메뉴 건너뛰기




Volumn 52, Issue 1, 2013, Pages 188-198

Spectroscopic, steady-state kinetic, and mechanistic characterization of the radical SAM enzyme QueE, which catalyzes a complex cyclization reaction in the biosynthesis of 7-deazapurines

Author keywords

[No Author keywords available]

Indexed keywords

BACILLUS SUBTILIS; BIOSYNTHETIC PATHWAY; CATALYTIC CYCLES; COFACTORS; CYCLIZATION REACTIONS; DIVALENT METAL ION; ENZYMATIC TRANSFORMATION; HYDROGEN ATOM ABSTRACTION; MOSSBAUER; REACTION CATALYZED; REDUCTIVE CLEAVAGE; RING CONTRACTION; S ADENOSYL L METHIONINES; SPECTROSCOPIC FEATURES; STEADY-STATE KINETICS; SYNTHASES;

EID: 84872108164     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi301156w     Document Type: Article
Times cited : (52)

References (62)
  • 1
  • 2
    • 84864396740 scopus 로고    scopus 로고
    • Biosynthesis of pyrrolopyrimidines
    • McCarty, R. M. and Bandarian, V. (2012) Biosynthesis of pyrrolopyrimidines Bioorg. Chem. 43, 15-25
    • (2012) Bioorg. Chem. , vol.43 , pp. 15-25
    • McCarty, R.M.1    Bandarian, V.2
  • 3
    • 0016804870 scopus 로고
    • Structure of the modified nucleoside Q isolated from Escherichia coli transfer ribonucleic acid. 7-(4,5- cis -dihydroxy-1-cyclopenten-3-ylaminomethyl) -7-deazaguanosine
    • Kasai, H., Oashi, Z., Harada, F., Nishimura, S., Oppenheimer, N., Crain, P., Liehr, J., Minden, D., and McCloskey, J. (1975) Structure of the modified nucleoside Q isolated from Escherichia coli transfer ribonucleic acid. 7-(4,5- cis -dihydroxy-1-cyclopenten-3-ylaminomethyl)-7-deazaguanosine Biochemistry 14, 4198-4208
    • (1975) Biochemistry , vol.14 , pp. 4198-4208
    • Kasai, H.1    Oashi, Z.2    Harada, F.3    Nishimura, S.4    Oppenheimer, N.5    Crain, P.6    Liehr, J.7    Minden, D.8    McCloskey, J.9
  • 4
    • 0027191379 scopus 로고
    • Structure of the archaeal transfer RNA nucleoside G*-15 (2-amino-4,7-dihydro-4-oxo-7-β- d -ribofuranosyl-1 H -pyrrolo[2,3- d ]pyrimidine-5-carboximidamide (archaeosine))
    • Gregson, J. M., Crain, P. F., Edmonds, C. G., Gupta, R., Hashizume, T., Phillipson, D. W., and McCloskey, J. A. (1993) Structure of the archaeal transfer RNA nucleoside G*-15 (2-amino-4,7-dihydro-4-oxo-7-β- d -ribofuranosyl-1 H -pyrrolo[2,3- d ]pyrimidine-5-carboximidamide (archaeosine)) J. Biol. Chem. 268, 10076-10086
    • (1993) J. Biol. Chem. , vol.268 , pp. 10076-10086
    • Gregson, J.M.1    Crain, P.F.2    Edmonds, C.G.3    Gupta, R.4    Hashizume, T.5    Phillipson, D.W.6    McCloskey, J.A.7
  • 5
    • 0015514384 scopus 로고
    • Asp from Escherichia coli B. Universal presence of nucleoside Q in the first postion of the anticondons of these transfer ribonucleic acids
    • Asp from Escherichia coli B. Universal presence of nucleoside Q in the first postion of the anticondons of these transfer ribonucleic acids Biochemistry 11, 301-308
    • (1972) Biochemistry , vol.11 , pp. 301-308
    • Harada, F.1    Nishimura, S.2
  • 7
    • 0015924554 scopus 로고
    • Activity of a transfer RNA modifying enzyme during the development of Drosophila and its relationship to the su(s) locus
    • White, B. N. and Tener, G. M. (1973) Activity of a transfer RNA modifying enzyme during the development of Drosophila and its relationship to the su(s) locus J. Mol. Biol. 74, 635-651
    • (1973) J. Mol. Biol. , vol.74 , pp. 635-651
    • White, B.N.1    Tener, G.M.2
  • 8
    • 0019332704 scopus 로고
    • Effect of diet on the queuosine family of tRNAs of germ-free mice
    • Farkas, W. R. (1980) Effect of diet on the queuosine family of tRNAs of germ-free mice J. Biol. Chem. 255, 6832-6835
    • (1980) J. Biol. Chem. , vol.255 , pp. 6832-6835
    • Farkas, W.R.1
  • 9
    • 0019330581 scopus 로고
    • Transfer ribonucleic acid guanine transglycosylase isolated from rat liver
    • Shindo-Okada, N., Okada, N., Ohgi, T., Goto, T., and Nishimura, S. (1980) Transfer ribonucleic acid guanine transglycosylase isolated from rat liver Biochemistry 19, 395-400
    • (1980) Biochemistry , vol.19 , pp. 395-400
    • Shindo-Okada, N.1    Okada, N.2    Ohgi, T.3    Goto, T.4    Nishimura, S.5
  • 10
    • 0020037023 scopus 로고
    • Queuine, a modified base incorporated posttranscriptionally into eukaryotic transfer RNA: Wide distribution in nature
    • Katze, J. R., Basile, B., and McCloskey, J. A. (1982) Queuine, a modified base incorporated posttranscriptionally into eukaryotic transfer RNA: Wide distribution in nature Science 216, 55-56
    • (1982) Science , vol.216 , pp. 55-56
    • Katze, J.R.1    Basile, B.2    McCloskey, J.A.3
  • 11
    • 49449106283 scopus 로고    scopus 로고
    • Deciphering deazapurine biosynthesis: Pathway for pyrrolopyrimidine nucleosides toyocamycin and sangivamycin
    • McCarty, R. M. and Bandarian, V. (2008) Deciphering deazapurine biosynthesis: Pathway for pyrrolopyrimidine nucleosides toyocamycin and sangivamycin Chem. Biol. 15, 790-798
    • (2008) Chem. Biol. , vol.15 , pp. 790-798
    • McCarty, R.M.1    Bandarian, V.2
  • 12
  • 13
    • 64849084260 scopus 로고    scopus 로고
    • Escherichia coli QueD is a 6-carboxy-5,6,7,8-tetrahydropterin synthase
    • McCarty, R. M., Somogyi, A., and Bandarian, V. (2009) Escherichia coli QueD is a 6-carboxy-5,6,7,8-tetrahydropterin synthase Biochemistry 48, 2301-2303
    • (2009) Biochemistry , vol.48 , pp. 2301-2303
    • McCarty, R.M.1    Somogyi, A.2    Bandarian, V.3
  • 14
    • 66149108786 scopus 로고    scopus 로고
    • The deazapurine biosynthetic pathway revealed: In vitro enzymatic synthesis of preQ0 from guanosine 5′-triphosphate in four steps
    • McCarty, R. M., Somogyi, A., Lin, G., Jacobsen, N. E., and Bandarian, V. (2009) The deazapurine biosynthetic pathway revealed: In vitro enzymatic synthesis of preQ0 from guanosine 5′-triphosphate in four steps Biochemistry 48, 3847-3852
    • (2009) Biochemistry , vol.48 , pp. 3847-3852
    • McCarty, R.M.1    Somogyi, A.2    Lin, G.3    Jacobsen, N.E.4    Bandarian, V.5
  • 15
    • 0014409033 scopus 로고
    • The biosynthesis of folic acid. 8. Purification and properties of the enzyme that catalyzes the production of formate from carbon atom 8 of guanosine triphosphate
    • Burg, A. and Brown, G. (1968) The biosynthesis of folic acid. 8. Purification and properties of the enzyme that catalyzes the production of formate from carbon atom 8 of guanosine triphosphate J. Biol. Chem. 243, 2349-2358
    • (1968) J. Biol. Chem. , vol.243 , pp. 2349-2358
    • Burg, A.1    Brown, G.2
  • 16
    • 0016665419 scopus 로고
    • Biosynthesis of biopterin by two clones of mouse neuroblastoma
    • Buff, K. and Dairman, W. (1975) Biosynthesis of biopterin by two clones of mouse neuroblastoma Mol. Pharmacol. 11, 87-93
    • (1975) Mol. Pharmacol. , vol.11 , pp. 87-93
    • Buff, K.1    Dairman, W.2
  • 17
    • 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., Chen, G., Hetzler, B., Reyes-Spindola, J., and Miller, N. (2001) 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 Nucleic Acids Res. 29, 1097-1106
    • (2001) Nucleic Acids Res. , vol.29 , pp. 1097-1106
    • Sofia, H.1    Chen, G.2    Hetzler, B.3    Reyes-Spindola, J.4    Miller, N.5
  • 19
    • 73649096195 scopus 로고    scopus 로고
    • Identification and characterization of a novel member of the radical AdoMet enzyme superfamily and implications for the biosynthesis of the Hmd hydrogenase active site cofactor
    • McGlynn, S. E., Boyd, E. S., Shepard, E. M., Lange, R. K., Gerlach, R., Broderick, J. B., and Peters, J. W. (2010) Identification and characterization of a novel member of the radical AdoMet enzyme superfamily and implications for the biosynthesis of the Hmd hydrogenase active site cofactor J. Bacteriol. 192, 595-598
    • (2010) J. Bacteriol. , vol.192 , pp. 595-598
    • McGlynn, S.E.1    Boyd, E.S.2    Shepard, E.M.3    Lange, R.K.4    Gerlach, R.5    Broderick, J.B.6    Peters, J.W.7
  • 21
    • 13844275460 scopus 로고    scopus 로고
    • Spectroscopic Approaches to Elucidating Novel Iron-Sulfur Chemistry in the "radical-SAM" Protein Superfamily
    • Walsby, C. J., Ortillo, D., Yang, J., Nnyepi, M. R., Broderick, W. E., Hoffman, B. M., and Broderick, J. B. (2005) Spectroscopic Approaches to Elucidating Novel Iron-Sulfur Chemistry in the "Radical-SAM" Protein Superfamily Inorg. Chem. 44, 727-741
    • (2005) Inorg. Chem. , vol.44 , pp. 727-741
    • Walsby, C.J.1    Ortillo, D.2    Yang, J.3    Nnyepi, M.R.4    Broderick, W.E.5    Hoffman, B.M.6    Broderick, J.B.7
  • 22
    • 0037174377 scopus 로고    scopus 로고
    • An Anchoring Role for FeS Clusters: Chelation of the Amino Acid Moiety of S -Adenosylmethionine to the Unique Iron Site of the [4Fe-4S] Cluster of Pyruvate Formate-Lyase Activating Enzyme
    • Walsby, C. J., Ortillo, D., Broderick, W. E., Broderick, J. B., and Hoffman, B. M. (2002) An Anchoring Role for FeS Clusters: Chelation of the Amino Acid Moiety of S -Adenosylmethionine to the Unique Iron Site of the [4Fe-4S] Cluster of Pyruvate Formate-Lyase Activating Enzyme J. Am. Chem. Soc. 124, 11270-11271
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 11270-11271
    • Walsby, C.J.1    Ortillo, D.2    Broderick, W.E.3    Broderick, J.B.4    Hoffman, B.M.5
  • 23
    • 0024496311 scopus 로고
    • Lysine 2,3-aminomutase. Support for a mechanism of hydrogen transfer involving S-adenosylmethionine
    • Baraniak, J., Moss, M. L., and Frey, P. A. (1989) Lysine 2,3-aminomutase. Support for a mechanism of hydrogen transfer involving S-adenosylmethionine J. Biol. Chem. 264, 1357-1360
    • (1989) J. Biol. Chem. , vol.264 , pp. 1357-1360
    • Baraniak, J.1    Moss, M.L.2    Frey, P.A.3
  • 24
    • 0037181382 scopus 로고    scopus 로고
    • Direct H atom abstraction from spore photoproduct C-6 initiates DNA repair in the reaction catalyzed by spore photoproduct lyase: Evidence for a reversibly generated adenosyl radical intermediate
    • Cheek, J. and Broderick, J. B. (2002) Direct H atom abstraction from spore photoproduct C-6 initiates DNA repair in the reaction catalyzed by spore photoproduct lyase: Evidence for a reversibly generated adenosyl radical intermediate J. Am. Chem. Soc. 124, 2860-2861
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 2860-2861
    • Cheek, J.1    Broderick, J.B.2
  • 25
    • 0034792676 scopus 로고    scopus 로고
    • Radical mechanisms of S-adenosylmethionine-dependent enzymes
    • Frey, P. A. and Booker, S. J. (2001) Radical mechanisms of S-adenosylmethionine-dependent enzymes Adv. Protein Chem. 58, 1-45
    • (2001) Adv. Protein Chem. , vol.58 , pp. 1-45
    • Frey, P.A.1    Booker, S.J.2
  • 26
    • 35348854977 scopus 로고    scopus 로고
    • Self-sacrifice in radical S-adenosylmethionine proteins
    • Booker, S. J., Cicchillo, R. M., and Grove, T. L. (2007) Self-sacrifice in radical S-adenosylmethionine proteins Curr. Opin. Chem. Biol. 11, 543-552
    • (2007) Curr. Opin. Chem. Biol. , vol.11 , pp. 543-552
    • Booker, S.J.1    Cicchillo, R.M.2    Grove, T.L.3
  • 28
    • 65249142024 scopus 로고    scopus 로고
    • Anaerobic functionalization of unactivated C-H bonds
    • Booker, S. J. (2009) Anaerobic functionalization of unactivated C-H bonds Curr. Opin. Chem. Biol. 13, 58-73
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 58-73
    • Booker, S.J.1
  • 29
    • 0037397764 scopus 로고    scopus 로고
    • Formation of iron-sulfur clusters in bacteria: An emerging field in bioinorganic chemistry
    • Frazzon, J. and Dean, D. R. (2003) Formation of iron-sulfur clusters in bacteria: An emerging field in bioinorganic chemistry Curr. Opin. Chem. Biol. 7, 166-173
    • (2003) Curr. Opin. Chem. Biol. , vol.7 , pp. 166-173
    • Frazzon, J.1    Dean, D.R.2
  • 30
    • 0036670725 scopus 로고    scopus 로고
    • Biosynthesis of iron-sulphur clusters is a complex and highly conserved process
    • Frazzon, J., Fick, J. R., and Dean, D. R. (2001) Biosynthesis of iron-sulphur clusters is a complex and highly conserved process Biochem. Soc. Trans. 30, 680-685
    • (2001) Biochem. Soc. Trans. , vol.30 , pp. 680-685
    • Frazzon, J.1    Fick, J.R.2    Dean, D.R.3
  • 31
    • 0001778171 scopus 로고
    • Use of chloramphenicol to study control of RNA synthesis in bacteria
    • Fraenkel, D. G. and Neidhardt, F. C. (1961) Use of chloramphenicol to study control of RNA synthesis in bacteria Biochim. Biophys. Acta 53, 96-110
    • (1961) Biochim. Biophys. Acta , vol.53 , pp. 96-110
    • Fraenkel, D.G.1    Neidhardt, F.C.2
  • 32
    • 0002556548 scopus 로고
    • Chemistry of naturally occurring pterins
    • In (Blakley, R. L. and Benkovic, S. J. Eds.) pp. John Wiley & Sons, Inc. New York.
    • Pfleiderer, W. (1985) Chemistry of naturally occurring pterins. In Folates and pterins (Blakley, R. L. and Benkovic, S. J., Eds.) pp 44-114. John Wiley & Sons, Inc., New York.
    • (1985) Folates and Pterins , pp. 44-114
    • Pfleiderer, W.1
  • 33
  • 34
    • 0016173119 scopus 로고
    • Activation of methionine synthetase by a reduced triphosphopyridine nucleotide-dependent flavoprotein system
    • Fujii, K. and Huennekens, F. M. (1974) Activation of methionine synthetase by a reduced triphosphopyridine nucleotide-dependent flavoprotein system J. Biol. Chem. 249, 6745-6753
    • (1974) J. Biol. Chem. , vol.249 , pp. 6745-6753
    • Fujii, K.1    Huennekens, F.M.2
  • 36
    • 0021718029 scopus 로고
    • The sequence of metK, the structural gene for S -adenosylmethionine synthetase in Escherichia coli
    • Markham, G., DeParasis, J., and Gatmaitan, J. (1984) The sequence of metK, the structural gene for S -adenosylmethionine synthetase in Escherichia coli J. Biol. Chem. 259, 14505-14507
    • (1984) J. Biol. Chem. , vol.259 , pp. 14505-14507
    • Markham, G.1    Deparasis, J.2    Gatmaitan, J.3
  • 37
    • 34447558542 scopus 로고    scopus 로고
    • The copper-inducible cin operon encodes an unusual methionine-rich azurin-like protein and a preQ0 reductase in Pseudomonas putida KT2440
    • Quaranta, D., McCarty, R., Bandarian, V., and Rensing, C. (2007) The copper-inducible cin operon encodes an unusual methionine-rich azurin-like protein and a preQ0 reductase in Pseudomonas putida KT2440 J. Bacteriol. 189, 5361-5371
    • (2007) J. Bacteriol. , vol.189 , pp. 5361-5371
    • Quaranta, D.1    McCarty, R.2    Bandarian, V.3    Rensing, C.4
  • 39
    • 0020776388 scopus 로고
    • Semi-micro methods for analysis of labile sulfide and of labile sulfide plus sulfane sulfur in unusually stable iron-sulfur proteins
    • Beinert, H. (1983) Semi-micro methods for analysis of labile sulfide and of labile sulfide plus sulfane sulfur in unusually stable iron-sulfur proteins Anal. Biochem. 131, 373-378
    • (1983) Anal. Biochem. , vol.131 , pp. 373-378
    • Beinert, H.1
  • 40
    • 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
    • Lieder, K. W., Booker, S. J., Ruzicka, F. J., Beinert, H., Reed, G. H., and Frey, P. A. (1998) S -Adenosylmethionine-dependent reduction of lysine 2,3-aminomutase and observation of the catalytically functional iron-sulfur centers by electron paramagnetic resonance Biochemistry 37, 2578-2585
    • (1998) Biochemistry , vol.37 , pp. 2578-2585
    • Lieder, K.W.1    Booker, S.J.2    Ruzicka, F.J.3    Beinert, H.4    Reed, G.H.5    Frey, P.A.6
  • 43
    • 0020064853 scopus 로고
    • Routes of flavodoxin and ferredoxin reduction in Escherichia coli CoA-acylating pyruvate: Flavodoxin and NADPH:flavodoxin oxidoreductases participating in the activation of pyruvate formate-lyase
    • Blaschkowski, H. P., Neuer, G., Ludwig-Festl, M., and Knappe, J. (1982) Routes of flavodoxin and ferredoxin reduction in Escherichia coli CoA-acylating pyruvate: Flavodoxin and NADPH:flavodoxin oxidoreductases participating in the activation of pyruvate formate-lyase Eur. J. Biochem. 123, 563-569
    • (1982) Eur. J. Biochem. , vol.123 , pp. 563-569
    • Blaschkowski, H.P.1    Neuer, G.2    Ludwig-Festl, M.3    Knappe, J.4
  • 44
    • 0029047343 scopus 로고
    • Biotin synthase from Escherichia coli, an investigation of the low molecular weight and protein components required for activity in vitro
    • Birch, O., Fuhrmann, M., and Shaw, N. (1995) Biotin synthase from Escherichia coli, an investigation of the low molecular weight and protein components required for activity in vitro J. Biol. Chem. 270, 19158-19165
    • (1995) J. Biol. Chem. , vol.270 , pp. 19158-19165
    • Birch, O.1    Fuhrmann, M.2    Shaw, N.3
  • 46
    • 47349101467 scopus 로고    scopus 로고
    • In vitro characterization of AtsB, a radical SAM formylglycine-generating enzyme that contains three [4Fe-4S] clusters
    • Grove, T. L., Lee, K.-H., St Clair, J., Krebs, C., and Booker, S. J. (2008) In vitro characterization of AtsB, a radical SAM formylglycine-generating enzyme that contains three [4Fe-4S] clusters Biochemistry 47, 7523-7538
    • (2008) Biochemistry , vol.47 , pp. 7523-7538
    • Grove, T.L.1    Lee, K.-H.2    St Clair, J.3    Krebs, C.4    Booker, S.J.5
  • 47
    • 37049024768 scopus 로고    scopus 로고
    • Characterization and Mechanistic Study of a Radical SAM Dehydrogenase in the Biosynthesis of Butirosin
    • Yokoyama, K., Numakura, M., Kudo, F., Ohmori, D., and Eguchi, T. (2007) Characterization and Mechanistic Study of a Radical SAM Dehydrogenase in the Biosynthesis of Butirosin J. Am. Chem. Soc. 129, 15147-15155
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 15147-15155
    • Yokoyama, K.1    Numakura, M.2    Kudo, F.3    Ohmori, D.4    Eguchi, T.5
  • 48
    • 0038434902 scopus 로고    scopus 로고
    • Reconstitution and characterization of the polynuclear iron-sulfur cluster in pyruvate formate-lyase-activating enzyme
    • Külzer, R., Pils, T., Kappl, R., Hüttermann, J., and Knappe, J. (1998) Reconstitution and characterization of the polynuclear iron-sulfur cluster in pyruvate formate-lyase-activating enzyme J. Biol. Chem. 273, 4897-4903
    • (1998) J. Biol. Chem. , vol.273 , pp. 4897-4903
    • Külzer, R.1    Pils, T.2    Kappl, R.3    Hüttermann, J.4    Knappe, J.5
  • 49
    • 70350113877 scopus 로고    scopus 로고
    • Characterization and mechanistic studies of DesII: A radical S -adenosyl- l -methionine enzyme involved in the biosynthesis of TDP- d -desosamine
    • Szu, P.-H., Ruszczycky, M. W., Choi, S.-H., Yan, F., and Liu, H.-W. (2009) Characterization and mechanistic studies of DesII: A radical S -adenosyl- l -methionine enzyme involved in the biosynthesis of TDP- d -desosamine J. Am. Chem. Soc. 131, 14030-14042
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 14030-14042
    • Szu, P.-H.1    Ruszczycky, M.W.2    Choi, S.-H.3    Yan, F.4    Liu, H.-W.5
  • 50
    • 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
    • Chang, C. H., Ballinger, M. D., Reed, G. H., and Frey, P. A. (1996) Lysine 2,3-aminomutase: Rapid mix-freeze-quench electron paramagnetic resonance studies establishing the kinetic competence of a substrate-based radical intermediate Biochemistry 35, 11081-11084
    • (1996) Biochemistry , vol.35 , pp. 11081-11084
    • Chang, C.H.1    Ballinger, M.D.2    Reed, G.H.3    Frey, P.A.4
  • 51
    • 80052212683 scopus 로고    scopus 로고
    • Complex Biotransformations Catalyzed by Radical S -Adenosylmethionine Enzymes
    • Zhang, Q. and Liu, W. (2011) Complex Biotransformations Catalyzed by Radical S -Adenosylmethionine Enzymes J. Biol. Chem. 286, 30245-30252
    • (2011) J. Biol. Chem. , vol.286 , pp. 30245-30252
    • Zhang, Q.1    Liu, W.2
  • 52
    • 0032561180 scopus 로고    scopus 로고
    • Biosynthesis of pteridines. NMR studies on the reaction mechanisms of GTP cyclohydrolase I, pyruvoyltetrahydropterin synthase, and sepiapterin reductase
    • Bracher, A. (1998) Biosynthesis of pteridines. NMR studies on the reaction mechanisms of GTP cyclohydrolase I, pyruvoyltetrahydropterin synthase, and sepiapterin reductase J. Biol. Chem. 273, 28132-28141
    • (1998) J. Biol. Chem. , vol.273 , pp. 28132-28141
    • Bracher, A.1
  • 53
    • 0028971611 scopus 로고
    • 6-Pyruvoyl tetrahydropterin synthase, an enzyme with a novel type of active site involving both zinc binding and an intersubunit catalytic triad motif; Site-directed mutagenesis of the proposed active center, characterization of the metal binding site and modelling of substrate binding
    • Burgisser, D., Thony, B., Redweik, U., Hess, D., Heizmann, C., Huber, R., and Nar, H. (1995) 6-Pyruvoyl tetrahydropterin synthase, an enzyme with a novel type of active site involving both zinc binding and an intersubunit catalytic triad motif; site-directed mutagenesis of the proposed active center, characterization of the metal binding site and modelling of substrate binding J. Mol. Biol. 253, 358-369
    • (1995) J. Mol. Biol. , vol.253 , pp. 358-369
    • Burgisser, D.1    Thony, B.2    Redweik, U.3    Hess, D.4    Heizmann, C.5    Huber, R.6    Nar, H.7
  • 54
    • 0014940066 scopus 로고
    • Biosynthesis of the pyrrolopyrimidine nucleoside antibiotic, toyocamycin. VII. Origin of the pyrrole carbons and the cyano carbon
    • Suhadolnik, R. J. and Uematsu, T. (1970) Biosynthesis of the pyrrolopyrimidine nucleoside antibiotic, toyocamycin. VII. Origin of the pyrrole carbons and the cyano carbon J. Biol. Chem. 245, 4365-4371
    • (1970) J. Biol. Chem. , vol.245 , pp. 4365-4371
    • Suhadolnik, R.J.1    Uematsu, T.2
  • 55
    • 70350236635 scopus 로고    scopus 로고
    • Pyrroloquinoline quinone biogenesis: Demonstration that PqqE from Klebsiella pneumoniae is a radical S -adenosyl- l -methionine enzyme
    • Wecksler, S. R., Stoll, S., Tran, H., Magnusson, O. T., Wu, S.-P., King, D., Britt, R. D., and Klinman, J. P. (2009) Pyrroloquinoline quinone biogenesis: Demonstration that PqqE from Klebsiella pneumoniae is a radical S -adenosyl- l -methionine enzyme Biochemistry 48, 10151-10161
    • (2009) Biochemistry , vol.48 , pp. 10151-10161
    • Wecksler, S.R.1    Stoll, S.2    Tran, H.3    Magnusson, O.T.4    Wu, S.-P.5    King, D.6    Britt, R.D.7    Klinman, J.P.8
  • 56
    • 0026444094 scopus 로고
    • Structure of a substrate radical intermediate in the reaction of lysine 2,3-aminomutase
    • Ballinger, M., Frey, P., and Reed, G. (1992) Structure of a substrate radical intermediate in the reaction of lysine 2,3-aminomutase Biochemistry 31, 10782-10789
    • (1992) Biochemistry , vol.31 , pp. 10782-10789
    • Ballinger, M.1    Frey, P.2    Reed, G.3
  • 57
    • 0026606405 scopus 로고
    • An organic radical in the lysine 2,3-aminomutase reaction
    • Ballinger, M., Reed, G., and Frey, P. (1992) An organic radical in the lysine 2,3-aminomutase reaction Biochemistry 31, 949-953
    • (1992) Biochemistry , vol.31 , pp. 949-953
    • Ballinger, M.1    Reed, G.2    Frey, P.3
  • 58
    • 0033551437 scopus 로고    scopus 로고
    • Effects of structure on α C-H bond enthalpies of amino acid residues: Relevance to H transfers in enzyme mechanisms and in protein oxidation
    • Rauk, A., Yu, D., Taylor, J., Shustov, G. V., Block, D. A., and Armstrong, D. A. (1999) Effects of structure on α C-H bond enthalpies of amino acid residues: Relevance to H transfers in enzyme mechanisms and in protein oxidation Biochemistry 38, 9089-9096
    • (1999) Biochemistry , vol.38 , pp. 9089-9096
    • Rauk, A.1    Yu, D.2    Taylor, J.3    Shustov, G.V.4    Block, D.A.5    Armstrong, D.A.6
  • 60
    • 0035948184 scopus 로고    scopus 로고
    • Addition of carbon-centered radicals to imines and related compounds
    • Friestad, G. K. (2001) Addition of carbon-centered radicals to imines and related compounds Tetrahedron 572, 5461-5496
    • (2001) Tetrahedron , vol.572 , pp. 5461-5496
    • Friestad, G.K.1
  • 61
    • 80054696193 scopus 로고    scopus 로고
    • Pyridoxal-5′-phosphate as the catalyst for radical isomerization in reactions of PLP-dependent aminomutases
    • Frey, P. A. and Reed, G. H. (2011) Pyridoxal-5′-phosphate as the catalyst for radical isomerization in reactions of PLP-dependent aminomutases Biochim. Biophys. Acta 1814, 1548-1557
    • (2011) Biochim. Biophys. Acta , vol.1814 , pp. 1548-1557
    • Frey, P.A.1    Reed, G.H.2
  • 62
    • 0013985062 scopus 로고
    • Base-catalyzed hydrogen-deuterium exchange in bivalent metal-EDTA chelates
    • Terrill, J. B. and Reilley, C. N. (1966) Base-catalyzed hydrogen-deuterium exchange in bivalent metal-EDTA chelates Anal. Chem. 38, 1876-1881
    • (1966) Anal. Chem. , vol.38 , pp. 1876-1881
    • Terrill, J.B.1    Reilley, C.N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.