메뉴 건너뛰기




Volumn , Issue , 2009, Pages 275-289

Folate-dependent ihymidylate-forming enzymes: Parallels between DNA and RNA metabolic enzymes and evolutionary implications

Author keywords

[No Author keywords available]

Indexed keywords


EID: 84867608052     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (6)

References (63)
  • 1
    • 0344810869 scopus 로고
    • Studies on the conversion of dcoxyuridylic acid to thymidylic acid by a soluble extract from rat thymus
    • Humphreys GK, Greenberg DM. Studies on the conversion of dcoxyuridylic acid to thymidylic acid by a soluble extract from rat thymus. Arch Biochem Biophys 1958; 78(2):275-287.
    • (1958) Arch Biochem Biophys , vol.78 , Issue.2 , pp. 275-287
    • Humphreys, G.K.1    Greenberg, D.M.2
  • 2
    • 0015210983 scopus 로고
    • Thymidylate synthetase from amethopterin-resistant lactobacillus casei
    • Dunlap RB, Harding NG, Hucnnekens FM. Thymidylate synthetase from amethopterin-resistant Lactobacillus casei. Biochemistry 1971; 10(1):88-97.
    • (1971) Biochemistry , vol.10 , Issue.1 , pp. 88-97
    • Dunlap, R.B.1    Harding, N.G.2    Hucnnekens, F.M.3
  • 3
    • 0010742202 scopus 로고
    • A new enzyme of rna synthesis: Rna methylase
    • Fleissner E, Borck E. A new enzyme of RNA synthesis: RNA methylase. Proc Natl Acad Sci USA 1962; 48:1199-1203.
    • (1962) Proc Natl Acad Sci USA , vol.48 , pp. 1199-1203
    • Fleissner, E.1    Borck, E.2
  • 4
    • 0344437760 scopus 로고
    • Studies on microbial ma. L transfer of methyl groups from methionine to soluble ma from escherichia coli
    • Svensson I, Boman HG, Eriksson KG et al Studies on microbial ma. L Transfer of methyl groups from methionine to soluble ma from Escherichia coli. J Mol Biol 1963; 7:254-271.
    • (1963) J Mol Biol , vol.7 , pp. 254-271
    • Svensson, I.1    Boman, H.G.2    Eriksson, K.G.3
  • 5
    • 0023667711 scopus 로고
    • Catalytic mechanism and inhibition of trna (Uracil-5-)methyltransferase: Evidence for covalent catalysis
    • Santi DV, Hardy LW. Catalytic mechanism and inhibition of tRNA (uracil-5-)methyltransferase: evidence for covalent catalysis. Biochemistry 1987; 26(26):8599-8606.
    • (1987) Biochemistry , vol.26 , Issue.26 , pp. 8599-8606
    • Santi, D.V.1    Hardy, L.W.2
  • 6
    • 0016688603 scopus 로고
    • Transductional mapping of gene trma responsible for the production of 5-methyluridine in transfer ribonucleic acid of escherichia coli
    • Bjork GR. Transductional mapping of gene trmA responsible for the production of 5-methyluridine in transfer ribonucleic acid of Escherichia coli. J Bactcriol 1975; 124(1):92-98.
    • (1975) J Bactcriol , vol.124 , Issue.1 , pp. 92-98
    • Bjork, G.R.1
  • 7
    • 0034130606 scopus 로고    scopus 로고
    • Identification of the trm2 gene encoding the trna(M5u54)methyltransferase of saccharomyces cercvisiae
    • Nordlund ME, Johansson JO, von Pawel-Rammingen U et al Identification of the TRM2 gene encoding the tRNA(m5U54)methyltransferase of Saccharomyces cercvisiae. RNA 2000; 6(6):844-860.
    • (2000) RNA , vol.6 , Issue.6 , pp. 844-860
    • Nordlund, M.E.1    Johansson, J.O.2    Von Pawel-Rammingen, U.3
  • 8
    • 37349022099 scopus 로고    scopus 로고
    • Acquisition of a bacterial ruma-typc trna(Uracil-54, c5)-methyltransferase by archaea through an ancient horizontal gene transfer
    • Urbonavicius J, Auxilien S, Walbott H et al Acquisition of a bacterial RumA-typc tRNA(uracil-54, C5)-methyltransferase by Archaea through an ancient horizontal gene transfer. Mol Microbiol 2008; 67(2):323-335.
    • (2008) Mol Microbiol , vol.67 , Issue.2 , pp. 323-335
    • Urbonavicius, J.1    Auxilien, S.2    Walbott, H.3
  • 9
    • 0002242695 scopus 로고
    • Direct spectrophotometric evidence for the oxidation of tetrahydrofolate during the enzymatic synthesis of thymidylate
    • Wahba AJ, Friedkin M. Direct spectrophotometric evidence for the oxidation of tetrahydrofolate during the enzymatic synthesis of thymidylate. J Biol Chem 1961; 236:PC11-12.
    • (1961) J Biol Chem , vol.236 , pp. PC11-PC12
    • Wahba, A.J.1    Friedkin, M.2
  • 10
    • 0001530879 scopus 로고
    • The enzymatic synthesis of thymidylate. I. early steps in the purification of thy-midylate synthetase of escherichia coll
    • Wahba AJ, Friedkin M. The enzymatic synthesis of thymidylate. I. Early steps in the purification of thy-midylate synthetase of Escherichia coll. J Biol Chem 1962; 237:3794-3801.
    • (1962) J Biol Chem , vol.237 , pp. 3794-3801
    • Wahba, A.J.1    Friedkin, M.2
  • 11
    • 11544254760 scopus 로고
    • The biosynthesis of methylated bases in ribonucleic acid
    • Mandel LR, Borek E. The biosynthesis of methylated bases in ribonucleic acid. Biochemistry 1963; 2:555-560.
    • (1963) Biochemistry , vol.2 , pp. 555-560
    • Mandel, L.R.1    Borek, E.2
  • 12
    • 0029036377 scopus 로고
    • The catalytic mechanism and structure of thymidylate synthase
    • Carreras CW, Santi DV. The catalytic mechanism and structure of thymidylate synthase. Annu Rev Biochcm1995; 64:721-762.
    • (1995) Annu Rev Biochcm , vol.64 , pp. 721-762
    • Carreras, C.W.1    Santi, D.V.2
  • 13
    • 0001184472 scopus 로고    scopus 로고
    • Mechanisms of rna-modifying and editing enzymes
    • Gros jean H, Benne R, eds, Washington DC: ASM Press
    • Garcia GA, Goodenough-Lashna DM. Mechanisms of RNA-modifying and editing enzymes. In: Gros jean H, Benne R, eds. Modification and Editing of RNA. Washington DC: ASM Press, 1998:135-168.
    • (1998) Modification and Editing of RNA , pp. 135-168
    • Garcia, G.A.1    Goodenough-Lashna, D.M.2
  • 14
    • 0037088598 scopus 로고    scopus 로고
    • Characterization of the 23 s ribosomal rna m5u1939 mcthyltrans-ferase from escherichia coli
    • Agarwalla S, Kealey JT, Sand DV et al Characterization of the 23 S ribosomal RNA m5U1939 mcthyltrans-ferase from Escherichia coli. J Biol Chem 2002; 277(11):8835-8840.
    • (2002) J Biol Chem , vol.277 , Issue.11 , pp. 8835-8840
    • Agarwalla, S.1    Kealey, J.T.2    Sand, D.V.3
  • 15
    • 4544271510 scopus 로고    scopus 로고
    • Redox reactions of the iron-sulfur cluster in a ribosomal rna methyltransfeiase, ruma: Optical and epr studies
    • Agarwalla S, Stroud RM, Gaffney BJ. Redox reactions of the iron-sulfur cluster in a ribosomal RNA methyltransfeiase, RumA: optical and EPR studies. J Biol Chem 2004; 279(33):34123-34129.
    • (2004) J Biol Chem , vol.279 , Issue.33 , pp. 34123-34129
    • Agarwalla, S.1    Stroud, R.M.2    Gaffney, B.J.3
  • 16
    • 0345306616 scopus 로고    scopus 로고
    • Identifying the methyltransferases for m(5)u747 and m(5) u1939 in 23s rrna using maldi mass spectrometry
    • Madsen CT, Mengel-Jotgcnsen J, Kirpekar F et al Identifying the methyltransferases for m(5)U747 and m(5) U1939 in 23S rRNA using MALDI mass spectrometry. Nucleic Acids Res 2003; 31(16):738-4746.
    • (2003) Nucleic Acids Res , vol.31 , Issue.16 , pp. 738-4746
    • Madsen, C.T.1    Mengel-Jotgcnsen, J.2    Kirpekar, F.3
  • 18
    • 34548740836 scopus 로고    scopus 로고
    • In vitro detection of the enzymatic activity of folate-dependent trna (Uracil-54,-c5)-mcthyltransferase: Evolutionary implications
    • Urbonavicius J, Brochier-Armanet C, Skouloubris S et al In vitro detection of the enzymatic activity of folate-dependent tRNA (Uracil-54,-C5)-mcthyltransferase: evolutionary implications. Methods Enzymol2007; 425:103-119.
    • (2007) Methods Enzymol , vol.425 , pp. 103-119
    • Urbonavicius, J.1    Brochier-Armanet, C.2    Skouloubris, S.3
  • 19
    • 0024743516 scopus 로고
    • Molecular complémentation of a genetic marker in dictyostelium using a genomic dna library
    • Dynes JL, Firtel RA. Molecular complémentation of a genetic marker in dictyostelium using a genomic DNA library. Proc Natl Acad Sci USA 1989; 86(20):7966-7970.
    • (1989) Proc Natl Acad Sci USA , vol.86 , Issue.20 , pp. 7966-7970
    • Dynes, J.L.1    Firtel, R.A.2
  • 20
    • 0037025191 scopus 로고    scopus 로고
    • An alternative flavin-dependent mechanism fot thymidylate synthesis
    • Myllykallio H, Lipowski G, Leduc D et al. An alternative flavin-dependent mechanism fot thymidylate synthesis. Science 2002; 297(5578):105-107.
    • (2002) Science , vol.297 , Issue.5578 , pp. 105-107
    • Myllykallio, H.1    Lipowski, G.2    Leduc, D.3
  • 21
    • 0037195380 scopus 로고    scopus 로고
    • Genetic evidence for a novel thymidylate synthase in the halophilic archacon halobacterium salinarum and in campylobacter jejuni fems
    • Giladi M, Bitan-Banin G, Mevarech M et al Genetic evidence for a novel thymidylate synthase in the halophilic archacon Halobacterium salinarum and in Campylobacter jejuni FEMS Microbiol Lett 2002; 216(1):105-109.
    • (2002) Microbiol Lett , vol.216 , Issue.1 , pp. 105-109
    • Giladi, M.1    Bitan-Banin, G.2    Mevarech, M.3
  • 22
    • 0016669480 scopus 로고
    • Biosynthesis of ribosylthymine in the transfer rna of streptococcus fitecalis: a folate-dependent méthylation not involving s-adenosylmethionine
    • Delk AS, Rabinowitz JC. Biosynthesis of ribosylthymine in the transfer RNA of Streptococcus fitecalis: a folate-dependent méthylation not involving S-adenosylmethionine. Proc Natl Acad Sci USA 1975; 72(2):528-530.
    • (1975) Proc Natl Acad Sci USA , vol.72 , Issue.2 , pp. 528-530
    • Delk, A.S.1    Rabinowitz, J.C.2
  • 23
    • 0017145150 scopus 로고
    • Biosynthesis of ribothymidine in the transfer rna of streptococcus faecalis and bacillus subtilis. A méthylation of rna involving 5,10-methylenetcttahydrofolate
    • Delk AS, Romeo JM, Nagle DP Jr et al Biosynthesis of ribothymidine in the transfer RNA of Streptococcus faecalis and Bacillus subtilis. A méthylation of RNA involving 5,10-methylenetcttahydrofolate. J Biol Chem 1976; 251(23):7649-7656.
    • (1976) J Biol Chem , vol.251 , Issue.23 , pp. 7649-7656
    • Delk, A.S.1    Romeo, J.M.2    Nagle, D.P.3
  • 24
    • 0016344184 scopus 로고
    • The occurrence of a transmethylation reaction not involving s-adenosylmethionine in the formation of ribothymidine in bacillus subtilis transfor-rna
    • Romeo JM, Delk AS, Rabinowitz JC. The occurrence of a transmethylation reaction not involving S-adenosylmethionine in the formation of ribothymidine in Bacillus subtilis transfor-RNA. Biochcm Biophys Res Commun 1974; 61(4):1256-1261.
    • (1974) Biochcm Biophys Res Commun , vol.61 , Issue.4 , pp. 1256-1261
    • Romeo, J.M.1    Delk, A.S.2    Rabinowitz, J.C.3
  • 25
    • 0016379127 scopus 로고
    • Initiation of protein synthesis by folate-sufficient and folate-deficient streptococcus faecalis r: Partial purification and properties of methionyl-transfer ribonucleic acid synthetase and methionyl-transfer ribonucleic acid formyltransferase
    • Samuel CE, Rabinowitz JC. Initiation of protein synthesis by folate-sufficient and folate-deficient Streptococcus faecalis R: partial purification and properties of methionyl-transfer ribonucleic acid synthetase and methionyl-transfer ribonucleic acid formyltransferase. J Bacteriol 1974; 118(1):21-31.
    • (1974) J Bacteriol , vol.118 , Issue.1 , pp. 21-31
    • Samuel, C.E.1    Rabinowitz, J.C.2
  • 26
    • 0016807479 scopus 로고
    • Inhibition of the tettahydrofolate-dependent biosynthesis of ribothymidine in trnas of b. Subtilis and m. lysodeikticus by trimethoprim
    • Arnold HH, Kersten H. Inhibition of the tettahydrofolate-dependent biosynthesis of ribothymidine in tRNAs of B. subtilis and M. lysodeikticus by trimethoprim. FEBS Lett 1975; 53(2):258-261.
    • (1975) FEBS Lett , vol.53 , Issue.2 , pp. 258-261
    • Arnold, H.H.1    Kersten, H.2
  • 27
    • 0018901584 scopus 로고
    • Methylcnctettahydrofolate-dependent biosynthesis of ribothymidine in transfer rna of streptococcus faecalis. Evidence for reduction of the 1-carbon unit by fadh2
    • Delk AS, Nagle DP Jr, Rabinowitz JC. Methylcnctettahydrofolate-dependent biosynthesis of ribothymidine in transfer RNA of Streptococcus faecalis. Evidence for reduction of the 1-carbon unit by FADH2. J Biol Chem 1980; 255(10):4387-4390.
    • (1980) J Biol Chem , vol.255 , Issue.10 , pp. 4387-4390
    • Delk, A.S.1    Nagle, D.P.2    Rabinowitz, J.C.3
  • 28
    • 22844445708 scopus 로고    scopus 로고
    • Identification of a novel gene encoding a flavin-dependent trna: M5u methyltransferase in bacteria—evolutionary implications
    • Urbonavicius J, Skouloubris S, Myllykallio H et al Identification of a novel gene encoding a flavin-dependent tRNA:m5U methyltransferase in bacteria—evolutionary implications. Nucleic Acids Res 2005; 33(13):3955-3964.
    • (2005) Nucleic Acids Res , vol.33 , Issue.13 , pp. 3955-3964
    • Urbonavicius, J.1    Skouloubris, S.2
  • 29
    • 0023121146 scopus 로고
    • Atomic structure of thymidylate synthase: target for rational drug design
    • Hardy LW, Fincr-Moorc JS, Montfort WK et al Atomic structure of thymidylate synthase: target for rational drug design. Science 1987; 235(4787):448-455.
    • (1987) Science , vol.235 , Issue.4787 , pp. 448-455
    • Hardy, L.W.1    Fincr-Moorc, J.S.2    Montfort, W.K.3
  • 30
    • 33747674260 scopus 로고    scopus 로고
    • Catalytic mechanism and structure of viral flavin-dependent thymidylate synthase thyx
    • Graziani S, Bemauer J, Skouloubris S et al Catalytic mechanism and structure of viral flavin-dependent thymidylate synthase ThyX. J Biol Chem 2006; 281(33):24048-24057.
    • (2006) J Biol Chem , vol.281 , Issue.33 , pp. 24048-24057
    • Graziani, S.1    Bemauer, J.2    Skouloubris, S.3
  • 31
    • 0036782099 scopus 로고    scopus 로고
    • Crystal structure of thyl, a thymidylate synthase complementing protein from thermotoga maritima at 2.25 a resolution
    • Kuhn P, Lesley SA, Mathews II et al Crystal structure of thyl, a thymidylate synthase complementing protein from Thermotoga maritima at 2.25 A resolution. Proteins 2002; 49(1): 142-145.
    • (2002) Proteins , vol.49 , Issue.1 , pp. 142-145
    • Kuhn, P.1    Lesley, S.A.2    Mathews, I.I.3
  • 32
    • 0142103146 scopus 로고    scopus 로고
    • Functional analysis of substrate and cofactor complex structures of a thymidylate synthase-complementing protein
    • Mathews II, Deacon AM, Canaves JM et al Functional analysis of substrate and cofactor complex structures of a thymidylate synthase-complementing protein. Structure 2003; 11(6):677-690.
    • (2003) Structure , vol.11 , Issue.6 , pp. 677-690
    • Mathews, I.I.1    Deacon, A.M.2    Canaves, J.M.3
  • 33
    • 11144235173 scopus 로고    scopus 로고
    • Functional analysis of fad-dependent thymidylate synthase thyx from paramecium bursaria chlorella virus-1
    • Graziani S, Xia Y, Gumon JR et al Functional analysis of FAD-dependent thymidylate synthase ThyX from Paramecium bursaria Chlorella virus-1. J Biol Chem 2004; 279(52):54340-54347.
    • (2004) J Biol Chem , vol.279 , Issue.52 , pp. 54340-54347
    • Graziani, S.1    Xia, Y.2    Gumon, J.R.3
  • 34
    • 0037457980 scopus 로고    scopus 로고
    • Lessons and conclusions from dissecting the mechanism of a bisubstrate enzyme: Thymidylate synthase mutagenesis, function and structure
    • Finer-Moore JS, Santi DV, Stroud RM. Lessons and conclusions from dissecting the mechanism of a bisubstrate enzyme: thymidylate synthase mutagenesis, function and structure. Biochemistry 2003; 42(2):48-256.
    • (2003) Biochemistry , vol.42 , Issue.2 , pp. 48-256
    • Finer-Moore, J.S.1    Santi, D.V.2    Stroud, R.M.3
  • 35
    • 0026611477 scopus 로고
    • Asnl77 in escherichia coli thymidylate synthase is a major determinant of pyrimidine specificity
    • Hardy LW, Nalivaika E. Asnl77 in Escherichia coli thymidylate synthase is a major determinant of pyrimidine specificity. Proc Natl Acad Sci USA 1992; 89(20):9725-9729.
    • (1992) Proc Natl Acad Sci USA , vol.89 , Issue.20 , pp. 9725-9729
    • Hardy, L.W.1    Nalivaika, E.2
  • 36
    • 0026680632 scopus 로고
    • Mutation of asparagine 229 to aspartate in thymidylatc synthase converts the enzyme to a deoxycytidylate methylase
    • Liu L, Santi DV. Mutation of asparagine 229 to aspartate in thymidylatc synthase converts the enzyme to a deoxycytidylate methylase. Biochemistry 1992; 31(22):5100-5104.
    • (1992) Biochemistry , vol.31 , Issue.22 , pp. 5100-5104
    • Liu, L.1    Santi, D.V.2
  • 37
    • 0031440846 scopus 로고    scopus 로고
    • A novel dcmp methylase by engineering thymidylatc synthase
    • AgarwaUa S, LaPorte S, Liu L et al. A novel dCMP methylase by engineering thymidylatc synthase. Biochemistry 1997; 36(50):15909-15917.
    • (1997) Biochemistry , vol.36 , Issue.50 , pp. 15909-15917
    • AgarwaUa, S.1    LaPorte, S.2    Liu, L.3
  • 38
    • 33947669870 scopus 로고    scopus 로고
    • A quantum mechanics/molecular mechanics study of the catalytic mechanism of the thymidylate synthase
    • Kanaan N, Marti S, Molincr V et al. A quantum mechanics/molecular mechanics study of the catalytic mechanism of the thymidylate synthase. Biochemistry 2007; 46(12):3704-3713.
    • (2007) Biochemistry , vol.46 , Issue.12 , pp. 3704-3713
    • Kanaan, N.1    Marti, S.2    Molincr, V.3
  • 39
    • 2442601478 scopus 로고    scopus 로고
    • Functional evidence for active site location of tetrameric thymidylatc synthase x at the interphase of three monomers
    • Leduc D, Graziani S, Lipowski G et al Functional evidence for active site location of tetrameric thymidylatc synthase X at the interphase of three monomers. Proc Natl Acad Sci USA 2004; 101(19):7252-7257.
    • (2004) Proc Natl Acad Sci USA , vol.101 , Issue.19 , pp. 7252-7257
    • Leduc, D.1    Graziani, S.2    Lipowski, G.3
  • 40
    • 40449136466 scopus 로고    scopus 로고
    • Functional analysis of the mycobacterium tuberculosis fad-dcpendent thymidylate synthase, thyx, reveals new amino acid residues contributing to an extended thyx motif
    • Ulmer JE, Boum Y, Thouvenel CD et al. Functional analysis of the Mycobacterium tuberculosis FAD-dcpendent thymidylate synthase, ThyX, reveals new amino acid residues contributing to an extended ThyX motif. J Bacteriol 2008; 190(6):2056-2064.
    • (2008) J Bacteriol , vol.190 , Issue.6 , pp. 2056-2064
    • Ulmer, J.E.1    Boum, Y.2    Thouvenel, C.D.3
  • 41
    • 12444261732 scopus 로고    scopus 로고
    • Direct observation of the participation of flavin in product formation by thyx-en-coded thymidylate synthase
    • 4L Gattis SG, Palfey BA. Direct observation of the participation of flavin in product formation by thyX-en-coded thymidylate synthase. J Am Chem Soc 2005; 127(3):832-833.
    • (2005) J am Chem Soc , vol.127 , Issue.3 , pp. 832-833
    • Gattis, S.G.1    Palfey, B.A.2
  • 42
    • 14044273636 scopus 로고    scopus 로고
    • Catalytic mechanism of chlamydia trachomatis flavin-dependent thymidylate synthase
    • GrifEn J, Roshick C, Uiffe-Lcc E et al. Catalytic mechanism of Chlamydia trachomatis flavin-dependent thymidylate synthase. J Biol Chem 2005; 280(7):5456-5467.
    • (2005) J Biol Chem , vol.280 , Issue.7 , pp. 5456-5467
    • GrifEn, J.1    Roshick, C.2    Uiffe-Lcc, E.3
  • 43
    • 34548506752 scopus 로고    scopus 로고
    • Comparative genomics of bacterial and plant folate synthesis and salvage: Predictions and validations
    • de Crecy-Lagard V, El Yacoubi B, de la Garza RD et al Comparative genomics of bacterial and plant folate synthesis and salvage: predictions and validations. BMC Genomics 2007; 8:245.
    • (2007) BMC Genomics , vol.8 , pp. 245
    • De Crecy-Lagard, V.1    El Yacoubi, B.2    De La Garza, R.D.3
  • 44
    • 36749011792 scopus 로고    scopus 로고
    • Flavin-dependent thymidylate synthase thyx activity: Implications for the folate cycle in bacteria
    • Leduc D, Escartin F, Nijhout HF et al. Flavin-dependent thymidylate synthase ThyX activity: implications for the folate cycle in bacteria. J Bacteriol 2007; 189(23):8537-8545.
    • (2007) J Bacteriol , vol.189 , Issue.23 , pp. 8537-8545
    • Leduc, D.1    Escartin, F.2    Nijhout, H.F.3
  • 45
    • 0015366448 scopus 로고
    • Mchenry cs. 5-fluoro-2’-deoxyuridylate: Covalent complex with thymidylate synthetase
    • Santi DV, McHenry CS. 5-Fluoro-2’-deoxyuridylate: covalent complex with thymidylate synthetase. Proc Natl Acad Sci USA 1972; 69(7):1855-1857.
    • (1972) Proc Natl Acad Sci USA , vol.69 , Issue.7 , pp. 1855-1857
    • Santi, D.V.1
  • 46
    • 0032168569 scopus 로고    scopus 로고
    • Catalytic triads and their relatives
    • Dodson G, Wlodawer A. Catalytic triads and their relatives. Trends Biochem Sci 1998; 23(9):347-352.
    • (1998) Trends Biochem Sci , vol.23 , Issue.9 , pp. 347-352
    • Dodson, G.1    Wlodawer, A.2
  • 47
    • 24944591878 scopus 로고    scopus 로고
    • Structure of the mycobacterium tuberculosis flavin dependent thymidylate synthase (Mtbthyx) at 2.0 a resolution
    • Sampathkumar P, Turley S, Ulmer JE et al. Structure of the Mycobacterium tuberculosis flavin dependent thymidylate synthase (MtbThyX) at 2.0 A Resolution. Journal of Molecular Biology 2005; 352(5):1091.
    • (2005) Journal of Molecular Biology , vol.352 , Issue.5 , pp. 1091
    • Sampathkumar, P.1    Turley, S.2    Ulmer, J.E.3
  • 48
    • 4043057882 scopus 로고    scopus 로고
    • Mechanistic studies of a flavin-dependent thymidylate synthase
    • Agrawal N, Lesley SA, Kuhn P et al. Mechanistic studies of a flavin-dependent thymidylate synthase. Biochemistry 2004; 43(32):10295-10301.
    • (2004) Biochemistry , vol.43 , Issue.32 , pp. 10295-10301
    • Agrawal, N.1    Lesley, S.A.2    Kuhn, P.3
  • 49
    • 48249142369 scopus 로고    scopus 로고
    • Flavin-dependent thymidylate synthase x limits chromosomal dna replication
    • Escartin F, Skouloubris S, Liebl U et al. Flavin-dependent thymidylate synthase X limits chromosomal DNA replication. Proc Natl Acad Sci USA 2008; 105(29):9948-9952.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.29 , pp. 9948-9952
    • Escartin, F.1    Skouloubris, S.2    Liebl, U.3
  • 50
    • 0034854206 scopus 로고    scopus 로고
    • Sequence-structure analysis of fad-containing proteins
    • Dym O, Eisenberg D. Sequence-structure analysis of FAD-containing proteins. Protein Sci 2001; 10(9):1712-1728.
    • (2001) Protein Sci , vol.10 , Issue.9 , pp. 1712-1728
    • Dym, O.1    Eisenberg, D.2
  • 51
    • 27144531195 scopus 로고
    • Purification of mcthylenetetrahydrofolate-dependent methyltransferase catalysizing biosynthesis of ribothymidine in transfer rna of streptococcus faecalis
    • Kisliuk RL, Brown GM, eds, New York: Elsevier/North Holland Publishing
    • Dclk AS, Nagle DP Jr, Rabinowitz JC. Purification of mcthylenetetrahydrofolate-dependent methyltransferase catalysizing biosynthesis of ribothymidine in transfer RNA of Streptococcus faecalis. In: Kisliuk RL, Brown GM, eds. Chemistry and Biology of Pteridines. New York: Elsevier/North Holland Publishing 1979:389-394.
    • (1979) Chemistry and Biology of Pteridines , pp. 389-394
    • Dclk, A.S.1    Nagle, D.P.2    Rabinowitz, J.C.3
  • 52
    • 44349185734 scopus 로고    scopus 로고
    • Structure of a trma-rna complex: A consensus rna fold contributes to substrate selectivity and catalysis in m5u mcthyltransferases
    • Alian A, Lee TT, Grincr SL et al. Structure of a TrmA-RNA complex: A consensus RNA fold contributes to substrate selectivity and catalysis in m5U mcthyltransferases. Proc Natl Acad Sci USA 2008; 105(19):6876-6881.
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.19 , pp. 6876-6881
    • Alian, A.1    Lee, T.T.2    Grincr, S.L.3
  • 53
    • 40449104681 scopus 로고    scopus 로고
    • Crystallization and preliminary x-ray crystallographic characterization of trmfo, a folate-dependent trna methyltransferase from thermotoga maritima
    • Cicmil N. Crystallization and preliminary X-ray crystallographic characterization of TrmFO, a folate-dependent tRNA methyltransferase from Thermotoga maritima. Acta Crystallogr Sect F Struct Biol Cryst Commun 2008; 64(Pt 3): 193-195.
    • (2008) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.64 , pp. 193-195
    • Cicmil, N.1
  • 54
    • 0035449350 scopus 로고    scopus 로고
    • Translational misreading: A trna modification counteracts a +2 ribosomal frameshift
    • Brcgeon D, Colot V, Radman M et al. Translational misreading: a tRNA modification counteracts a +2 ribosomal frameshift. Genes Dev 2001; 15(17):2295-2306.
    • (2001) Genes Dev , vol.15 , Issue.17 , pp. 2295-2306
    • Brcgeon, D.1    Colot, V.2    Radman, M.3
  • 55
    • 44949138270 scopus 로고    scopus 로고
    • Crystal structures of the conserved trna-modifying enzyme gida: implications for its interaction with mnme and substrate
    • Meyer S, Scrima A, Versées W et al. Crystal structures of the conserved tRNA-modifying enzyme GidA: implications for its interaction with MnmE and substrate. J Mol Biol 2008; 380(3):532-547.
    • (2008) J Mol Biol , vol.380 , Issue.3 , pp. 532-547
    • Meyer, S.1    Scrima, A.2    Versées, W.3
  • 56
    • 13244284641 scopus 로고    scopus 로고
    • The structure of the trme gtp-binding protein and its implications for trna modification
    • Scrima A, Vetter IR, Armengod ME et al. The structure of the TrmE GTP-binding protein and its implications for tRNA modification. EMBO J 2005; 24(1):23-33.
    • (2005) EMBO J , vol.24 , Issue.1 , pp. 23-33
    • Scrima, A.1    Vetter, I.R.2    Armengod, M.E.3
  • 57
    • 0038374971 scopus 로고    scopus 로고
    • Many paths to methyltransfer: A chronicle of convergence
    • Schubert HL, Blumenthal RM, Cheng X. Many paths to methyltransfer: a chronicle of convergence. Trends Biochem Sci 2003; 28(6):329-335.
    • (2003) Trends Biochem Sci , vol.28 , Issue.6 , pp. 329-335
    • Schubert, H.L.1    Blumenthal, R.M.2    Cheng, X.3
  • 58
    • 2342631335 scopus 로고    scopus 로고
    • S-adenosylmethionine: Nothing goes to waste
    • Fontecavc M, Area M, Mulliez E. S-adenosylmethionine: nothing goes to waste. Trends Biochem Sci 2004; 29(5):243-249.
    • (2004) Trends Biochem Sci , vol.29 , Issue.5 , pp. 243-249
    • Fontecavc, M.1    Area, M.2    Mulliez, E.3
  • 59
    • 44649153722 scopus 로고    scopus 로고
    • Design, synthesis and evaluation of potent thymidylatc synthase x inhibitors
    • Esra Onen F, Boum Y, Jacqucment C et al. Design, synthesis and evaluation of potent thymidylatc synthase X inhibitors. BioorgMed Chem Lett 2008; 18(12):3628-3631.
    • (2008) Bioorgmed Chem Lett , vol.18 , Issue.12 , pp. 3628-3631
    • Esra Onen, F.1    Boum, Y.2    Jacqucment, C.3
  • 60
    • 0033382609 scopus 로고    scopus 로고
    • Functional genomics and enzyme evolution. Homologous and analogous enzymes encoded in microbial genomes
    • Galperin MY, Koonin EV. Functional genomics and enzyme evolution. Homologous and analogous enzymes encoded in microbial genomes. Genetica 1999; 106(1-2):159-170.
    • (1999) Genetica , vol.106 , Issue.1-2 , pp. 159-170
    • Galperin, M.Y.1    Koonin, E.V.2
  • 61
    • 0017771466 scopus 로고
    • Evolution and tinkering
    • Jacob F. Evolution and tinkering. Science 1977; 196(4295):1161-1166.
    • (1977) Science , vol.196 , Issue.4295 , pp. 1161-1166
    • Jacob, F.1
  • 62
    • 0028650333 scopus 로고
    • Enzymatic mechanism of trna (M5u54)methyltransferase
    • Kealey JT, Gu X, Santi DV. Enzymatic mechanism of tRNA (m5U54)methyltransferase. Biochimie 1994; 76(12):1133-1142.
    • (1994) Biochimie , vol.76 , Issue.12 , pp. 1133-1142
    • Kealey, J.T.1    Gu, X.2    Santi, D.V.3
  • 63
    • 0035061447 scopus 로고    scopus 로고
    • Crystal structure of a deletion mutant of human thymidylatc synthase {{delta}} (7-29) and its ternary complex with tomudex and dump
    • Almog R, Waddling CA, Maley F et al Crystal structure of a deletion mutant of human thymidylatc synthase {{Delta}} (7-29) and its ternary complex with tomudex and dUMP. Protein Science 2001; 10(5):988.
    • (2001) Protein Science , vol.10 , Issue.5 , pp. 988
    • Almog, R.1    Waddling, C.A.2    Maley, F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.