메뉴 건너뛰기




Volumn 48, Issue 47, 2009, Pages 11243-11251

Identification of the rate-determining step of tRNA-guanine transglycosylase from Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTATES; COVALENT COMPLEX; EXCHANGE PROCESS; GLYCOSIDIC BOND; HYDROXYL GROUPS; NEGATIVE CHARGE; OVERALL RATE; RATE DETERMINING STEP; REACTION PATHWAYS; STEADY STATE;

EID: 72749105136     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi901501a     Document Type: Article
Times cited : (11)

References (14)
  • 2
    • 5644289361 scopus 로고    scopus 로고
    • The pseudouridine synthases: Revisiting a mechanism that seemed settled
    • Spedaliere, C. J., et al. (2004) The pseudouridine synthases: Revisiting a mechanism that seemed settled. J. Am. Chem. Soc. 126, 12758-12759.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 12758-12759
    • Spedaliere, C.J.1
  • 3
    • 0029754654 scopus 로고    scopus 로고
    • Mutagenesis and crystallographic studies of Zymomonas mobilis tRNA- Guanine transglycosylase reveal aspartate 102 as the active site nucleophile
    • DOI 10.1021/bi962003n
    • Romier, C., et al. (1996) Mutagenesis and crystallographic studies of Zymomonas mobilis tRNA-guanine transglycosylase reveal aspartate 102 as the active site nucleophile. Biochemistry 35, 15734-15739. (Pubitemid 26422310)
    • (1996) Biochemistry , vol.35 , Issue.49 , pp. 15734-15739
    • Romier, C.1    Reuter, K.2    Suck, D.3    Ficner, R.4
  • 4
    • 0033963529 scopus 로고    scopus 로고
    • Glycosidase mechanisms: Anatomy of a finely tuned catalyst
    • Zechel, D. L., and Withers, S. G. (2000) Glycosidase mechanisms: Anatomy of a finely tuned catalyst. Acc. Chem. Res. 33, 11-18.
    • (2000) Acc. Chem. Res. , vol.33 , pp. 11-18
    • Zechel, D.L.1    Withers, S.G.2
  • 5
    • 0035960560 scopus 로고    scopus 로고
    • TRNA-guanine transglycosylase from Escherichia coli: Molecular mechanism and role of aspartate 89
    • DOI 10.1021/bi0110589
    • Kittendorf, J. D., et al. (2001) tRNA-guanine transglycosylase from Escherichia coli: Molecular mechanism and role of aspartate 89. Biochemistry 40, 14123-14133. (Pubitemid 33081615)
    • (2001) Biochemistry , vol.40 , Issue.47 , pp. 14123-14133
    • Kittendorf, J.D.1    Barcomb, L.M.2    Nonekowski, S.T.3    Garcia, G.A.4
  • 6
    • 0142149105 scopus 로고    scopus 로고
    • An essential role for aspartate 264 in catalysis by tRNA-guanine transglycosylase from Escherichia coli
    • Kittendorf, J. D., et al. (2003) An essential role for aspartate 264 in catalysis by tRNA-guanine transglycosylase from Escherichia coli. J. Biol. Chem. 278, 42369-42376.
    • (2003) J. Biol. Chem. , vol.278 , pp. 42369-42376
    • Kittendorf, J.D.1
  • 7
    • 0038160045 scopus 로고    scopus 로고
    • TRNA-Guanine Transglycosylase fromEscherichia coli:APing-Pong KineticMechanism is Consistent with Nucleophilic Catalysis
    • Goodenough-Lashua, D.M., and Garcia, G. A. (2003) tRNA-Guanine Transglycosylase fromEscherichia coli:APing-Pong KineticMechanism is Consistent with Nucleophilic Catalysis. Bioorg. Chem. 31, 331-344.
    • (2003) Bioorg. Chem. , vol.31 , pp. 331-344
    • Goodenough-Lashua, D.M.1    Garcia, G.A.2
  • 8
    • 34548739667 scopus 로고    scopus 로고
    • Probing the Intermediacy of Covalent RNA-Enzyme Complexes in RNA Modification Enzymes
    • Chervin, S. M., Kittendorf, J. D., and Garcia, G. A. (2007) Probing the Intermediacy of Covalent RNA-Enzyme Complexes in RNA Modification Enzymes. Methods Enzymol. 425, 121-137.
    • (2007) Methods Enzymol. , vol.425 , pp. 121-137
    • Chervin, S.M.1    Kittendorf, J.D.2    Garcia, G.A.3
  • 9
    • 0027300858 scopus 로고
    • TRNA-Guanine Transglycosylase from Escherichia coli: Gross tRNA Structural Requirements for Recognition
    • Curnow, A. W., et al. (1993) tRNA-Guanine Transglycosylase from Escherichia coli: Gross tRNA Structural Requirements for Recognition. Biochemistry 32, 5239-5246.
    • (1993) Biochemistry , vol.32 , pp. 5239-5246
    • Curnow, A.W.1
  • 10
    • 0034757682 scopus 로고    scopus 로고
    • TRNA Recognition by the E. coli TGT: The Role of U33 in U-G-U Sequence Recognition
    • Nonekowski, S. T., and Garcia, G. A. (2001) tRNA Recognition by the E. coli TGT: The Role of U33 in U-G-U Sequence Recognition. RNA 7, 1432-1441.
    • (2001) RNA , vol.7 , pp. 1432-1441
    • Nonekowski, S.T.1    Garcia, G.A.2
  • 11
    • 0036510739 scopus 로고    scopus 로고
    • The Escherichia coli tRNA-Guanine Transglycosylase Can Recognize and Modify DNA
    • Nonekowski, S. T., Kung, F. L., and Garcia, G. A. (2002) The Escherichia coli tRNA-Guanine Transglycosylase Can Recognize and Modify DNA. J. Biol. Chem. 277, 7178-7182.
    • (2002) J. Biol. Chem. , vol.277 , pp. 7178-7182
    • Nonekowski, S.T.1    Kung, F.L.2    Garcia, G.A.3
  • 12
    • 0141596159 scopus 로고    scopus 로고
    • Chemical trapping and crystal structure of a catalytic tRNA guanine transglycosylase covalent intermediate
    • Xie, W., Liu, X. J., and Huang, R. H. (2003) Chemical trapping and crystal structure of a catalytic tRNA guanine transglycosylase covalent intermediate. Nat. Struct. Biol. 10, 781-788.
    • (2003) Nat. Struct. Biol. , vol.10 , pp. 781-788
    • Xie, W.1    Liu, X.J.2    Huang, R.H.3
  • 14
    • 0032514723 scopus 로고    scopus 로고
    • Transient kinetics of formation and reaction of the uridylyl-enzyme form of galactose-1-P uridylyltransferase and its Q168R-variant: Insight into the molecular basis of galactosemia
    • DOI 10.1021/bi9815546
    • Geeganage, S., and Frey, P. A. (1998) Transient Kinetics of Formation and Reaction of the Uridylyl-Enzyme Form of Galactose-1-P Uridylyltransferase and Its Q168R Variant: Insight into the Molecular Basis of Galactosemia. Biochemsitry 37, 14500-14507. (Pubitemid 28489058)
    • (1998) Biochemistry , vol.37 , Issue.41 , pp. 14500-14507
    • Geeganage, S.1    Frey, P.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.