메뉴 건너뛰기




Volumn 26, Issue 2, 2001, Pages 93-99

The evolution of ribonucleotide reduction revisited

Author keywords

[No Author keywords available]

Indexed keywords

DEOXYRIBONUCLEOTIDE; PURINE; PYRIMIDINE; RIBONUCLEOTIDE; RIBONUCLEOTIDE REDUCTASE;

EID: 0035252647     PISSN: 09680004     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0968-0004(00)01764-3     Document Type: Review
Times cited : (88)

References (47)
  • 2
    • 0034637161 scopus 로고    scopus 로고
    • The structural basis of ribosome activity in peptide bond synthesis
    • (2000) Science , vol.289 , pp. 920-930
    • Nissen, P.1
  • 7
    • 0033525599 scopus 로고    scopus 로고
    • A glycyl radical site in the crystal structure of a class III ribonucleotide reductase
    • (1999) Science , vol.283 , pp. 1499-1504
    • Logan, D.T.1
  • 8
    • 0000062832 scopus 로고    scopus 로고
    • Pyruvate formate lyase is structurally homologous to type I ribonucleotide reductase
    • (1999) Struct. Fold. Des. , vol.7 , pp. 733-744
    • Leppanen, V.1
  • 9
    • 0032851377 scopus 로고    scopus 로고
    • Structure and mechanism of the glycyl radical enzyme pyruvate formate-lyase
    • (1999) Nat. Struct. Biol. , vol.6 , Issue.10 , pp. 969-975
    • Becker, A.1
  • 10
    • 0031571616 scopus 로고    scopus 로고
    • Binding of allosteric effectors to ribonucleotide reductase protein R1: Reduction of active-site cysteines promotes substrate binding
    • (1997) Structure , vol.5 , pp. 1077-1092
    • Eriksson, M.1
  • 11
    • 0019182317 scopus 로고
    • On the mechanism of ribonucleoside diphosphate reductase from Escherichia coli. Evidence for 3′ C-H bond cleavage
    • (1980) J. Biol. Chem. , vol.255 , pp. 18027-18030
    • Stubbe, J.1    Ackles, D.2
  • 12
    • 0022339341 scopus 로고
    • Mechanism of inactivation of Escherichia coli ribonucleotide reductase by 2′-chloro-2′-deoxyuridine 5′-diphosphate: Evidence for generation of a 2′-deoxy-3′-ketonucleotide via a net 1,2 hydrogen shift
    • (1985) Biochemistry , vol.24 , pp. 7214-7221
    • Ator, M.A.1    Stubbe, J.2
  • 13
    • 0023643435 scopus 로고
    • Location of the redox-active thiols of ribonucleotide reductase: Sequence similarity between the Escherichia coli and Lactobacillus leichmannii enzymes
    • (1987) Biochemistry , vol.26 , pp. 6905-6909
    • Lin, A.I.1
  • 14
    • 0019444286 scopus 로고
    • On the mechanism of ribonucleoside triphosphate reductase from Lactobacillus leichmannii: Evidence for 3′ C-H bond cleavage
    • (1981) J. Biol. Chem. , vol.256 , pp. 4843-4846
    • Stubbe, J.1
  • 15
    • 0028172124 scopus 로고
    • Coenzyme B12-dependent ribonucleotide reductase: Evidence for the participation of five cysteine residues in ribonucleotide reduction
    • (1994) Biochemistry , vol.33 , pp. 12676-12685
    • Booker, S.1
  • 16
    • 0030028971 scopus 로고    scopus 로고
    • Thiyl radicals in ribonucleotide reductases
    • (1996) Science , vol.271 , pp. 477-481
    • Licht, S.1
  • 18
    • 0028053807 scopus 로고
    • Interactions of 2′-modified azidoanalogs and haloanalogs of deoxycytidine 5′-triphosphate with the anaerobic ribonucleotide reductase of Escherichia coli
    • (1994) J. Biol. Chem. , vol.269 , pp. 26116-26120
    • Eliasson, R.1
  • 19
  • 21
    • 0000289664 scopus 로고    scopus 로고
    • Mechanistic investigations of ribonucleotide reductases
    • Comprehensive Natural Products Chemistry (Barton, S.D. et al., eds.), Elsevier Science
    • (1999) , vol.5 , pp. 163
    • Licht, S.1    Stubbe, J.2
  • 23
    • 9844228508 scopus 로고    scopus 로고
    • Activation of the anaerobic ribonucleotide reductase from Escherichia coli
    • (1997) J. Biol. Chem. , vol.272 , pp. 24216-24223
    • Ollagnier, S.1
  • 24
    • 0034717328 scopus 로고    scopus 로고
    • The activating component of the anaerobic ribonucleotide reductase from Escherichia coli - An iron-sulfur center with only three cysteines
    • (2000) J. Biol. Chem. , vol.275 , pp. 15669-15675
    • Tamarit, J.1
  • 29
    • 0034734328 scopus 로고    scopus 로고
    • +1 cluster of pyruvate formate-lyase activating enzyme generates the glycyl radical on pyruvate formate-lyase: EPR-detected single turnover
    • (2000) J.Am. Chem. Soc. , vol.122 , pp. 8331-8332
    • Henshaw, T.F.1
  • 30
    • 0034733603 scopus 로고    scopus 로고
    • Cysteines involved in radical generation and catalysis of class III anaerobic ribonucleotide reductase
    • (2000) J. Biol. Chem. , vol.275 , pp. 19449-19455
    • Andersson, J.1
  • 31
    • 0031471116 scopus 로고    scopus 로고
    • B12-dependent ribonucleotide reductases from deeply rooted eubacteria are structurally related to the aerobic enzyme from Escherichia coli
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 13487-13492
    • Jordan, A.1
  • 33
    • 0028804728 scopus 로고
    • Hydrogen exchange of the glycyl radical of pyruvate formate-lyase is catalyzed by cysteine 419
    • (1995) Biochemistry , vol.34 , pp. 2393-2399
    • Parast, C.V.1
  • 34
    • 0029812067 scopus 로고    scopus 로고
    • Two conserved tyrosine residues in protein R1 participate in an intermolecular electron transfer in ribonucleotide reductase
    • (1996) J. Biol. Chem. , vol.271 , pp. 20655-20659
    • Ekberg, M.1
  • 37
    • 0028034941 scopus 로고
    • Allosteric control of the substrate specificity of the anaerobic ribonucleotide reductase from Escherichia coli
    • (1994) J. Biol. Chem. , vol.269 , pp. 26052-26057
    • Eliasson, R.1
  • 38
    • 0033548274 scopus 로고    scopus 로고
    • Allosteric control of three B12-dependent (class II) ribonucleotide reductases
    • (1999) J. Biol. Chem. , vol.274 , pp. 7182-7189
    • Eliasson, R.1
  • 39
    • 0027177564 scopus 로고
    • From RNA to DNA, why so many ribonucleotide reductases
    • (1993) Science , vol.260 , pp. 1773-1777
    • Reichard, P.1
  • 40
    • 0034723174 scopus 로고    scopus 로고
    • The anaerobic (class III) ribonucleotide reductase from Lactococcus lactis
    • (1999) J. Biol. Chem. , vol.275 , pp. 2463-2471
    • Torrents, E.1
  • 41
    • 0017056054 scopus 로고
    • Allosterism, regulation, and cooperativity: The case of ribonucleotide reductase of Lactobacillus leichmannii
    • (1977) Adv. Enzyme Regul. , vol.15 , pp. 81-101
    • Singh, D.1
  • 42
    • 0034733578 scopus 로고    scopus 로고
    • Allosteric regulation of the class III anaerobic ribonucleotide reductase from bacteriophage T4
    • (2000) J. Biol. Chem. , vol.275 , pp. 19443-19448
    • Andersson, J.1
  • 44
    • 0032491527 scopus 로고    scopus 로고
    • Allosteric regulation of vaccinia virus ribonucleotide reductase, analysed by simultaneous monitoring of its four activities
    • (1998) J. Biol. Chem. , vol.273 , pp. 29512-29518
    • Hendricks, S.1    Mathews, C.2
  • 46
    • 0027297718 scopus 로고
    • Lysine 2,3-aminomutase - Is adenosylmethionine a poorman's adenosylcobalamin?
    • (1993) FASEB J. , vol.7 , pp. 662-670
    • Frey, P.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.