메뉴 건너뛰기




Volumn 7, Issue 11, 1999, Pages

Glycyl radical enzymes: A conservative structural basis for radicals

Author keywords

[No Author keywords available]

Indexed keywords

ENZYME; FORMATE ACETYLTRANSFERASE; RADICAL; RIBONUCLEOTIDE REDUCTASE; UNCLASSIFIED DRUG;

EID: 0033571352     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(00)80019-2     Document Type: Review
Times cited : (69)

References (34)
  • 1
    • 0025293287 scopus 로고
    • Three-dimensional structure of the free radical protein of ribonucleotide reductase
    • Nordlund, P., Sjöberg, B.-M. & Eklund, H. (1990). Three-dimensional structure of the free radical protein of ribonucleotide reductase. Nature 345, 593-598.
    • (1990) Nature , vol.345 , pp. 593-598
    • Nordlund, P.1    Sjöberg, B.-M.2    Eklund, H.3
  • 2
    • 0026801085 scopus 로고
    • A model for the role of multiple cysteine residues involved in ribonucleotide reduction: Amazing and still confusing
    • Mao, S.S., et al., & Stubbe, J. (1992). A model for the role of multiple cysteine residues involved in ribonucleotide reduction: Amazing and still confusing. Biochemistry 31, 9733-9743.
    • (1992) Biochemistry , vol.31 , pp. 9733-9743
    • Mao, S.S.1    Stubbe, J.2
  • 3
    • 0030028971 scopus 로고    scopus 로고
    • Thiyl radicals in ribonucleotide reductases
    • Licht, S., Gerten, G.J. & Stubbe, J. (1996). Thiyl radicals in ribonucleotide reductases. Science 271, 477-481.
    • (1996) Science , vol.271 , pp. 477-481
    • Licht, S.1    Gerten, G.J.2    Stubbe, J.3
  • 4
    • 13344279373 scopus 로고    scopus 로고
    • The free radical of the anaerobic ribonucleotide reductase from Escherichia coli is at glycine 681
    • Sun, X.Y., et al., & Sjöberg, B.-M. (1996). The free radical of the anaerobic ribonucleotide reductase from Escherichia coli is at glycine 681. J. Biol. Chem. 271, 6827-6831.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6827-6831
    • Sun, X.Y.1    Sjöberg, B.-M.2
  • 5
    • 0029048182 scopus 로고
    • Formate is the hydrogen donor for the anaerobic ribonucleotide reductase from Escherichia coli
    • Mulliez, E., Ollagnier, S., Fontecave, M., Eliasson, R. & Reichard, P. (1995). Formate is the hydrogen donor for the anaerobic ribonucleotide reductase from Escherichia coli. Proc. Natl Acad. Sci. USA 92, 8759-8762.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 8759-8762
    • Mulliez, E.1    Ollagnier, S.2    Fontecave, M.3    Eliasson, R.4    Reichard, P.5
  • 7
    • 0027177564 scopus 로고
    • From RNA to DNA, why so many ribonucleotide reductases?
    • Reichard, P. (1993). From RNA to DNA, why so many ribonucleotide reductases? Science 260, 1773-1777.
    • (1993) Science , vol.260 , pp. 1773-1777
    • Reichard, P.1
  • 9
    • 0028486194 scopus 로고
    • Structure of ribonucleotide reductase protein R1
    • Uhlin, U. & Eklund, H. (1994). Structure of ribonucleotide reductase protein R1. Nature 370, 533-539.
    • (1994) Nature , vol.370 , pp. 533-539
    • Uhlin, U.1    Eklund, H.2
  • 10
    • 0031025616 scopus 로고    scopus 로고
    • Ribonucleotide reductase in the archaeon Pyrococcus furiosus: A critical enzyme in the evolution of DNA genomes?
    • Riera, J., Robb, FT., Weiss, R. & Fontecave, M. (1997). Ribonucleotide reductase in the archaeon Pyrococcus furiosus: A critical enzyme in the evolution of DNA genomes? Proc. Natl Acad. Sci. USA 94, 475-478.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 475-478
    • Riera, J.1    Robb, F.T.2    Weiss, R.3    Fontecave, M.4
  • 11
    • 0030614339 scopus 로고    scopus 로고
    • 12-dependent ribonucleotide reductase from the archaebacterium Thermoplasma acidophila: An evolutionary solution to the ribonucleotide reductase conundrum
    • 12-dependent ribonucleotide reductase from the archaebacterium Thermoplasma acidophila: An evolutionary solution to the ribonucleotide reductase conundrum. Proc. Natl Acad. Sci. USA 94, 53-58.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 53-58
    • Tauer, A.1    Benner, S.A.2
  • 12
    • 0031471116 scopus 로고    scopus 로고
    • B12-dependent ribonucleotide reductases from deeply rooted eubacteria are structurally related to the aerobic enzyme from Escherichia coli
    • Jordan, A., et al., & Reichard, P. (1997). B12-dependent ribonucleotide reductases from deeply rooted eubacteria are structurally related to the aerobic enzyme from Escherichia coli. Proc. Natl Acad. Sci. USA 94, 13487-13492.
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 13487-13492
    • Jordan, A.1    Reichard, P.2
  • 13
    • 0029918138 scopus 로고    scopus 로고
    • The anaerobic Escherichia coli ribonucleotide reductase - Subunit structure and iron sulfur center
    • Ollagnier, S., et al., & Reichard, P. (1996). The anaerobic Escherichia coli ribonucleotide reductase - Subunit structure and iron sulfur center. J. Biol. Chem. 271, 9410-9416.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9410-9416
    • Ollagnier, S.1    Reichard, P.2
  • 14
    • 9844228508 scopus 로고    scopus 로고
    • Activation of the anaerobic ribonucleotide reductase from Escherichia coli - The essential role of the iron-sulfur center for S-adenosylmethionine reduction
    • Ollagnier, S., et al., & Fontecave, M. (1997). Activation of the anaerobic ribonucleotide reductase from Escherichia coli - The essential role of the iron-sulfur center for S-adenosylmethionine reduction. J. Biol. Chem. 272, 24216-24223.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24216-24223
    • Ollagnier, S.1    Fontecave, M.2
  • 15
    • 0031571616 scopus 로고    scopus 로고
    • Binding of allosteric effectors to ribonucleotide reductase protein R1 : Reduction of active-site cysteines promotes substrate binding
    • Eriksson, M., et al., & Eklund, H. (1997). Binding of allosteric effectors to ribonucleotide reductase protein R1 : Reduction of active-site cysteines promotes substrate binding. Structure 5, 1077-1092.
    • (1997) Structure , vol.5 , pp. 1077-1092
    • Eriksson, M.1    Eklund, H.2
  • 16
    • 0033525599 scopus 로고    scopus 로고
    • A glycyl radical site in the crystal structure of a class III ribonucleotide reductase
    • Logan, D., Andersson, J., Sjöberg, B.-M. & Nordlund, P. (1999). A glycyl radical site in the crystal structure of a class III ribonucleotide reductase. Science 283, 1499-1504.
    • (1999) Science , vol.283 , pp. 1499-1504
    • Logan, D.1    Andersson, J.2    Sjöberg, B.-M.3    Nordlund, P.4
  • 17
    • 0000062832 scopus 로고    scopus 로고
    • Pyruvate formate-lyase is structurally homologous to type I ribonucleotide reductase
    • Leppänen, V.-M., et al., & Goldman, A. (1999). Pyruvate formate-lyase is structurally homologous to type I ribonucleotide reductase. Structure 7, 733-744.
    • (1999) Structure , vol.7 , pp. 733-744
    • Leppänen, V.-M.1    Goldman, A.2
  • 18
    • 0032851377 scopus 로고    scopus 로고
    • Structure and mechanism of the glycyl radical enzyme pyruvate formate-lyase
    • Becker, A., et al., & Wagner, A.F.V (1999). Structure and mechanism of the glycyl radical enzyme pyruvate formate-lyase. Nat. Struct. Biol., 6, 969-975.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 969-975
    • Becker, A.1    Wagner, A.F.V.2
  • 19
    • 0028034941 scopus 로고
    • Allosteric control of the substrate specificity of the anaerobic ribonucleotide reductase from Escherichia coli
    • Eliasson, R., Pontis, E., Sun, X.Y. & Reichard, P. (1994). Allosteric control of the substrate specificity of the anaerobic ribonucleotide reductase from Escherichia coli. J. Biol. Chem. 269, 26052-26057.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26052-26057
    • Eliasson, R.1    Pontis, E.2    Sun, X.Y.3    Reichard, P.4
  • 20
    • 0029157060 scopus 로고
    • Glycyl free radical in pyruvate formate lyase: Synthesis, structure characteristics, and involvement in catalysis
    • Knappe, J. & Wagner, A.F. (1995). Glycyl free radical in pyruvate formate lyase: Synthesis, structure characteristics, and involvement in catalysis. Methods Enzymol. 258, 343-362.
    • (1995) Methods Enzymol. , vol.258 , pp. 343-362
    • Knappe, J.1    Wagner, A.F.2
  • 21
    • 0029006940 scopus 로고
    • Electron paramagnetic resonance evidence for a cysteine-based radical in pyruvate formate-lyase inactivated with mercaptopyruvate
    • Parast, C.V., Wong, K.W., Kozarich, J.W., Peisach, J. & Magliozzo, R.S. (1995). Electron paramagnetic resonance evidence for a cysteine-based radical in pyruvate formate-lyase inactivated with mercaptopyruvate. Biochemistry 34, 5712-5717.
    • (1995) Biochemistry , vol.34 , pp. 5712-5717
    • Parast, C.V.1    Wong, K.W.2    Kozarich, J.W.3    Peisach, J.4    Magliozzo, R.S.5
  • 22
    • 0029810886 scopus 로고    scopus 로고
    • Bacteriophage T4 anaerobic ribonucleotide reductase contains a stable glycyl radical at position 580
    • Young, P., Andersson, J., Sahlin, M. & Sjöberg, B.M. (1996). Bacteriophage T4 anaerobic ribonucleotide reductase contains a stable glycyl radical at position 580. J. Biol. Chem. 271, 20770-20775.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20770-20775
    • Young, P.1    Andersson, J.2    Sahlin, M.3    Sjöberg, B.M.4
  • 23
    • 0000830511 scopus 로고
    • Post-translational activation introduces a free radical into pyruvate formate-lyase
    • Knappe, J., Neugebauer, F.A., Blaschkowski, H.P. & Ganzler, M. (1984). Post-translational activation introduces a free radical into pyruvate formate-lyase. Proc. Natl Acad. Sci. USA 81, 1332-1335.
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 1332-1335
    • Knappe, J.1    Neugebauer, F.A.2    Blaschkowski, H.P.3    Ganzler, M.4
  • 24
    • 0028275314 scopus 로고
    • 2H]glycine-substituted enzyme and peptides homologous to the glycine 734 site
    • 2H]glycine-substituted enzyme and peptides homologous to the glycine 734 site. J. Biol. Chem. 269, 12432-12437.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12432-12437
    • Frey, M.1    Rothe, M.2    Wagner, A.F.3    Knappe, J.4
  • 25
    • 0028908959 scopus 로고
    • Mass spectrometric determination of the radical scission site in the anaerobic ribonucleotide reductase of Escherichia coli
    • King, D.S. & Reichard, P. (1995). Mass spectrometric determination of the radical scission site in the anaerobic ribonucleotide reductase of Escherichia coli. Biochem. Biophys. Res. Commun. 206, 731-735.
    • (1995) Biochem. Biophys. Res. Commun. , vol.206 , pp. 731-735
    • King, D.S.1    Reichard, P.2
  • 26
    • 0029812067 scopus 로고    scopus 로고
    • Two conserved tyrosine residues in protein R1 participate in an intermolecular electron transfer in ribonucleotide reductase
    • Ekberg, M., Sahlin, M., Eriksson, M. & Sjöberg, B.M. (1996). Two conserved tyrosine residues in protein R1 participate in an intermolecular electron transfer in ribonucleotide reductase. J. Biol. Chem. 271, 20655-20659.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20655-20659
    • Ekberg, M.1    Sahlin, M.2    Eriksson, M.3    Sjöberg, B.M.4
  • 27
    • 0031465450 scopus 로고    scopus 로고
    • A new mechanism-based radical intermediate in a mutant R1 protein affecting the catalytically essential Glu441 in Escherichia coli ribonucleotide reductase
    • Persson, A.L, et al., & Sjöberg, B.-M. (1997). A new mechanism-based radical intermediate in a mutant R1 protein affecting the catalytically essential Glu441 in Escherichia coli ribonucleotide reductase. J. Biol. Chem. 272, 31533-31541.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31533-31541
    • Persson, A.L.1    Sjöberg, B.-M.2
  • 28
    • 0032023777 scopus 로고    scopus 로고
    • Protein radicals in enzyme catalysis
    • van der Donk, W.A. & Stubbe, J. (1998). Protein radicals in enzyme catalysis. Chem. Rev. 98, 705-762.
    • (1998) Chem. Rev. , vol.98 , pp. 705-762
    • Van Der Donk, W.A.1    Stubbe, J.2
  • 29
    • 0002131030 scopus 로고    scopus 로고
    • Chemistry and biochemistry of B12
    • (Banerjee, R., ed.), John Wiley and Sons Inc., New York
    • 12. (Banerjee, R., ed.), pp. 731 -756, John Wiley and Sons Inc., New York.
    • (1999) 12. , pp. 731-756
    • Fontecave, M.1    Mulliez, E.2
  • 31
    • 0029093215 scopus 로고
    • The mechanism of the anaerobic Eschericha coli ribonucleotide reductase investigated with nuclear magnetic resonance spectroscopy
    • Eliasson, R., et al. & Otting, G. (1995). The mechanism of the anaerobic Eschericha coli ribonucleotide reductase investigated with nuclear magnetic resonance spectroscopy. Biochem. Biophys. Res. Commun. 214, 28-35.
    • (1995) Biochem. Biophys. Res. Commun. , vol.214 , pp. 28-35
    • Eliasson, R.1    Otting, G.2
  • 32
    • 0027320421 scopus 로고
    • Pyruvate formate-lyase mechanism involving the protein-based glycyl radical
    • Knappe, J., Elbert, S., Frey, M. & Wagner, A.F.V. (1993). Pyruvate formate-lyase mechanism involving the protein-based glycyl radical. Biochem. Soc. Trans. 21, 731-734.
    • (1993) Biochem. Soc. Trans. , vol.21 , pp. 731-734
    • Knappe, J.1    Elbert, S.2    Frey, M.3    Wagner, A.F.V.4
  • 33
    • 0028804728 scopus 로고
    • Hydrogen exchange of the glycyl radical of pyruvate formate-lyase is catalysed by cysteine 419
    • Parast, C.V., Wong, K.K., Lewisch, S.A. & Kozarich, J.W. (1995). Hydrogen exchange of the glycyl radical of pyruvate formate-lyase is catalysed by cysteine 419. Biochemistry 34, 2392-2399.
    • (1995) Biochemistry , vol.34 , pp. 2392-2399
    • Parast, C.V.1    Wong, K.K.2    Lewisch, S.A.3    Kozarich, J.W.4
  • 34
    • 0032508865 scopus 로고    scopus 로고
    • Catalytic mechanism of pyruvate formate lyase (PFL), A theoretical study
    • Himo, F. & Eriksson, LA. (1998). Catalytic mechanism of pyruvate formate lyase (PFL). A theoretical study. J. Am. Chem. Soc. 120, 11449-11455.
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 11449-11455
    • Himo, F.1    Eriksson, L.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.