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Volumn 50, Issue 21, 2011, Pages 4712-4719

RCL hydrolyzes 2'-deoxyribonucleoside 5'-monophosphate via formation of a reaction intermediate

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ANALYSIS; BOND CLEAVAGES; CATALYTIC MECHANISMS; CATALYTIC REACTIONS; DISSOCIATION CONSTANT; HOMODIMERS; KINETIC EVIDENCE; METHANOLYSIS; MONOPHOSPHATES; MULTIDIMENSIONAL NMR; NMR STUDIES; PHOSPHATE GROUP; SITE DIRECTED MUTAGENESIS; STRUCTURAL STUDIES; WILD TYPES;

EID: 79958123286     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi101742z     Document Type: Article
Times cited : (12)

References (32)
  • 1
    • 34247230158 scopus 로고    scopus 로고
    • The c-Myc target gene Rcl (C6orf108) encodes a novel enzyme, deoxynucleoside 5′-monophosphate N-glycosidase
    • DOI 10.1074/jbc.M610648200
    • Ghiorghi, Y. K., Zeller, K. I., Dang, C. V., and Kaminski, P. A. (2007) The c-Myc target gene Rcl (C6orf108) encodes a novel enzyme, deoxynucleoside 50-monophosphate N-glycosidase. J. Biol. Chem. 282, 8150-8156. (Pubitemid 47093578)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.11 , pp. 8150-8156
    • Ghiorghi, Y.K.1    Zeller, K.I.2    Dang, C.V.3    Kaminski, P.A.4
  • 2
    • 0030794277 scopus 로고    scopus 로고
    • Identification of putative c-Myc-responsive genes: Characterization of rcl, a novel growth-related gene
    • Lewis, B. C., Shim, H., Li, Q., Wu, C. S., Lee, L. A., Maity, A., and Dang, C. V. (1997) Identification of putative c-Myc-responsive genes: Characterization of rcl, a novel growth-related gene. Mol. Cell. Biol. 17, 4967-4978. (Pubitemid 27357596)
    • (1997) Molecular and Cellular Biology , vol.17 , Issue.9 , pp. 4967-4978
    • Lewis, B.C.1    Shim, H.2    Li, Q.3    Wu, C.S.4    Lee, L.A.5    Maity, A.6    Dang, C.V.7
  • 3
    • 0037154774 scopus 로고    scopus 로고
    • Induction of rcl, a novel growth-related gene by Coptidis Rhizoma in rat H4IIE cells
    • DOI 10.1016/S0024-3205(01)01547-8, PII S0024320501015478
    • Chan, C. P., But, P. P., and Ho, J. W. (2002) Induction of rcl, a novel growth-related gene by coptidis rhizoma in rat H4IIE cells. Life Sci. 70, 1691-1699. (Pubitemid 34178376)
    • (2002) Life Sciences , vol.70 , Issue.14 , pp. 1691-1699
    • Chan, C.P.1    But, P.P.-H.2    Ho, J.W.3
  • 4
    • 34249785105 scopus 로고    scopus 로고
    • A microarray analysis of the temporal response of liver to methylprednisolone: A comparative analysis of two dosing regimens
    • DOI 10.1210/en.2006-0790
    • Almon, R. R., DuBois, D. C., and Jusko, W. J. (2007) A microarray analysis of the temporal response of liver to methylprednisolone: A comparative analysis of two dosing regimens. Endocrinology 148, 2209-2225. (Pubitemid 46997037)
    • (2007) Endocrinology , vol.148 , Issue.5 , pp. 2209-2225
    • Almon, R.R.1    Dubois, D.C.2    Jusko, W.J.3
  • 5
    • 17644407354 scopus 로고    scopus 로고
    • Analysis of gene expression induced by diethylstilbestrol (DES) in human primitive Müllerian duct cells using microarray
    • DOI 10.1016/j.canlet.2004.07.024
    • Miki, Y., Suzuki, T., Tazawa, C., Ishizuka, M., Semba, S., Gorai, I., and Sasano, H. (2005) Analysis of gene expression induced by diethylstilbestrol (DES) in human primitive Mullerian duct cells using microarray. Cancer Lett. 220, 197-210. (Pubitemid 40568777)
    • (2005) Cancer Letters , vol.220 , Issue.2 , pp. 197-210
    • Miki, Y.1    Suzuki, T.2    Tazawa, C.3    Ishizuka, M.4    Semba, S.5    Gorai, I.6    Sasano, H.7
  • 6
  • 7
    • 0036682376 scopus 로고    scopus 로고
    • Meta-analysis of microarrays: Interstudy validation of gene expression profiles reveals pathway dysregulation in prostate cancer
    • Rhodes, D. R., Barrette, T. R., Rubin, M. A., Ghosh, D., and Chinnaiyan, A. M. (2002) Meta-analysis of microarrays: Interstudy validation of gene expression profiles reveals pathway dysregulation in prostate cancer. Cancer Res. 62, 4427-4433. (Pubitemid 34827303)
    • (2002) Cancer Research , vol.62 , Issue.15 , pp. 4427-4433
    • Rhodes, D.R.1    Barrette, T.R.2    Rubin, M.A.3    Ghosh, D.4    Chinnaiyan, A.M.5
  • 8
    • 0037648338 scopus 로고    scopus 로고
    • Skp2 regulates Myc protein stability and activity
    • DOI 10.1016/S1097-2765(03)00173-4
    • Kim, S. Y., Herbst, A., Tworkowski, K. A., Salghetti, S. E., and Tansey, W. P. (2003) Skp2 regulates Myc protein stability and activity. Mol. Cell 11, 1177-1188. (Pubitemid 36645138)
    • (2003) Molecular Cell , vol.11 , Issue.5 , pp. 1177-1188
    • Kim, S.Y.1    Herbst, A.2    Tworkowski, K.A.3    Salghetti, S.E.4    Tansey, W.P.5
  • 10
    • 0842278571 scopus 로고    scopus 로고
    • An integrated database of genes responsive to the Myc oncogenic transcription factor: Identification of direct genomic targets
    • Zeller, K. I., Jegga, A. G., Aronow, B. J., O'Donnell, K. A., and Dang, C. V. (2003) An integrated database of genes responsive to the Myc oncogenic transcription factor: Identification of direct genomic targets. Genome Biol. 4, R69.
    • (2003) Genome Biol. , vol.4
    • Zeller, K.I.1    Jegga, A.G.2    Aronow, B.J.3    O'Donnell, K.A.4    Dang, C.V.5
  • 11
    • 70449534068 scopus 로고    scopus 로고
    • Solution structure of RCL, a novel 20- deoxyribonucleoside 50-monophosphate N-glycosidase
    • Doddapaneni, K., Mahler, B., Pavlovicz, R., Haushalter, A., Yuan, C., and Wu, Z. (2009) Solution structure of RCL, a novel 20- deoxyribonucleoside 50-monophosphate N-glycosidase. J. Mol. Biol. 394, 423-434.
    • (2009) J. Mol. Biol , vol.394 , pp. 423-434
    • Doddapaneni, K.1    Mahler, B.2    Pavlovicz, R.3    Haushalter, A.4    Yuan, C.5    Wu, Z.6
  • 12
    • 70449519338 scopus 로고    scopus 로고
    • Structural characterization of the mammalian deoxynucleotide N-hydrolase Rcl and its stabilizing interactions with two inhibitors
    • Yang, Y., Padilla, A., Zhang, C., Labesse, G., and Kaminski, P. A. (2009) Structural characterization of the mammalian deoxynucleotide N-hydrolase Rcl and its stabilizing interactions with two inhibitors. J. Mol. Biol. 394, 435-447.
    • (2009) J. Mol. Biol , vol.394 , pp. 435-447
    • Yang, Y.1    Padilla, A.2    Zhang, C.3    Labesse, G.4    Kaminski, P.A.5
  • 13
    • 0029643856 scopus 로고    scopus 로고
    • Crystal structures of nucleoside 2-deoxyribosyltransferase in native and ligand-bound forms reveal architecture of the active site
    • Armstrong, S. R., Cook, W. J., Short, S. A., and Ealick, S. E. (1996) Crystal structures of nucleoside 2-deoxyribosyltransferase in native and ligand-bound forms reveal architecture of the active site. Structure 4, 97-107. (Pubitemid 126658528)
    • (1996) Structure , vol.4 , Issue.1 , pp. 97-107
    • Armstrong, S.R.1    Cook, W.J.2    Short, S.A.3    Ealick, S.E.4
  • 14
    • 0029034947 scopus 로고
    • Identification of the active site nucleophile in nucleoside 2-deoxyribosyltransferase as glutamic acid 98
    • Porter, D. J., Merrill, B. M., and Short, S. A. (1995) Identification of the active site nucleophile in nucleoside 2-deoxyribosyltransferase as glutamic acid 98. J. Biol. Chem. 270, 15551-15556.
    • (1995) J. Biol. Chem , vol.270 , pp. 15551-15556
    • Porter, D.J.1    Merrill, B.M.2    Short, S.A.3
  • 15
    • 1542267775 scopus 로고    scopus 로고
    • Structures of Purine 2′-Deoxyribosyltransferase, Substrate Complexes, and the Ribosylated Enzyme Intermediate at 2.0 Å Resolution
    • DOI 10.1021/bi035723k
    • Anand, R., Kaminski, P. A., and Ealick, S. E. (2004) Structures of purine 20-deoxyribosyltransferase, substrate complexes, and the ribosylated enzyme intermediate at 2.0 A resolution. Biochemistry 43, 2384-2393. (Pubitemid 38327833)
    • (2004) Biochemistry , vol.43 , Issue.9 , pp. 2384-2393
    • Anand, R.1    Kaminski, P.A.2    Ealick, S.E.3
  • 16
    • 0029959892 scopus 로고    scopus 로고
    • Active site amino acids that participate in the catalytic mechanism of nucleoside 20-deoxyribosyltransferase
    • Short, S. A., Armstrong, S. R., Ealick, S. E., and Porter, D. J. (1996) Active site amino acids that participate in the catalytic mechanism of nucleoside 20-deoxyribosyltransferase. J. Biol. Chem. 271, 4978-4987.
    • (1996) J. Biol. Chem , vol.271 , pp. 4978-4987
    • Short, S.A.1    Armstrong, S.R.2    Ealick, S.E.3    Porter, D.J.4
  • 17
    • 78650675594 scopus 로고    scopus 로고
    • Probing the Active Site of the Deoxynucleotide N-Hydrolase Rcl Encoded by the Rat Gene c6orf108
    • Dupouy, C., Zhang, C., Padilla, A., Pochet, S., and Kaminski, P. A. (2010) Probing the Active Site of the Deoxynucleotide N-Hydrolase Rcl Encoded by the Rat Gene c6orf108. J. Biol. Chem. 285, 41806-41814.
    • (2010) J. Biol. Chem. , vol.285 , pp. 41806-41814
    • Dupouy, C.1    Zhang, C.2    Padilla, A.3    Pochet, S.4    Kaminski, P.A.5
  • 18
    • 0348111556 scopus 로고    scopus 로고
    • Catalysis by nucleoside hydrolases
    • DOI 10.1016/j.sbi.2003.10.002
    • Versees, W., and Steyaert, J. (2003) Catalysis by nucleoside hydrolases. Curr. Opin. Struct. Biol. 13, 731-738. (Pubitemid 37522149)
    • (2003) Current Opinion in Structural Biology , vol.13 , Issue.6 , pp. 731-738
    • Versees, W.1    Steyaert, J.2
  • 19
    • 0025833737 scopus 로고
    • Nucleoside hydrolase from Crithidia fasciculata: Metabolic role, purification, specificity, and kinetic mechanism
    • Parkin, D. W., Horenstein, B. A., Abdulah, D. R., Estupinan, B., and Schramm, V. L. (1991) Nucleoside hydrolase from Crithidia fasciculata. Metabolic role, purification, specificity, and kinetic mechanism. J. Biol. Chem. 266, 20658-20665. (Pubitemid 21908513)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.31 , pp. 20658-20665
    • Parkin, D.W.1    Horenstein, B.A.2    Abdulah, D.R.3    Estupinan, B.4    Schramm, V.L.5
  • 20
    • 0025738381 scopus 로고
    • Characterization of the mutT nucleoside triphosphatase of Escherichia coli
    • Bhatnagar, S. K., Bullions, L. C., and Bessman, M. J. (1991) Characterization of the mutT nucleoside triphosphatase of Escherichia coli. J. Biol. Chem. 266, 9050-9054. (Pubitemid 21906617)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.14 , pp. 9050-9054
    • Bhatnagar, S.K.1    Bullions, L.C.2    Bessman, M.J.3
  • 22
    • 0345311216 scopus 로고
    • 1Hand13Cassignments from sensitivity enhanced detection of heteronuclear multiple bond connectivity by 2D multiple quantum NMR
    • Bax, A., and Summers,M. F. (1986) 1Hand13Cassignments from sensitivity enhanced detection of heteronuclear multiple bond connectivity by 2D multiple quantum NMR. J. Am. Chem. Soc. 108, 2093-2094.
    • (1986) J. Am. Chem. Soc , vol.108 , pp. 2093-2094
    • Bax, A.1    Summers, M.F.2
  • 23
    • 33745304189 scopus 로고    scopus 로고
    • Characterization of BIsM, a nucleotide hydrolase involved in cytosine production for the biosynthesis of blasticidin S
    • DOI 10.1002/cbic.200600026
    • Grochowski, L. L., and Zabriskie, T. M. (2006) Characterization of BlsM, a nucleotide hydrolase involved in cytosine production for the biosynthesis of blasticidin S. ChemBioChem 7, 957-964. (Pubitemid 43938619)
    • (2006) ChemBioChem , vol.7 , Issue.6 , pp. 957-964
    • Grochowski, L.L.1    Zabriskie, T.M.2
  • 24
    • 0023879665 scopus 로고
    • Conformations of methyl 20-deoxy-alpha-d-ribofuranoside and methyl 20-deoxy-beta-d-ribofuranoside - A proton magnetic-resonance spectroscopy and molecular mechanics study
    • Raap, J., Vanboom, J. H., Vanlieshout, H. C., and Haasnoot, C. A. G. (1988) Conformations of Methyl 20-Deoxy-Alpha-D-Ribofuranoside and Methyl 20-Deoxy-Beta-D-Ribofuranoside - a Proton Magnetic- Resonance Spectroscopy and Molecular Mechanics Study. J. Am. Chem. Soc. 110, 2736-2743.
    • (1988) J. Am. Chem. Soc , vol.110 , pp. 2736-2743
    • Raap, J.1    Vanboom, J.H.2    Vanlieshout, H.C.3    Haasnoot, C.A.G.4
  • 25
    • 0346319022 scopus 로고    scopus 로고
    • Detailed kinetic analysis and identification of the nucleophile in α-L-arabinofuranosidase from Geobacillus stearothermophilus T-6, a family 51 glycoside hydrolase
    • DOI 10.1074/jbc.M208285200
    • Shallom, D., Belakhov, V., Solomon, D., Shoham, G., Baasov, T., and Shoham, Y. (2002) Detailed kinetic analysis and identification of the nucleophile in alpha-L-arabinofuranosidase from Geobacillus stearothermophilus T-6, a family 51 glycoside hydrolase. J. Biol. Chem. 277, 43667-43673. (Pubitemid 36157782)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.46 , pp. 43667-43673
    • Shallom, D.1    Belakhov, V.2    Solomon, D.3    Shoham, G.4    Baasov, T.5    Shoham, Y.6
  • 26
    • 0028609166 scopus 로고
    • Mechanisms of enzymatic glycoside hydrolysis
    • McCarter, J. D., and Withers, S. G. (1994) Mechanisms of enzymatic glycoside hydrolysis. Curr. Opin. Struct. Biol. 4, 885-892.
    • (1994) Curr. Opin. Struct. Biol , vol.4 , pp. 885-892
    • McCarter, J.D.1    Withers, S.G.2
  • 27
    • 42449116132 scopus 로고    scopus 로고
    • Mechanism for controlling the dimer-monomer switch and coupling dimerization to catalysis of the severe acute respiratory syndrome coronavirus 3C-like protease
    • DOI 10.1128/JVI.02680-07
    • Shi, J., Sivaraman, J., and Song, J. (2008) Mechanism for controlling the dimer-monomer switch and coupling dimerization to catalysis of the severe acute respiratory syndrome coronavirus 3C-like protease. J. Virol. 82, 4620-4629. (Pubitemid 351563698)
    • (2008) Journal of Virology , vol.82 , Issue.9 , pp. 4620-4629
    • Shi, J.1    Sivaraman, J.2    Song, J.3
  • 28
    • 0030602181 scopus 로고    scopus 로고
    • Stereochemical course of hydrolysis catalyzed by arabinofuranosyl hydrolases
    • DOI 10.1016/S0014-5793(96)01153-2, PII S0014579396011532
    • Pitson, S. M., Voragen, A. G., and Beldman, G. (1996) Stereochemical course of hydrolysis catalyzed by arabinofuranosyl hydrolases. FEBS Lett. 398, 7-11. (Pubitemid 26400333)
    • (1996) FEBS Letters , vol.398 , Issue.1 , pp. 7-11
    • Pitson, S.M.1    Voragen, A.G.J.2    Beldman, G.3
  • 29
    • 34250326342 scopus 로고    scopus 로고
    • Structure-based design, synthesis, evaluation, and crystal structures of transition state analogue inhibitors of inosine monophosphate cyclohydrolase
    • DOI 10.1074/jbc.M607293200
    • Xu, L., Chong, Y., Hwang, I., D'Onofrio, A., Amore, K., Beardsley, G. P., Li, C., Olson, A. J., Boger, D. L., and Wilson, I. A. (2007) Structure-based design, synthesis, evaluation, and crystal structures of transition state analogue inhibitors of inosine monophosphate cyclohydrolase. J. Biol. Chem. 282, 13033-13046. (Pubitemid 47100603)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.17 , pp. 13033-13046
    • Xu, L.1    Chong, Y.2    Hwang, I.3    D'Onofrio, A.4    Amore, K.5    Beardsley, G.P.6    Li, C.7    Olson, A.J.8    Boger, D.L.9    Wilson, I.A.10
  • 30
    • 0842348744 scopus 로고    scopus 로고
    • Catalytic Mechanism of the Cyclohydrolase Activity of Human Aminoimidazole Carboxamide Ribonucleotide Formyltransferase/Inosine Monophosphate Cyclohydrolase
    • DOI 10.1021/bi035139b
    • Vergis, J. M., and Beardsley, G. P. (2004) Catalytic mechanism of the cyclohydrolase activity of human aminoimidazole carboxamide ribonucleotide formyltransferase/inosine monophosphate cyclohydrolase. Biochemistry 43, 1184-1192. (Pubitemid 38176516)
    • (2004) Biochemistry , vol.43 , Issue.5 , pp. 1184-1192
    • Vergis, J.M.1    Beardsley, G.P.2
  • 31
    • 0037151063 scopus 로고    scopus 로고
    • The kinetic mechanism of the human bifunctional enzyme ATIC (5-amino-4-imidazolecarboxamide ribonucleotide transformylase/inosine 5′-monophosphate cyclohydrolase). A surprising lack of substrate channeling
    • DOI 10.1074/jbc.M111964200
    • Bulock, K. G., Beardsley, G. P., and Anderson, K. S. (2002) The kinetic mechanism of the human bifunctional enzyme ATIC (5-amino- 4-imidazolecarboxamide ribonucleotide transformylase/inosine 50- monophosphate cyclohydrolase). A surprising lack of substrate channeling. J. Biol. Chem. 277, 22168-22174. (Pubitemid 34967181)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.25 , pp. 22168-22174
    • Bulock, K.G.1    Peter Beardsley, G.2    Anderson, K.S.3
  • 32
    • 33750456519 scopus 로고    scopus 로고
    • Global, In Vivo, and Site-Specific Phosphorylation Dynamics in Signaling Networks
    • DOI 10.1016/j.cell.2006.09.026, PII S0092867406012748
    • Olsen, J. V., Blagoev, B., Gnad, F., Macek, B., Kumar, C., Mortensen, P., and Mann, M. (2006) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. Cell 127, 635-648. (Pubitemid 44647421)
    • (2006) Cell , vol.127 , Issue.3 , pp. 635-648
    • Olsen, J.V.1    Blagoev, B.2    Gnad, F.3    Macek, B.4    Kumar, C.5    Mortensen, P.6    Mann, M.7


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