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Volumn 47, Issue 2, 2014, Pages 540-549

Travels with carbon-centered radicals. 5′-deoxyadenosine and 5′-deoxyadenosine-5′-yl in radical enzymology

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EID: 84894244865     PISSN: 00014842     EISSN: 15204898     Source Type: Journal    
DOI: 10.1021/ar400194k     Document Type: Article
Times cited : (40)

References (62)
  • 1
    • 0008611230 scopus 로고
    • An intramolecular oxidation reduction requiring a vitamin B12 coenzyme
    • Abeles, R. H.; Lee, H. A. An intramolecular oxidation reduction requiring a vitamin B12 coenzyme J. Biol. Chem. 1961, 236, 2347-2350
    • (1961) J. Biol. Chem. , vol.236 , pp. 2347-2350
    • Abeles, R.H.1    Lee, H.A.2
  • 4
    • 77954628691 scopus 로고    scopus 로고
    • Cobalamin coenzymes in enzymology
    • Mander, L. Liu, H.-W. Begley, T. Vol. Elsevier: Oxford
    • Frey, P. A. Cobalamin coenzymes in enzymology. In Comprehensive Natural Products II Chemistry and Biology; Mander, L.; Liu, H.-W., Eds.; Begley, T., Vol. Ed.; Elsevier: Oxford, 2010; Vol. 7, pp 501-546.
    • (2010) Comprehensive Natural Products II Chemistry and Biology , vol.7 , pp. 501-546
    • Frey, P.A.1
  • 5
    • 84894247599 scopus 로고
    • 12 coenzyme. PhD Dissertation, Brandeis University, University Microfilms, Ann Arbor, MI - 160
    • 12 coenzyme. PhD Dissertation, Brandeis University, University Microfilms, Ann Arbor, MI, 1967, pp 16-160.
    • (1967) , pp. 16
    • Frey, P.A.1
  • 6
    • 0014010844 scopus 로고
    • The stereochemistry of the conversion of D and L 1,2-propanediols to propionaldehyde
    • Zagalak, B.; Frey, P. A.; Karabatsos, G. L.; Abeles, R. H. The stereochemistry of the conversion of D and L 1,2-propanediols to propionaldehyde J. Biol. Chem. 1966, 241, 3028-3035
    • (1966) J. Biol. Chem. , vol.241 , pp. 3028-3035
    • Zagalak, B.1    Frey, P.A.2    Karabatsos, G.L.3    Abeles, R.H.4
  • 8
    • 0014027350 scopus 로고
    • Studies on the mechanism of action of cobamide coenzymes. Chemical properties of the enzyme-coenzyme complex
    • Wagner, O. W.; Lee, H. A., Jr.; Frey, P. A.; Abeles, R. H. Studies on the mechanism of action of cobamide coenzymes. Chemical properties of the enzyme-coenzyme complex J. Biol. Chem. 1966, 241, 1751-1762
    • (1966) J. Biol. Chem. , vol.241 , pp. 1751-1762
    • Wagner, O.W.1    Lee, Jr.H.A.2    Frey, P.A.3    Abeles, R.H.4
  • 9
    • 0034705081 scopus 로고    scopus 로고
    • Identification of cis-ethanesemidione as the organic radical derived from glycolaldehyde in the suicide inactivation of dioldehydrase and of ethanolamine ammonia-lyase
    • DOI 10.1021/bi992963k
    • Abend, A.; Bandarian, V.; Reed, G. H.; Frey, P. A. Identification of cis-ethanesemidione as the organic radical derived from glycolaldehyde in the suicide inactivation of dioldehydrase and of ethanolamine ammonia-lyase Biochemistry 2000, 39, 6250-6257 (Pubitemid 30327103)
    • (2000) Biochemistry , vol.39 , Issue.20 , pp. 6250-6257
    • Abend, A.1    Bandarian, V.2    Reed, G.H.3    Frey, P.A.4
  • 10
    • 4644359224 scopus 로고    scopus 로고
    • Suicide inactivation of dioldehydratase by glycolaldehyde and chloroacetaldehyde: An examination of the reaction mechanism
    • DOI 10.1021/ja047377f
    • Sandala, G. M.; Smith, D. M.; Coote, M. L.; Radom, L. Suicide inactivation of dioldehydrase by glycolaldehyde and chloroacetaldehyde: an examination of the reaction mechanism J. Am. Chem. Soc. 2004, 126, 12206-12207 (Pubitemid 39304870)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.39 , pp. 12206-12207
    • Sandala, G.M.1    Smith, D.M.2    Coote, M.L.3    Radom, L.4
  • 11
    • 0014010666 scopus 로고
    • 12 coenzyme in the conversion of 1,2-propanediol to propionaldehyde
    • 12 coenzyme in the conversion of 1,2-propanediol to propionaldehyde J. Biol. Chem. 1966, 241, 2732-2733
    • (1966) J. Biol. Chem. , vol.241 , pp. 2732-2733
    • Frey, P.A.1    Abeles, R.H.2
  • 12
    • 0014217409 scopus 로고
    • Studies on the mechanism of hydrogen transfer in the cobamide coenzyme-dependent dioldehydrase reaction
    • Frey, P. A.; Essenberg, M. K.; Abeles, R. H. Studies on the mechanism of hydrogen transfer in the cobamide coenzyme-dependent dioldehydrase reaction J. Biol. Chem. 1967, 242, 5369-5377
    • (1967) J. Biol. Chem. , vol.242 , pp. 5369-5377
    • Frey, P.A.1    Essenberg, M.K.2    Abeles, R.H.3
  • 13
    • 0015935273 scopus 로고
    • Electron spin resonance studies with dioldehydrase. Evidence for radical intermediates in reactions catalyzed by coenzyme B12
    • Finlay, T. H.; Valinsky, J.; Mildvan, A. S.; Abeles, R. H. Electron spin resonance studies with dioldehydrase. Evidence for radical intermediates in reactions catalyzed by coenzyme B12 J. Biol. Chem. 1973, 248, 1285-1290
    • (1973) J. Biol. Chem. , vol.248 , pp. 1285-1290
    • Finlay, T.H.1    Valinsky, J.2    Mildvan, A.S.3    Abeles, R.H.4
  • 14
    • 0022430394 scopus 로고
    • 12-dependent rearangements
    • 12-dependent rearangements Science 1985, 227, 869-875
    • (1985) Science , vol.227 , pp. 869-875
    • Halpern, J.1
  • 15
    • 33845373586 scopus 로고
    • Thermolysis of the cobalt-carbon bond of adenosylcobalamin. 2. Products, kinetics, and cobalt-carbon bond dissociatin energy in aqueous solution
    • Hay, B. P.; Finke, R. G. Thermolysis of the cobalt-carbon bond of adenosylcobalamin. 2. Products, kinetics, and cobalt-carbon bond dissociatin energy in aqueous solution J. Am. Chem. Soc. 1986, 108, 4820-4829
    • (1986) J. Am. Chem. Soc. , vol.108 , pp. 4820-4829
    • Hay, B.P.1    Finke, R.G.2
  • 16
    • 13544256281 scopus 로고    scopus 로고
    • Identification of the 1,2-propanediol-1-yl radical as an intermediate in adenosylcobalamin-dependent diol dehydratase reaction
    • DOI 10.1021/bi0481850
    • Yamanishi, M.; Ide, H.; Murakami, Y.; Toraya, T. Identification of the 1,2-propanediol-1-yl as an intermediate in adenosylcobalamin-dependent diol dehydratase reaction Biochemistry 2005, 44, 2113-2118 (Pubitemid 40223639)
    • (2005) Biochemistry , vol.44 , Issue.6 , pp. 2113-2118
    • Yamanishi, M.1    Ide, H.2    Murakami, Y.3    Toraya, T.4
  • 17
    • 0014939344 scopus 로고
    • Lysine 2,3-aminomutase. Purification and properties of a pyridoxal phosphate and S-adenosylmethionine-activated enzyme
    • Chirpich, T. P.; Zappia, V.; Costilow, R. N.; Barker, H. A. Lysine 2,3-aminomutase. Purification and properties of a pyridoxal phosphate and S-adenosylmethionine-activated enzyme J. Biol. Chem. 1970, 245, 1778-1789
    • (1970) J. Biol. Chem. , vol.245 , pp. 1778-1789
    • Chirpich, T.P.1    Zappia, V.2    Costilow, R.N.3    Barker, H.A.4
  • 18
    • 0023482438 scopus 로고
    • S-adenosylmethionine and the mechanism of hydrogen transfer in the lysine 2,3-aminomutase reaction
    • Frey, P. A.; Moss, M. L. S-Adenosylmethionine and the mechanism of hydrogen transfer in the lysine 2,3-aminomutase reaction Cold Spring Harbor Symp. Quant. Biol., Evol. Catal. Funct. 1987, LII, 571-577 (Pubitemid 18262368)
    • (1987) Cold Spring Harbor Symposia on Quantitative Biology , vol.52 , pp. 571-577
    • Frey, P.A.1    Moss, M.L.2
  • 19
    • 0023645851 scopus 로고
    • The role of S -adenosylmethionine in the lysine 2,3,-aminomutase reaction
    • Moss, M. L.; Frey, P. A. The role of S -adenosylmethionine in the lysine 2,3,-aminomutase reaction J. Biol. Chem. 1987, 262, 14859-14862
    • (1987) J. Biol. Chem. , vol.262 , pp. 14859-14862
    • Moss, M.L.1    Frey, P.A.2
  • 20
    • 0024496311 scopus 로고
    • Lysine 2,3-aminomutase. Support for a mechanism of hydrogen transfer involving S-adenosylmethionine
    • Baraniak, J.; Moss, M. L.; Frey, P. A. Lysine 2,3-aminomutase. Support for a mechanism of hydrogen transfer involving S -adenosylmethionine J. Biol. Chem. 1989, 264, 1357-1360 (Pubitemid 19050969)
    • (1989) Journal of Biological Chemistry , vol.264 , Issue.3 , pp. 1357-1360
    • Baraniak, J.1    Moss, M.L.2    Frey, P.A.3
  • 21
    • 0025119601 scopus 로고
    • Activation of lysine 2,3-aminomutase by S-adenosylmethionine
    • Moss, M. L.; Frey, P. A. Activation of lysine 2,3-aminomutase by S-adenosylmethionine J. Biol. Chem. 1990, 265, 18112-18115
    • (1990) J. Biol. Chem. , vol.265 , pp. 18112-18115
    • Moss, M.L.1    Frey, P.A.2
  • 22
    • 0035895311 scopus 로고    scopus 로고
    • Identification of lysine 346 as a functionally important residue for pyridoxal 5′-phosphate binding and catalysis in lysine 2,3-aminomutase from Bacillus subtilis
    • DOI 10.1021/bi002265w
    • Chen, D.; Frey, P. A. Identification of lysine 346 as a functionally important residue for pyridoxal 5′-phosphate binding and catalysis in lysine 2,3-aminomutase from Bacillus subtilis Biochemistry 2001, 40, 596-602 (Pubitemid 32063239)
    • (2001) Biochemistry , vol.40 , Issue.2 , pp. 596-602
    • Chen, D.1    Frey, P.A.2
  • 23
    • 0000112024 scopus 로고
    • Stereochemistry of lysine 2,3-aminomutase isolated from Clostridium subterminale strain SB4
    • Aberhart, D. J.; Gould, S. J.; Lin, H. J.; Thiruvengadam, T. K.; Weiller, B. Stereochemistry of lysine 2,3-aminomutase isolated from Clostridium subterminale strain SB4 J. Am. Chem. Soc. 1983, 105, 5461-5470
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 5461-5470
    • Aberhart, D.J.1    Gould, S.J.2    Lin, H.J.3    Thiruvengadam, T.K.4    Weiller, B.5
  • 24
    • 0017115986 scopus 로고
    • A Novel reaction of S -adenosyl-L-methionine correlated with the activation of pyruvate-formate lyase
    • Knappe, J.; Schmit, T. A Novel reaction of S -adenosyl-L-methionine correlated with the activation of pyruvate-formate lyase Biochem. Biophys. Res. Commun. 1976, 71, 1110-1117
    • (1976) Biochem. Biophys. Res. Commun. , vol.71 , pp. 1110-1117
    • Knappe, J.1    Schmit, T.2
  • 25
    • 0021296422 scopus 로고
    • Pyruvate formate-lyase (inactive form) and pyruvate formate-lyase activating enzyme of Escherichia coli: Isolation and structural properties
    • Conradt, H.; Hohmann-Berger, M.; Hohmann, H. P.; Blaschkowski, H. P.; Knappe, J. Pyruvate formate-lyase (inactive form) and pyruvate formate-lyase activating enzyme of Escherichia coli: isolation and structural properties Arch. Biochem. Biophys. 1984, 228, 133-142
    • (1984) Arch. Biochem. Biophys. , vol.228 , pp. 133-142
    • Conradt, H.1    Hohmann-Berger, M.2    Hohmann, H.P.3    Blaschkowski, H.P.4    Knappe, J.5
  • 28
    • 0026483949 scopus 로고
    • Characterization of iron-sulfur clusters in lysine 2,3-aminomutase by electron paramagnetic resonance spectroscopy
    • Petrovich, R. M.; Ruzicka, F. J.; Reed, G. H.; Frey, P. A. Characterization of iron-sulfur clusters in lysine 2,3-aminomutase by electron paramagnetic resonance spectroscopy Biochemistry 1992, 31, 10774-10781
    • (1992) Biochemistry , vol.31 , pp. 10774-10781
    • Petrovich, R.M.1    Ruzicka, F.J.2    Reed, G.H.3    Frey, P.A.4
  • 29
    • 0032562217 scopus 로고    scopus 로고
    • S-adenosylmethionine-dependent reduction of lysine 2,3-aminomutase and observation of the catalytically functional iron-sulfur centers by electron paramagnetic resonance
    • DOI 10.1021/bi972417w
    • Lieder, K. W.; Booker, S.; Ruzicka, F. J.; Beinert, H.; Reed, G. H.; Frey, P. A. S -Adenosylmethionine-dependent reduction of lysine 2,3-aminomutase and observation of the catalytically functional iron-sulfur centers by electron paramagnetic resonance Biochemistry 1998, 37, 2578-2585 (Pubitemid 28119335)
    • (1998) Biochemistry , vol.37 , Issue.8 , pp. 2578-2585
    • Lieder, K.W.1    Booker, S.2    Ruzicka, F.J.3    Beinert, H.4    Reed, G.H.5    Frey, P.A.6
  • 30
    • 0026606405 scopus 로고
    • An organic radical in the lysine 2,3-aminomutase reaction
    • Ballinger, M. D.; Reed, G. H.; Frey, P. A. An organic radical in the lysine 2,3-aminomutase reaction Biochemistry 1992, 31, 949-953
    • (1992) Biochemistry , vol.31 , pp. 949-953
    • Ballinger, M.D.1    Reed, G.H.2    Frey, P.A.3
  • 31
    • 0026444094 scopus 로고
    • Structure of a substrate radical intermediate in the reaction of lysine 2,3-aminomutase
    • Ballinger, M. D.; Frey, P. A.; Reed, G. H. Structure of a substrate radical intermediate in the reaction of lysine 2,3-aminomutase Biochemistry 1992, 31, 10782-10789
    • (1992) Biochemistry , vol.31 , pp. 10782-10789
    • Ballinger, M.D.1    Frey, P.A.2    Reed, G.H.3
  • 32
    • 0029736685 scopus 로고    scopus 로고
    • Lysine 2,3-aminomutase: Rapid mix-freeze-quench electron paramagnetic resonance studies establishing the kinetic competence of a substrate-based radical intermediate
    • DOI 10.1021/bi960850k
    • Chang, C. H.; Ballinger, M. D.; Reed, G. H.; Frey, P. A. Lysine 2,3-aminomutase: Rapid mix-freeze-quench electron paramagnetic resonance studies establishing the kinetic competence of a substrate-based radical intermediate Biochemistry 1996, 35, 11081-11084 (Pubitemid 26298741)
    • (1996) Biochemistry , vol.35 , Issue.34 , pp. 11081-11084
    • Chang, C.H.1    Ballinger, M.D.2    Reed, G.H.3    Frey, P.A.4
  • 33
    • 0029089648 scopus 로고
    • Observation of a second substrate radical intermediate in the reaction of lysine 2,3-aminomutase: A radical centered on the β-carbon of the alternative substrate, 4-Thia-L-lysine
    • Wu, W.; Lieder, K. W.; Reed, G. H.; Frey, P. A. Observation of a second substrate radical intermediate in the reaction of lysine 2,3-aminomutase: A radical centered on the β-carbon of the alternative substrate, 4-Thia-L-lysine Biochemistry 1995, 34, 10532-10537
    • (1995) Biochemistry , vol.34 , pp. 10532-10537
    • Wu, W.1    Lieder, K.W.2    Reed, G.H.3    Frey, P.A.4
  • 34
    • 0034622523 scopus 로고    scopus 로고
    • Lysine 2,3-aminomutase and trans-4,5-dehydrolysine: Characterization of an allylic analogue of a substrate-based radical in the catalytic mechanism
    • DOI 10.1021/bi000658p
    • Wu, W.; Booker, S.; Lieder, K. W.; Bandarian, V.; Reed, G. H.; Frey, P. A. Lysine 2,3-aminomutase and trans -4,5-dehydrolysine: Characterization of an allylic analogue of a substrate-based radical in the catalytic mechanism Biochemistry 2000, 39, 9561-9570 (Pubitemid 30626346)
    • (2000) Biochemistry , vol.39 , Issue.31 , pp. 9561-9570
    • Wu, W.1    Booker, S.2    Lieder, K.W.3    Bandarian, V.4    Reed, G.H.5    Frey, P.A.6
  • 35
    • 0035800077 scopus 로고    scopus 로고
    • Characterization of an allylic analogue of the 5′-deoxyadenosyl radical: An intermediate in the reaction of lysine 2,3-aminomutase
    • DOI 10.1021/bi0104569
    • Magnusson, O. T.; Reed, G. H.; Frey, P. A. Characterization of an allylic analogue of the 5′-deoxyadenosyl radical: An intermediate in the reaction of lysine 2,3-aminomutase Biochemistry 2001, 40, 7773-7782 (Pubitemid 32622967)
    • (2001) Biochemistry , vol.40 , Issue.26 , pp. 7773-7782
    • Magnusson, O.Th.1    Reed, G.H.2    Frey, P.A.3
  • 36
    • 0034719099 scopus 로고    scopus 로고
    • Direct FeS cluster involvement in generation of a radical in lysine 2,3-aminomutase
    • DOI 10.1021/bi0022184
    • Cosper, N. J.; Booker, S. J.; Ruzicka, F.; Frey, P. A.; Scott, R. A. Direct FeS cluster involvement in generation of a radical in lysine 2,3-aminomutase Biochemistry 2000, 39, 15668-15673 (Pubitemid 32038228)
    • (2000) Biochemistry , vol.39 , Issue.51 , pp. 15668-15673
    • Cosper, N.J.1    Booker, S.J.2    Ruzicka, F.3    Frey, P.A.4    Scott, R.A.5
  • 40
    • 0141620318 scopus 로고    scopus 로고
    • Coordination and mechanism of reversible cleavage of S-adenosylmethionine by the [4Fe-4S] center in lysine 2,3-aminomutase
    • DOI 10.1021/ja036120z
    • Chen, D.; Walsby, C.; Hoffman, B. M.; Frey, P. A. Coordination and mechanism of reversible cleavage of S -adenosylmethionine by the [4Fe-4S] center in lysine 2,3-aminomutase J. Am. Chem. Soc. 2003, 125, 11788-11789 (Pubitemid 37175392)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.39 , pp. 11788-11789
    • Chen, D.1    Walsby, C.2    Hoffman, B.M.3    Frey, P.A.4
  • 42
    • 78650493707 scopus 로고    scopus 로고
    • Regioselectivity in the homolytic cleavage of S -adenosylmethionine
    • Kampmeier, J. A. Regioselectivity in the homolytic cleavage of S -adenosylmethionine Biochemistry 2010, 49, 10770-10772
    • (2010) Biochemistry , vol.49 , pp. 10770-10772
    • Kampmeier, J.A.1
  • 43
    • 0017061044 scopus 로고
    • Nucleic acid related compounds. 23. Transformation of ribonucleoside 2',3' O ortho esters into unsaturated and deoxy sugar nucleosides via enol ester substituted iodo intermediates
    • DOI 10.1021/ja00441a054
    • Robins, M. J.; Jones, R. A.; Mengel, A. Nucleic acid related compounds. 23. Transformation of ribonucleoside 2′,3′-O-ortho esters into unsaturated and deoxy sugar nucleosides via enol ester-substituted iodo intermediates J. Am. Chem. Soc. 1976, 98, 8213-8217 (Pubitemid 8014645)
    • (1976) Journal of the American Chemical Society , vol.98 , Issue.25 , pp. 8213-8217
    • Robins, M.J.1    Jones, R.A.2    Mengel, R.3
  • 44
    • 33845267636 scopus 로고    scopus 로고
    • Analysis of the cob(II)alamin-5′-deoxy-3′,4′- anhydroadenosyl radical triplet spin system in the active site of diol dehydrase
    • Mansoorabadi, S. O.; Magnusson, O.Th.; Poyner, R.; Frey, P. A.; Reed, G. H. Analysis of the cob(II)alamin-5′-deoxy-3′,4′- anhydroadenosyl radical triplet spin system in the active site of diol dehydrase Biochemistry 2006, 45, 4362-4370
    • (2006) Biochemistry , vol.45 , pp. 4362-4370
    • Mansoorabadi, S.O.1    Magnusson, O.Th.2    Poyner, R.3    Frey, P.A.4    Reed, G.H.5
  • 45
    • 0037461322 scopus 로고    scopus 로고
    • 2H]adenosylcobalamin by ribonucleoside triphosphate reductase: Cysteine 408-independent cleavage of the Co-C5′ bond
    • DOI 10.1021/bi030018x
    • 2H] adenosylcobalamin by ribonucleoside triphosphate reductase: Cysteine 408-independent cleavage of the Co-C5′ bond Biochemistry 2003, 42, 4578-4584 (Pubitemid 36457627)
    • (2003) Biochemistry , vol.42 , Issue.15 , pp. 4578-4584
    • Chen, D.1    Abend, A.2    Stubbe, J.3    Frey, P.A.4
  • 47
    • 33644860151 scopus 로고    scopus 로고
    • 2+/1+ in lysine 2,3-aminomutase
    • DOI 10.1021/bi0519497
    • 2+/1+ in lysine 2,3-aminomutase Biochemistry 2006, 45, 3219-3225 (Pubitemid 43376340)
    • (2006) Biochemistry , vol.45 , Issue.10 , pp. 3219-3225
    • Hinckley, G.T.1    Frey, P.A.2
  • 48
    • 36048929198 scopus 로고    scopus 로고
    • Binding energy in the one-electron reductive cleavage of S-adenosylmethionine in lysine 2,3-aminomutase, a radical SAM enzyme
    • DOI 10.1021/bi701745h
    • Wang, S. C.; Frey, P. A. Binding energy in the one-electron reductive cleavage of S -adenosylmethionine in lysine 2,3-aminomutase, a radical SAM enzyme Biochemistry 2007, 46, 12889-12895 (Pubitemid 350086212)
    • (2007) Biochemistry , vol.46 , Issue.45 , pp. 12889-12895
    • Wang, S.C.1    Frey, P.A.2
  • 49
    • 0034642248 scopus 로고    scopus 로고
    • Escherichia coli LipA is a lipoyl synthase: In vitro biosynthesis of lipoylated pyruvate dehydrogenas complex from octanoyl-acyl carrier protein
    • Miller, J. R.; Busby, R. W.; Jordan, S. W.; Cheek, J.; Henshaw, T. F.; Ashley, G. W.; Broderick, J. B.; Cronan, J. E., Jr.; Marletta, M. A. Escherichia coli LipA is a lipoyl synthase: In vitro biosynthesis of lipoylated pyruvate dehydrogenas complex from octanoyl-acyl carrier protein Biochemistry 2000, 39, 15166-15178
    • (2000) Biochemistry , vol.39 , pp. 15166-15178
    • Miller, J.R.1    Busby, R.W.2    Jordan, S.W.3    Cheek, J.4    Henshaw, T.F.5    Ashley, G.W.6    Broderick, J.B.7    Cronan, Jr.J.E.8    Marletta, M.A.9
  • 52
    • 0033988966 scopus 로고    scopus 로고
    • Lysine 2,3-aminomutase from Clostridium subterminale SB4: Mass spectral characterization of cyanogen bromide-treated peptides and cloning, sequencing, and expression of the gene kamA in Escherichia coli
    • DOI 10.1128/JB.182.2.469-476.2000
    • Ruzicka, F. J.; Lieder, K. W.; Frey, P. A. Lysine 2,3-aminomutase from Clostridium subterminale SB4: Mass spectral characterization of cyanogen bromide-treated peptides and cloning, sequencing, and expression of the gene kamA in Escherichia coli J. Bacteriol. 2000, 182, 469-476 (Pubitemid 30030133)
    • (2000) Journal of Bacteriology , vol.182 , Issue.2 , pp. 469-476
    • Ruzicka, F.J.1    Lieder, K.W.2    Frey, P.A.3
  • 53
    • 0035282866 scopus 로고    scopus 로고
    • Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: Functional characterization using new analysis and information visualization methods
    • Sofia, H. J.; Chen, G.; Hetzler, B. G.; Reyes-Spindola, J. F.; Miller, N. E. Radical SAM. A novel rotein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods Nuleic Acids Res. 2001, 29, 1097-1106 (Pubitemid 32186195)
    • (2001) Nucleic Acids Research , vol.29 , Issue.5 , pp. 1097-1106
    • Sofia, H.J.1    Chen, G.2    Hetzler, B.G.3    Reyes-Spindola, J.F.4    Miller, N.E.5
  • 54
    • 84866749191 scopus 로고    scopus 로고
    • Radical SAM-dependent carbon insertion into the nitrogenase M-cluster
    • Wiig, J. A.; Hu, Y.; Lee, C. C.; Ribbe, M. W. Radical SAM-dependent carbon insertion into the nitrogenase M-cluster Science 2012, 337, 1672-1675
    • (2012) Science , vol.337 , pp. 1672-1675
    • Wiig, J.A.1    Hu, Y.2    Lee, C.C.3    Ribbe, M.W.4
  • 55
    • 84877584386 scopus 로고    scopus 로고
    • The catalytic mechanism for anaerobic formation of methane by bacteria
    • Kamat, S. S.; Williams, H. J.; Dangott, L. J.; Chakrabarti, M.; Raushel, F. M. The catalytic mechanism for anaerobic formation of methane by bacteria Nature 2013, 497, 132-136
    • (2013) Nature , vol.497 , pp. 132-136
    • Kamat, S.S.1    Williams, H.J.2    Dangott, L.J.3    Chakrabarti, M.4    Raushel, F.M.5
  • 56
  • 58
    • 65249142024 scopus 로고    scopus 로고
    • Anaerobic functionalization of unactivated C-H bonds
    • Booker, S. J. Anaerobic functionalization of unactivated C-H bonds Curr. Opin. Chem. Biol. 2009, 13, 58-73
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 58-73
    • Booker, S.J.1
  • 59
    • 79953302584 scopus 로고    scopus 로고
    • Radicals from S -adenosylmethionine and their application to biosynthesis. Booker, S. J. Anaerobic functionalization of unactivated C-H bonds
    • Roach, P. L. Radicals from S -adenosylmethionine and their application to biosynthesis. Booker, S. J. Anaerobic functionalization of unactivated C-H bonds Curr. Opin. Chem. Biol. 2011, 15, 267-275
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 267-275
    • Roach, P.L.1
  • 60
    • 84859891708 scopus 로고    scopus 로고
    • Radical-mediated enzymatic methylation: A tale of two SAMS
    • Zhang, Q.; van der Donk, W. A.; Liu, W. Radical-mediated enzymatic methylation: a tale of two SAMS Acc. Chem. Res. 2012, 45, 555-564
    • (2012) Acc. Chem. Res. , vol.45 , pp. 555-564
    • Zhang, Q.1    Van Der Donk, W.A.2    Liu, W.3
  • 62
    • 84881231182 scopus 로고    scopus 로고
    • Radical SAM-mediated methylation reactions
    • Fujimori, D. G. Radical SAM-mediated methylation reactions Curr. Opin. Chem. Biol. 2013, 17, 597-604
    • (2013) Curr. Opin. Chem. Biol. , vol.17 , pp. 597-604
    • Fujimori, D.G.1


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