. I., Russo, N., and Acharya, K. R. (1999) Toward Rational Design of Ribonuclease Inhibitors: High-Resolution Crystal Strcuture of a Ribonuclease A Complex with a Potent 3′,5′-Pyrophosphate-Linked Dinucleotide Inhibitor. Biochemistry 38, 10287-10297.
    • (1999) Biochemistry , vol.38 , pp. 10287-10297
    • Leonidas, D.D.1    Shapiro, R.2    Irons, L.I.3    Russo, N.4    Acharya, K.R.5
  • 22
    • 0015936920 scopus 로고
    • Possible transition-state analogs for ribonuclease. The complexes of uridine with oxovanadium(IV) ion and vanadium(V) ion
    • Lindquist, R. N., Lynn, J. L., Jr., and Lienhard, G. E. (1973) Possible Transition-State Analogs for Ribonuclease. The Complexes of Uridine with Oxovanadium(IV) Ion and Vanadium(V) Ion. J. Am. Chem. Soc. 95, 8762-8768.
    • (1973) J. Am. Chem. Soc. , vol.95 , pp. 8762-8768
    • Lindquist, R.N.1    Lynn, J.L.2    Lienhard, G.E.3
  • 24
    • 0028983940 scopus 로고
    • Ribonuclease a: Revealing structure-function relationships with semisynthesis
    • Messmore, J. M., Fuchs, D. N., and Raines, R. T. (1995) Ribonuclease A: Revealing Structure-Function Relationships with Semisynthesis. J. Am. Chem. Soc. 117, 8057-8060.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 8057-8060
    • Messmore, J.M.1    Fuchs, D.N.2    Raines, R.T.3
  • 25
    • 0343872410 scopus 로고
    • Chemical modification and spin-labelling studies of the Arg 87 to Cys (R87c) mutant of staphylococcal nuclease
    • Pease, M. D., Serpersu, E. H., and Mildvan, A. S. (1987) Chemical modification and spin-labelling studies of the Arg 87 to Cys (R87C) mutant of Staphylococcal nuclease. Fed. Proc. 46, 1932.
    • (1987) Fed. Proc. , vol.46 , pp. 1932
    • Pease, M.D.1    Serpersu, E.H.2    Mildvan, A.S.3
  • 26
    • 0030912818 scopus 로고    scopus 로고
    • Nature's transitory covalent bond
    • Raines, R. T. (1997) Nature's transitory covalent bond. Nat. Struct. Biol. 4, 424-427.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 424-427
    • Raines, R.T.1
  • 27
    • 0001005285 scopus 로고    scopus 로고
    • Ribonuclease A
    • Raines, R. T. (1998) Ribonuclease A. Chem. Rev. 98, 1045-1065.
    • (1998) Chem. Rev. , vol.98 , pp. 1045-1065
    • Raines, R.T.1
  • 28
    • 0033591409 scopus 로고    scopus 로고
    • Potent inhibition of mammalian ribonucleases by 3′,5′-pyrophosphate-linked nucleotides
    • Russo, N., and Shapiro, R. (1999) Potent inhibition of mammalian ribonucleases by 3′,5′-pyrophosphate-linked nucleotides. J. Biol. Chem. 274, 14902-14908.
    • (1999) J. Biol. Chem. , vol.274 , pp. 14902-14908
    • Russo, N.1    Shapiro, R.2
  • 29
    • 0000231043 scopus 로고
    • The correlation of ribonuclease activity with specific aspects of tertiary structure
    • Sela, M., Anfinsen, C. B., and Harrington, W. F. (1957) The correlation of ribonuclease activity with specific aspects of tertiary structure. Biochim. Biophys. Acta 26, 502-512.
    • (1957) Biochim. Biophys. Acta , vol.26 , pp. 502-512
    • Sela, M.1    Anfinsen, C.B.2    Harrington, W.F.3
  • 32
    • 0343436631 scopus 로고    scopus 로고
    • New enzymes from old
    • P. A. Frey and D. B. Northrop, Eds. IOS Press, Washington DC.
    • Viola, R. E., and Wright, S. K. (1999) New enzymes from old. In Enzymatic Mechanisms (P. A. Frey and D. B. Northrop, Eds.) pp 116-130, IOS Press, Washington DC.
    • (1999) Enzymatic Mechanisms , pp. 116-130
    • Viola, R.E.1    Wright, S.K.2
  • 33
    • 0000997382 scopus 로고
    • Structure of bovine pancreatic ribonuclease by X-ray and neutron diffraction
    • F. A. Jurnak and A. McPherson, Eds. Wiley, New York
    • Wlodawer, A. (1985) Structure of bovine pancreatic ribonuclease by X-ray and neutron diffraction. In Biological Macromolecules and Assemblies, Vol. II, Nucleic Acids and Interactive Proteins (F. A. Jurnak and A. McPherson, Eds.) pp 395-439, Wiley, New York.
    • (1985) Biological Macromolecules and Assemblies, Vol. II, Nucleic Acids and Interactive Proteins , vol.2 , pp. 395-439
    • Wlodawer, A.1
  • 35
    • 0026574999 scopus 로고
    • A comparative study on the catalytic properies of guanylyl-specific ribonucleases
    • Yakovlev, G. I., Moiseyev, G. P., Bezborodova, S. I., Both, V., and Sevcik, J. (1992) A comparative study on the catalytic properies of guanylyl-specific ribonucleases. Eur. J. Biochem. 204, 187-190.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 187-190
    • Yakovlev, G.I.1    Moiseyev, G.P.2    Bezborodova, S.I.3    Both, V.4    Sevcik, J.5
  • 36
    • 0020523431 scopus 로고
    • Identification of two distinct regulatory regions adjacent to the human β-interferon gene
    • Zinn, K., DiMaio, D., and Maniatis, T. (1983) Identification of two distinct regulatory regions adjacent to the human β-interferon gene. Cell 34, 865-879.
    • (1983) Cell , vol.34 , pp. 865-879
    • Zinn, K.1    DiMaio, D.2    Maniatis, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.