메뉴 건너뛰기




Volumn 379, Issue 3, 2008, Pages 568-578

Molecular Mechanism of ADP-Ribose Hydrolysis By Human NUDT5 From Structural and Kinetic Studies

Author keywords

ADP ribose pyrophosphatase; ADPR; molecular mechanism; Nudix domain; NUDT5

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSE; ADENOSINE PHOSPHATE; ALPHA,BETA METHYLENEADENOSINE DIPHOSPHORIBOSE; ARGININE; GLUTAMIC ACID; INORGANIC PYROPHOSPHATASE; MAGNESIUM ION; NUDIX HYDROLASE; PROTEIN NUDT5; RIBOSE PHOSPHATE; TRYPTOPHAN; WATER;

EID: 43449120696     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2008.04.006     Document Type: Article
Times cited : (29)

References (31)
  • 1
    • 0029835350 scopus 로고    scopus 로고
    • The MutT proteins or “Nudix” hydrolases, a family of versatile, widely distributed, “housecleaning” enzymes
    • Bessman M.J. Frick D.N. O'Handley S.F. The MutT proteins or “Nudix” hydrolases, a family of versatile, widely distributed, “housecleaning” enzymes J. Biol. Chem. 271 1996 25059 25062
    • (1996) J. Biol. Chem. , vol.271 , pp. 25059-25062
    • Bessman, M.J.1    Frick, D.N.2    O'Handley, S.F.3
  • 2
    • 0035026968 scopus 로고    scopus 로고
    • The structure of ADP-ribose pyrophosphatase reveals the structural basis for the versatility of the Nudix family
    • Gabelli S.B. Bianchet M.A. Bessman M.J. Amzel L.M. The structure of ADP-ribose pyrophosphatase reveals the structural basis for the versatility of the Nudix family Nat. Struct. Biol. 8 2001 467 472
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 467-472
    • Gabelli, S.B.1    Bianchet, M.A.2    Bessman, M.J.3    Amzel, L.M.4
  • 3
    • 2642579311 scopus 로고    scopus 로고
    • The 26 Nudix hydrolases of Bacillus cereus, a close relative of Bacillus anthracis
    • Xu W. Dunn C.A. Jones C.R. D'Souza G. Bessman M.J. The 26 Nudix hydrolases of Bacillus cereus , a close relative of Bacillus anthracis J. Biol. Chem. 279 2004 24861 24865
    • (2004) J. Biol. Chem. , vol.279 , pp. 24861-24865
    • Xu, W.1    Dunn, C.A.2    Jones, C.R.3    D'Souza, G.4    Bessman, M.J.5
  • 4
    • 85120280681 scopus 로고
    • Aspects of NAD metabolism in prokaryotes and eukaryotes
    • Olivera B.M. Hughes K.T. Cordray P. Roth J.R. Aspects of NAD metabolism in prokaryotes and eukaryotes M.K. Jacobson E.L. Jacobson ADP-ribose transfer reactions. Mechanisms and biological significance 1989 Springer Verlag New York, NY
    • (1989)
    • Olivera, B.M.1    Hughes, K.T.2    Cordray, P.3    Roth, J.R.4
  • 5
    • 0031700924 scopus 로고    scopus 로고
    • Endogenous relatives of ADP-ribosylating bacterial toxins in mice and men: potential regulators of immune cell function
    • Haag F. Koch-Nolte F. Endogenous relatives of ADP-ribosylating bacterial toxins in mice and men: potential regulators of immune cell function J. Biol. Regul. Homeostatic Agents 12 1998 53 62
    • (1998) J. Biol. Regul. Homeostatic Agents , vol.12 , pp. 53-62
    • Haag, F.1    Koch-Nolte, F.2
  • 6
    • 33749260519 scopus 로고    scopus 로고
    • Nuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going?
    • Hassa P.O. Haenni S.S. Elser M. Hottiger M.O. Nuclear ADP-ribosylation reactions in mammalian cells: where are we today and where are we going? Microbiol. Mol. Biol. Rev. 70 2006 789 829
    • (2006) Microbiol. Mol. Biol. Rev. , vol.70 , pp. 789-829
    • Hassa, P.O.1    Haenni, S.S.2    Elser, M.3    Hottiger, M.O.4
  • 8
    • 0028044188 scopus 로고
    • Enzymatic and nonenzymatic ADP-ribosylation of cysteine
    • McDonald L.J. Moss J. Enzymatic and nonenzymatic ADP-ribosylation of cysteine Mol. Cell. Biochem. 138 1994 221 226
    • (1994) Mol. Cell. Biochem. , vol.138 , pp. 221-226
    • McDonald, L.J.1    Moss, J.2
  • 9
    • 0024543962 scopus 로고
    • Nonmuscle actin ADP-ribosylated by botulinum C2 toxin caps actin filaments
    • Weigt C. Just I. Wegner A. Aktories K. Nonmuscle actin ADP-ribosylated by botulinum C2 toxin caps actin filaments FEBS Lett. 246 1989 181 184
    • (1989) FEBS Lett. , vol.246 , pp. 181-184
    • Weigt, C.1    Just, I.2    Wegner, A.3    Aktories, K.4
  • 12
    • 33847065453 scopus 로고    scopus 로고
    • Regulation of calcium signalling by adenine-based second messengers
    • Fliegert R. Gasser A. Guse A.H. Regulation of calcium signalling by adenine-based second messengers Biochem. Soc. Trans. 35 2007 109 114
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 109-114
    • Fliegert, R.1    Gasser, A.2    Guse, A.H.3
  • 15
    • 0043133626 scopus 로고    scopus 로고
    • Structure and mechanism of MT-ADPRase, a Nudix hydrolase from Mycobacterium tuberculosis
    • Kang L.W. Gabelli S.B. Cunningham J.E. O'Handley S.F. Amzel L.M. Structure and mechanism of MT-ADPRase, a Nudix hydrolase from Mycobacterium tuberculosis Structure 11 2003 1015 1023
    • (2003) Structure , vol.11 , pp. 1015-1023
    • Kang, L.W.1    Gabelli, S.B.2    Cunningham, J.E.3    O'Handley, S.F.4    Amzel, L.M.5
  • 16
    • 4344578596 scopus 로고    scopus 로고
    • Structural insights into the Thermus thermophilus ADP-ribose pyrophosphatase mechanism via crystal structures with the bound substrate and metal
    • Yoshiba S. Ooga T. Nakagawa N. Shibata T. Inoue Y. Yokoyama S. Structural insights into the Thermus thermophilus ADP-ribose pyrophosphatase mechanism via crystal structures with the bound substrate and metal J. Biol. Chem. 279 2004 37163 37174
    • (2004) J. Biol. Chem. , vol.279 , pp. 37163-37174
    • Yoshiba, S.1    Ooga, T.2    Nakagawa, N.3    Shibata, T.4    Inoue, Y.5    Yokoyama, S.6
  • 17
    • 21644479309 scopus 로고    scopus 로고
    • Molecular mechanism of the Thermus thermophilus ADP-ribose pyrophosphatase from mutational and kinetic studies
    • Ooga T. Yoshiba S. Nakagawa N. Kuramitsu S. Masui R. Molecular mechanism of the Thermus thermophilus ADP-ribose pyrophosphatase from mutational and kinetic studies Biochemistry 44 2005 9320 9329
    • (2005) Biochemistry , vol.44 , pp. 9320-9329
    • Ooga, T.1    Yoshiba, S.2    Nakagawa, N.3    Kuramitsu, S.4    Masui, R.5
  • 18
    • 38649105493 scopus 로고    scopus 로고
    • Structural basis for different substrate specificities of two ADP-ribose pyrophosphatases from Thermus thermophilus HB8
    • Wakamatsu T. Nakagawa N. Kuramitsu S. Masui R. Structural basis for different substrate specificities of two ADP-ribose pyrophosphatases from Thermus thermophilus HB8 J. Bacteriol. 190 2008 1108 1117
    • (2008) J. Bacteriol. , vol.190 , pp. 1108-1117
    • Wakamatsu, T.1    Nakagawa, N.2    Kuramitsu, S.3    Masui, R.4
  • 20
    • 33751077100 scopus 로고    scopus 로고
    • Crystal structures of human NUDT5 reveal insights into the structural basis of the substrate specificity
    • Zha M. Zhong C. Peng Y. Hu H. Ding J. Crystal structures of human NUDT5 reveal insights into the structural basis of the substrate specificity J. Mol. Biol. 364 2006 1021 1033
    • (2006) J. Mol. Biol. , vol.364 , pp. 1021-1033
    • Zha, M.1    Zhong, C.2    Peng, Y.3    Hu, H.4    Ding, J.5
  • 21
    • 0037203939 scopus 로고    scopus 로고
    • Cloning, expression and characterisation of a human Nudix hydrolase specific for adenosine 5′-diphosphoribose (ADP-ribose)
    • Lin S. Gasmi L. Xie Y. Ying K. Gu S. Wang Z. Cloning, expression and characterisation of a human Nudix hydrolase specific for adenosine 5′-diphosphoribose (ADP-ribose) Biochim. Biophys. Acta 1594 2002 127 135
    • (2002) Biochim. Biophys. Acta , vol.1594 , pp. 127-135
    • Lin, S.1    Gasmi, L.2    Xie, Y.3    Ying, K.4    Gu, S.5    Wang, Z.6
  • 22
    • 0034708599 scopus 로고    scopus 로고
    • Cloning and characterization of a new member of the Nudix hydrolases from human and mouse
    • Yang H. Slupska M.M. Wei Y.F. Tai J.H. Luther W.M. Xia Y.R. Cloning and characterization of a new member of the Nudix hydrolases from human and mouse J. Biol. Chem. 275 2000 8844 8853
    • (2000) J. Biol. Chem. , vol.275 , pp. 8844-8853
    • Yang, H.1    Slupska, M.M.2    Wei, Y.F.3    Tai, J.H.4    Luther, W.M.5    Xia, Y.R.6
  • 23
    • 0033452851 scopus 로고    scopus 로고
    • Cloning, expression and characterization of YSA1H, a human adenosine 5′-diphosphosugar pyrophosphatase possessing a MutT motif
    • Gasmi L. Cartwright J.L. McLennan A.G. Cloning, expression and characterization of YSA1H, a human adenosine 5′-diphosphosugar pyrophosphatase possessing a MutT motif Biochem. J. 344 1999 331 337
    • (1999) Biochem. J. , vol.344 , pp. 331-337
    • Gasmi, L.1    Cartwright, J.L.2    McLennan, A.G.3
  • 24
    • 0345330064 scopus 로고    scopus 로고
    • An improved activity assay method for arginine kinase based on a ternary heteropolyacid system
    • Chen B. Guo Q. Guo Z. Wang X. An improved activity assay method for arginine kinase based on a ternary heteropolyacid system Tsinghua Sci. and Technol. 8 2003 422 427
    • (2003) Tsinghua Sci. and Technol. , vol.8 , pp. 422-427
    • Chen, B.1    Guo, Q.2    Guo, Z.3    Wang, X.4
  • 25
    • 0033527537 scopus 로고    scopus 로고
    • Studies on the ADP-ribose pyrophosphatase subfamily of the Nudix hydrolases and tentative identification of trgB, a gene associated with tellurite resistance
    • Dunn C.A. O'Handley S.F. Frick D.N. Bessman M.J. Studies on the ADP-ribose pyrophosphatase subfamily of the Nudix hydrolases and tentative identification of trgB, a gene associated with tellurite resistance J. Biol. Chem. 274 1999 32318 32324
    • (1999) J. Biol. Chem. , vol.274 , pp. 32318-32324
    • Dunn, C.A.1    O'Handley, S.F.2    Frick, D.N.3    Bessman, M.J.4
  • 26
    • 0030997672 scopus 로고    scopus 로고
    • Efficient synthesis of methylenebis(phosphonate) analogues of P1,P2-disubstituted pyrophosphates of biological interest. A novel plausible mechanism
    • Pankiewicz K. Lesiak K. Watanabe K. Efficient synthesis of methylenebis(phosphonate) analogues of P1,P2-disubstituted pyrophosphates of biological interest. A novel plausible mechanism J. Am. Chem. Soc. 119 1997 3691 3695
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 3691-3695
    • Pankiewicz, K.1    Lesiak, K.2    Watanabe, K.3
  • 27
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z. Minor W. Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276 1997 307 326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 29
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A. Zou J.Y. Cowan S.W. Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallogr., Sect. A: Found. Crystallogr. 47 1991 110 119
    • (1991) Acta Crystallogr., Sect. A: Found. Crystallogr. , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.