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Volumn 77, Issue 3, 2001, Pages 177-268

Structure and function of the radical enzyme ribonucleotide reductase

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; AZIDE; CARBOXYL GROUP; IRON; RIBONUCLEOTIDE REDUCTASE;

EID: 0035544604     PISSN: 00796107     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0079-6107(01)00014-1     Document Type: Review
Times cited : (273)

References (247)
  • 4
  • 7
    • 0030746616 scopus 로고    scopus 로고
    • Mechanism based inactivation of the adenosylcobalamin-dependent ribonucleotide reductase from L-leichmannii by 2′-ara-2′-azido-2′-deoxy adenosine-5′-triphosphate: Observation of paramagnetic intermediates
    • (1997) Tetrahedron , vol.53 , pp. 12005-12016
    • Ashley, G.W.1    Lawrence, C.C.2    Stubbe, J.3    Robins, M.J.4
  • 27
    • 0029774568 scopus 로고    scopus 로고
    • Deoxyribonucleotide synthesis in green algae. Cell cycle fluctuation of ribonucleotide reductase is only moderate in the unicellular, exsymbiotic green algae, Chlorella sp pbi
    • (1996) J. Plant Physiol. , vol.148 , pp. 657-661
    • Bornemann, C.1    Drude, K.2    Follmann, H.3
  • 31
    • 0026048737 scopus 로고
    • Investigation of an octapeptide inhibitor of Escherichia coli ribonucleotide reductase by transferred nuclear overhauser effect spectroscopy
    • (1991) Biochemistry , vol.30 , pp. 8144-8151
    • Bushweller, J.1    Bartlett, P.2
  • 32
    • 0023881789 scopus 로고
    • Molecular cloning of the cDNA for a mutant mouse ribonucleotide reductase M1 that produces a dominant mutator phenotype in mammalian cells
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 2698-2704
    • Caras, I.W.1    Martin Jr., D.W.2
  • 34
    • 0034625375 scopus 로고    scopus 로고
    • Controlled protein degradation regulates ribonucleotide reductase activity in proliferating mammalian cells during the normal cell cycle and in response to DNA damage and replication blocks
    • (2000) J. Biol. Chem. , vol.275 , pp. 17747-17753
    • Chabes, A.1    Thelander, L.2
  • 48
    • 0034651543 scopus 로고    scopus 로고
    • When fold is not important: A common structural framework for adenine and AMP binding in 12 unrelated protein families
    • (2000) Proteins , vol.38 , pp. 310-326
    • Denessiouk, K.A.1    Johnson, M.S.2
  • 70
    • 0028862302 scopus 로고
    • Role of a proximal NF-Y binding promoter element in S phase-specific expression of mouse ribonucleotide reductase R2 gene
    • (1995) J. Biol. Chem. , vol.270 , pp. 25239-25243
    • Filatov, D.1    Thelander, L.2
  • 95
    • 0030813561 scopus 로고    scopus 로고
    • Identification of RNR4, encoding a second essential small subunit of ribonucleotide reductase in Saccharomyces cerevisiae
    • (1997) Mol. Cell Biol. , vol.17 , pp. 6105-6113
    • Huang, M.X.1    Elledge, S.J.2
  • 98
    • 0029896950 scopus 로고    scopus 로고
    • A kinetic study on the influence of nucleoside triphosphate effectors on subunit interaction in mouse ribonucleotide reductase
    • (1996) Biochemistry , vol.35 , pp. 8603-8609
    • Ingemarson, R.1    Thelander, L.2
  • 102
  • 105
    • 0029618389 scopus 로고
    • Two different operons for the same function: Comparison of the Salmonella typhimurium nrdAB and nrdEF genes
    • (1995) Gene , vol.167 , pp. 75-79
    • Jordan, A.1    Gibert, I.2    Barbé, J.3
  • 112
  • 115
    • 0029157060 scopus 로고
    • Glycyl free radical in pyruvate formate lyase: Synthesis, structure characteristics, and involvement in catalysis
    • (1995) Meth. Enzymol. , vol.258 , pp. 343-362
    • Knappe, J.1    Wagner, A.F.2
  • 117
    • 0023746738 scopus 로고
    • Mutagenesis and deoxyribonucleotide pool imbalance
    • (1988) Mutat. Res. , vol.200 , pp. 133-147
    • Kunz, B.A.1
  • 124
    • 0035036499 scopus 로고    scopus 로고
    • Syntheses and antitumor activities of potent inhibitors of ribonucleotide reductase: 3-amino-4-methylpyridine-2-carboxaldehyde-thiosemicarba-zone (3-AMP), 3-amino-pyridine-2-carboxaldehyde-thiosemicarbazone (3-AP) and its water-soluble prodrugs
    • (2001) Curr. Med. Chem. , vol.8 , pp. 121-133
    • Li, J.1    Zheng, L.M.2    King, I.3    Doyle, T.W.4    Chen, S.H.5
  • 135
    • 0029126928 scopus 로고
    • Demonstration of segmental mobility in the functionally essential carboxyl terminal part of ribonucleotide reductase protein R2 from Escherichia coli
    • (1995) FEBS Lett. , vol.368 , pp. 441-444
    • Lycksell, P.O.1    Sahlin, M.2
  • 142
    • 0021253747 scopus 로고
    • The genetic consequences of nucleotide precursor pool imbalance in mammalian cells
    • (1984) Mutat. Res. , vol.126 , pp. 107-112
    • Meuth, M.1
  • 143
    • 0024505072 scopus 로고
    • The molecular basis of mutations induced by deoxyribonucleoside triphosphate pool imbalances in mammalian cells
    • (1989) Exp. Cell. Res. , vol.181 , pp. 305-316
    • Meuth, M.1
  • 160
    • 0029657918 scopus 로고    scopus 로고
    • The Cys292→Ala substitution in protein R1 of class I ribonucleotide reductase from Escherichia coli has a global effect on nucleotide binding at the specificity-determining allosteric site
    • (1996) Eur. J. Biochem. , vol.241 , pp. 363-367
    • Ormö, M.1    Sjöberg, B.M.2
  • 178
    • 0027177564 scopus 로고
    • From RNA to DNA, why so many ribonucleotide reductases?
    • (1993) Science , vol.260 , pp. 1773-1777
    • Reichard, P.1
  • 179
    • 0031106730 scopus 로고    scopus 로고
    • The evolution of ribonucleotide reduction
    • (1997) TIBS , vol.22 , pp. 81-85
    • Reichard, P.1
  • 195
    • 0032569201 scopus 로고    scopus 로고
    • Theoretical study of the substrate mechanism of ribonucleotide reductase
    • (1998) JACS , vol.120 , pp. 8417
    • Siegbahn, P.E.M.1
  • 197
    • 0028774182 scopus 로고
    • The ribonucleotide reductase jigsaw puzzle: A large piece falls into place
    • (1994) Structure , vol.2 , pp. 793-796
    • Sjöberg, B.M.1
  • 198
    • 0000613073 scopus 로고    scopus 로고
    • Ribonucleotide reductases - A group of enzymes with different metallosites and a similar reaction mechanism
    • (1997) Struct. Bonding , vol.88 , pp. 139-173
    • Sjöberg, B.M.1
  • 207
    • 0028776303 scopus 로고
    • Protein structure. Controlling radical reactions
    • (1994) Nature , vol.370 , pp. 502
    • Stubbe, J.1
  • 222
    • 0030614339 scopus 로고    scopus 로고
    • The B-12-dependent ribonucleotide reductase from the archaebacterium Thermoplasma acidophila: An evolutionary solution to the ribonucleotide reductase conundrum
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 53-58
    • Tauer, A.1    Benner, S.A.2
  • 233
    • 0027493255 scopus 로고
    • Crystallization and crystallographic investigations of ribonucleotide reductase protein R1 from Escherichia coli
    • (1993) FEBS Lett. , vol.336 , pp. 148-152
    • Uhlin, U.1    Uhlin, T.2    Eklund, H.3
  • 238
    • 0017669982 scopus 로고
    • Ribonucleotide reductase from Escherichia coli. Identification of allosteric effector sites by chromatography on immobilized effectors
    • (1977) Biochemistry , vol.16 , pp. 4368-4371
    • Von Döbeln, U.1
  • 245
    • 0028099575 scopus 로고
    • Isolation of ribonucleotide reductase from Mycobacterium tuberculosis and cloning, expression, and purification of the large subunit
    • (1994) J. Bacteriol. , vol.176 , pp. 6738-6743
    • Yang, F.D.1    Lu, G.Z.2    Rubin, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.