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Mutagenesis and crystallographic studies of Zymomonas mobilis tRNA‐guanine transglycosylase to elucidate the role of serine 103 for enzymatic activity

dc.contributor.authorGrädler, Ulrichen_US
dc.contributor.authorFicner, Ralfen_US
dc.contributor.authorGarcia, George A.en_US
dc.contributor.authorStubbs, Milton T.en_US
dc.contributor.authorKlebe, Gerharden_US
dc.contributor.authorReuter, Klausen_US
dc.date.accessioned2016-01-04T20:52:05Z
dc.date.available2016-01-04T20:52:05Z
dc.date.issued1999-07-02en_US
dc.identifier.citationGrädler, Ulrich ; Ficner, Ralf; Garcia, George A.; Stubbs, Milton T.; Klebe, Gerhard; Reuter, Klaus (1999). "Mutagenesis and crystallographic studies of Zymomonas mobilis tRNAâ guanine transglycosylase to elucidate the role of serine 103 for enzymatic activity." FEBS Letters 454(1-2): 142-146.en_US
dc.identifier.issn0014-5793en_US
dc.identifier.issn1873-3468en_US
dc.identifier.urihttps://hdl.handle.net/2027.42/116371
dc.publisherWiley Periodicals, Inc.en_US
dc.subject.otherModified nucleosideen_US
dc.subject.othertRNAen_US
dc.subject.otherCrystal structureen_US
dc.subject.otherCatalytic mechanismen_US
dc.subject.otherQueuineen_US
dc.titleMutagenesis and crystallographic studies of Zymomonas mobilis tRNA‐guanine transglycosylase to elucidate the role of serine 103 for enzymatic activityen_US
dc.typeArticleen_US
dc.rights.robotsIndexNoFollowen_US
dc.subject.hlbsecondlevelBiological Chemistryen_US
dc.subject.hlbtoplevelScienceen_US
dc.description.peerreviewedPeer Revieweden_US
dc.contributor.affiliationumInterdepartmental Program in Medicinal Chemistry, College of Pharmacy, University of Michigan, Ann Arbor, MI 48109-1065, USAen_US
dc.contributor.affiliationotherInstitut für Pharmazeutische Chemie, Philipps-Universität Marburg, Marbacher Weg 6, 35032 Marburg, Germanyen_US
dc.contributor.affiliationotherInstitut für Molekularbiologie und Tumorforschung, Philipps-Universität Marburg, Emil-Mannkopff-Str. 2, 35037 Marburg, Germanyen_US
dc.description.bitstreamurlhttp://deepblue.lib.umich.edu/bitstream/2027.42/116371/1/feb2s0014579399007930.pdf
dc.identifier.doi10.1016/S0014-5793(99)00793-0en_US
dc.identifier.sourceFEBS Lettersen_US
dc.identifier.citedreferenceS.N. Ho, H.D. Hunt, R.M. Horton, J.K. Pullen, L.R. Pease, Gene, 77,( 1989 ), 51 – 59.en_US
dc.identifier.citedreferenceN. Okada, S. Nishimura, J. Biol. Chem., 254,( 1979 ), 3061 – 3066.en_US
dc.identifier.citedreferenceR.K. Slany, H. Kersten, Biochimie, 76,( 1994 ), 1178 – 1182.en_US
dc.identifier.citedreferenceH.M. Goodman, J. Abelson, A. Landy, S. Brenner, J.D. Smith, Nature, 217,( 1968 ), 1019 – 1024.en_US
dc.identifier.citedreferenceF. Harada, S. Nishimura, Biochemistry, 11,( 1983 ), 302 – 308.en_US
dc.identifier.citedreferenceJ.R. Katze, B. Basile, J.A. McCloskey, Science, 216,( 1982 ), 55 – 56.en_US
dc.identifier.citedreferenceJ.R. Katze, U. Gündzün, D.L. Smith, C.S. Chen, J.A. McCloskey, Biochemistry, 23,( 1984 ), 1171 – 1176.en_US
dc.identifier.citedreferenceB.C. Persson, Mol. Microbiol., 8,( 1994 ), 1011 – 1016.en_US
dc.identifier.citedreferenceB.N. White, G.M. Tener, J. Holden, T. Suzuki, J. Mol. Biol., 74,( 1973 ), 635 – 651.en_US
dc.identifier.citedreferenceG. Dirheimer, W. Baranowski, G. Keith, Biochimie, 77,( 1995 ), 99 – 103.en_US
dc.identifier.citedreferenceJ.M. Durand, N. Okada, T. Tobe, M. Watarai, I. Fukuda, T. Suzuki, N. Nakata, K. Komatsu, M. Yoshikawa, C. Sasakawa, J. Bacteriol., 176,( 1994 ), 4627 – 4634.en_US
dc.identifier.citedreferenceC. Romier, K. Reuter, D. Suck, R. Ficner, EMBO J., 15,( 1996 ), 2850 – 2857.en_US
dc.identifier.citedreferenceC. Romier, K. Reuter, D. Suck, R. Ficner, Biochemistry, 35,( 1996 ), 15734 – 15739.en_US
dc.identifier.citedreferenceS. Nogushi, Y. Nishimura, Y. Hirota, S. Nishimura, J. Biol. Chem., 257,( 1982 ), 6544 – 6550.en_US
dc.identifier.citedreferenceK. Reuter, S. Chong, F. Ullrich, H. Kersten, G.A. Garcia, Biochemistry, 33,( 1994 ), 7041 – 7046.en_US
dc.identifier.citedreferenceC. Romier, J.E.W. Meyer, D. Suck, FEBS Lett., 416,( 1997 ), 93 – 98.en_US
dc.identifier.citedreferenceK. Reuter, R. Ficner, J. Bacteriol., 177,( 1995 ), 5284 – 5288.en_US
dc.identifier.citedreferenceOtwinowski, Z. (1993) DENZO, Yale University, New Haven, CT.en_US
dc.identifier.citedreferenceM. Ansaldi, M. Lepelletier, V. Mejean, Anal. Biochem., 234,( 1996 ), 110 – 111.en_US
dc.identifier.citedreferenceH. Akimoto, E. Imamiya, T. Hitaka, H. Nomura, S. Nishimura, J. Chem. Soc. Perkin Trans., 1,( 1988 ), 1638 – 1644.en_US
dc.identifier.citedreferenceC. Romier, R. Ficner, K. Reuter, D. Suck, Proteins Struct. Funct. Genet., 24,( 1996 ), 516 – 519.en_US
dc.identifier.citedreferenceBrünger, A.T. (1992) XPLOR, Version 3.4, Yale University, New Haven, CT.en_US
dc.identifier.citedreferenceT.A. Jones, J.Y. Zou, S.W. Cowan, M. Kjeldgaard, O Acta Cryst., A47,( 1991 ), 110 – 119.en_US
dc.identifier.citedreferenceV.S. Lamzin, K.S. Wilson, ARP Acta Cryst., D49,( 1993 ), 129 – 147.en_US
dc.identifier.citedreferenceS. Yokoyama, T. Miyazawa, Y. Iitaka, Z. Yamaizumi, H. Kasai, S. Nishimura, Nature, 282,( 1979 ), 107 – 109.en_US
dc.identifier.citedreferenceA.T. Brünger, Nature, 355,( 1992 ), 472 – 474.en_US
dc.owningcollnameInterdisciplinary and Peer-Reviewed


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