메뉴 건너뛰기




Volumn 376, Issue 2, 2008, Pages 554-569

Mechanism of dTTP Inhibition of the Bifunctional dCTP Deaminase:dUTPase Encoded by Mycobacterium tuberculosis

Author keywords

catalytic mechnism; deamination; deoxy ribonucleotide metabolism; dUTP; enzyme regulation

Indexed keywords

DEOXYCYTIDINE TRIPHOSPHATE; DEOXYURIDINE TRIPHOSPHATE DERIVATIVE; DEOXYURIDINE TRIPHOSPHATE PYROPHOSPHATASE; THYMIDINE TRIPHOSPHATE;

EID: 38349191358     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.11.099     Document Type: Article
Times cited : (31)

References (40)
  • 1
    • 0027177564 scopus 로고
    • From RNA to DNA, why so many ribonucleotide reductases?
    • Reichard P. From RNA to DNA, why so many ribonucleotide reductases?. Science 260 (1993) 1773-1777
    • (1993) Science , vol.260 , pp. 1773-1777
    • Reichard, P.1
  • 3
    • 0020577509 scopus 로고
    • Mechanism of ribonucleoside diphosphate reductase from Escherichia coli. Evidence for 3′-C-H bond cleavage
    • Stubbe J., Ator M., and Krenitsky T. Mechanism of ribonucleoside diphosphate reductase from Escherichia coli. Evidence for 3′-C-H bond cleavage. J. Biol. Chem. 258 (1983) 1625-1631
    • (1983) J. Biol. Chem. , vol.258 , pp. 1625-1631
    • Stubbe, J.1    Ator, M.2    Krenitsky, T.3
  • 4
    • 0014010709 scopus 로고
    • Enzymatic synthesis of deoxyribonucleotides. X. Reduction of purine ribonucleotides; allosteric behavior and substrate specificity of the enzyme system from Escherichia coli B
    • Larsson A., and Reichard P. Enzymatic synthesis of deoxyribonucleotides. X. Reduction of purine ribonucleotides; allosteric behavior and substrate specificity of the enzyme system from Escherichia coli B. J. Biol. Chem. 241 (1966) 2540-2549
    • (1966) J. Biol. Chem. , vol.241 , pp. 2540-2549
    • Larsson, A.1    Reichard, P.2
  • 5
    • 0014010713 scopus 로고
    • Enzymatic synthesis of deoxyribonucleotides. IX. Allosteric effects in the reduction of pyrimidine ribonucleotides by the ribonucleoside diphosphate reductase system of Escherichia coli
    • Larsson A., and Reichard P. Enzymatic synthesis of deoxyribonucleotides. IX. Allosteric effects in the reduction of pyrimidine ribonucleotides by the ribonucleoside diphosphate reductase system of Escherichia coli. J. Biol. Chem. 241 (1966) 2533-2539
    • (1966) J. Biol. Chem. , vol.241 , pp. 2533-2539
    • Larsson, A.1    Reichard, P.2
  • 7
    • 0019522434 scopus 로고
    • Mutator phenotypes in mammalian cell mutants with distinct biochemical defects and abnormal deoxyribonucleoside triphosphate pools
    • Weinberg G., Ullman B., and Martin Jr. D.W. Mutator phenotypes in mammalian cell mutants with distinct biochemical defects and abnormal deoxyribonucleoside triphosphate pools. Proc. Natl Acad. Sci. USA 78 (1981) 2447-2451
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 2447-2451
    • Weinberg, G.1    Ullman, B.2    Martin Jr., D.W.3
  • 8
    • 33746539166 scopus 로고    scopus 로고
    • DNA precursor metabolism and genomic stability
    • Mathews C.K. DNA precursor metabolism and genomic stability. FASEB J. 20 (2006) 1300-1314
    • (2006) FASEB J. , vol.20 , pp. 1300-1314
    • Mathews, C.K.1
  • 10
    • 0017888335 scopus 로고
    • Deoxycytidylate deaminase from Bacillus subtilis. Purification, characterization, and physiological function
    • Mollgaard H., and Neuhard J. Deoxycytidylate deaminase from Bacillus subtilis. Purification, characterization, and physiological function. J. Biol. Chem. 253 (1978) 3536-3542
    • (1978) J. Biol. Chem. , vol.253 , pp. 3536-3542
    • Mollgaard, H.1    Neuhard, J.2
  • 11
    • 0015014216 scopus 로고
    • Deoxycytidine triphosphate deaminase: identification and function in Salmonella typhimurium
    • Neuhard J., and Thomassen E. Deoxycytidine triphosphate deaminase: identification and function in Salmonella typhimurium. J. Bacteriol. 105 (1971) 657-665
    • (1971) J. Bacteriol. , vol.105 , pp. 657-665
    • Neuhard, J.1    Thomassen, E.2
  • 12
    • 0023487248 scopus 로고
    • Regulation of pyrimidine deoxyribonucleotide metabolism by substrate cycles in dCMP deaminase-deficient V79 hamster cells
    • Bianchi V., Pontis E., and Reichard P. Regulation of pyrimidine deoxyribonucleotide metabolism by substrate cycles in dCMP deaminase-deficient V79 hamster cells. Mol. Cell. Biol. 7 (1987) 4218-4224
    • (1987) Mol. Cell. Biol. , vol.7 , pp. 4218-4224
    • Bianchi, V.1    Pontis, E.2    Reichard, P.3
  • 13
    • 0023967987 scopus 로고
    • Lethality of a dut (deoxyuridine triphosphatase) mutation in Escherichia coli
    • el-Hajj H.H., Zhang H., and Weiss B. Lethality of a dut (deoxyuridine triphosphatase) mutation in Escherichia coli. J. Bacteriol. 170 (1988) 1069-1075
    • (1988) J. Bacteriol. , vol.170 , pp. 1069-1075
    • el-Hajj, H.H.1    Zhang, H.2    Weiss, B.3
  • 14
    • 7244249940 scopus 로고    scopus 로고
    • Three-dimensional structure of the R115E mutant of T4-bacteriophage 2′-deoxycytidylate deaminase
    • Almog R., Maley F., Maley G.F., Maccoll R., and Van Roey P. Three-dimensional structure of the R115E mutant of T4-bacteriophage 2′-deoxycytidylate deaminase. Biochemistry 43 (2004) 13715-13723
    • (2004) Biochemistry , vol.43 , pp. 13715-13723
    • Almog, R.1    Maley, F.2    Maley, G.F.3    Maccoll, R.4    Van Roey, P.5
  • 15
    • 13244253956 scopus 로고    scopus 로고
    • Structures of dCTP deaminase from Escherichia coli with bound substrate and product: reaction mechanism and determinants of mono- and bifunctionality for a family of enzymes
    • Johansson E., Fano M., Bynck J.H., Neuhard J., Larsen S., Sigurskjold B.W., et al. Structures of dCTP deaminase from Escherichia coli with bound substrate and product: reaction mechanism and determinants of mono- and bifunctionality for a family of enzymes. J. Biol. Chem. 280 (2005) 3051-3059
    • (2005) J. Biol. Chem. , vol.280 , pp. 3051-3059
    • Johansson, E.1    Fano, M.2    Bynck, J.H.3    Neuhard, J.4    Larsen, S.5    Sigurskjold, B.W.6
  • 16
    • 17744410903 scopus 로고    scopus 로고
    • A bifunctional dCTP deaminase-dUTP nucleotidohydrolase from the hyperthermophilic archaeon Methanocaldococcus jannaschii
    • Bjornberg O., Neuhard J., and Nyman P.O. A bifunctional dCTP deaminase-dUTP nucleotidohydrolase from the hyperthermophilic archaeon Methanocaldococcus jannaschii. J. Biol. Chem. 278 (2003) 20667-20672
    • (2003) J. Biol. Chem. , vol.278 , pp. 20667-20672
    • Bjornberg, O.1    Neuhard, J.2    Nyman, P.O.3
  • 17
    • 0037837811 scopus 로고    scopus 로고
    • The Methanococcus jannaschii dCTP deaminase is a bifunctional deaminase and diphosphatase
    • Li H., Xu H., Graham D.E., and White R.H. The Methanococcus jannaschii dCTP deaminase is a bifunctional deaminase and diphosphatase. J. Biol. Chem. 278 (2003) 11100-11106
    • (2003) J. Biol. Chem. , vol.278 , pp. 11100-11106
    • Li, H.1    Xu, H.2    Graham, D.E.3    White, R.H.4
  • 18
    • 0016658298 scopus 로고
    • Deoxycytidine triphosphate deaminase of Salmonella typhimurium. Purification and characterization
    • Beck C.F., Eisenhardt A.R., and Neuhard J. Deoxycytidine triphosphate deaminase of Salmonella typhimurium. Purification and characterization. J. Biol. Chem. 250 (1975) 609-616
    • (1975) J. Biol. Chem. , vol.250 , pp. 609-616
    • Beck, C.F.1    Eisenhardt, A.R.2    Neuhard, J.3
  • 19
    • 34547743104 scopus 로고    scopus 로고
    • Regulation of dCTP deaminase from Escherichia coli by nonallosteric dTTP binding to an inactive form of the enzyme
    • Johansson E., Thymark M., Bynck J.H., Fano M., Larsen S., and Willemoes M. Regulation of dCTP deaminase from Escherichia coli by nonallosteric dTTP binding to an inactive form of the enzyme. FEBS J. 274 (2007) 4188-4198
    • (2007) FEBS J. , vol.274 , pp. 4188-4198
    • Johansson, E.1    Thymark, M.2    Bynck, J.H.3    Fano, M.4    Larsen, S.5    Willemoes, M.6
  • 20
    • 0034744964 scopus 로고    scopus 로고
    • Homotrimeric dUTPases; structural solutions for specific recognition and hydrolysis of dUTP
    • Persson R., Cedergren-Zeppezauer E.S., and Wilson K.S. Homotrimeric dUTPases; structural solutions for specific recognition and hydrolysis of dUTP. Curr. Protein Pept. Sci. 2 (2001) 287-300
    • (2001) Curr. Protein Pept. Sci. , vol.2 , pp. 287-300
    • Persson, R.1    Cedergren-Zeppezauer, E.S.2    Wilson, K.S.3
  • 21
    • 0031559946 scopus 로고    scopus 로고
    • dUTPase from the retrovirus equine infectious anemia virus: specificity, turnover and inhibition
    • Nord J., Larsson G., Kvassman J.O., Rosengren A.M., and Nyman P.O. dUTPase from the retrovirus equine infectious anemia virus: specificity, turnover and inhibition. FEBS Lett. 414 (1997) 271-274
    • (1997) FEBS Lett. , vol.414 , pp. 271-274
    • Nord, J.1    Larsson, G.2    Kvassman, J.O.3    Rosengren, A.M.4    Nyman, P.O.5
  • 23
    • 0042847344 scopus 로고    scopus 로고
    • Structure of the bifunctional dCTP deaminase-dUTPase from Methanocaldococcus jannaschii and its relation to other homotrimeric dUTPases
    • Johansson E., Bjornberg O., Nyman P.O., and Larsen S. Structure of the bifunctional dCTP deaminase-dUTPase from Methanocaldococcus jannaschii and its relation to other homotrimeric dUTPases. J. Biol. Chem. 278 (2003) 27916-27922
    • (2003) J. Biol. Chem. , vol.278 , pp. 27916-27922
    • Johansson, E.1    Bjornberg, O.2    Nyman, P.O.3    Larsen, S.4
  • 24
    • 3342875968 scopus 로고    scopus 로고
    • Crystal structure of the Mycobacterium tuberculosis dUTPase: insights into the catalytic mechanism
    • Chan S., Segelke B., Lekin T., Krupka H., Cho U.S., Kim M.Y., et al. Crystal structure of the Mycobacterium tuberculosis dUTPase: insights into the catalytic mechanism. J. Mol. Biol. 341 (2004) 503-517
    • (2004) J. Mol. Biol. , vol.341 , pp. 503-517
    • Chan, S.1    Segelke, B.2    Lekin, T.3    Krupka, H.4    Cho, U.S.5    Kim, M.Y.6
  • 25
    • 5644258283 scopus 로고    scopus 로고
    • Structural insights into the catalytic mechanism of phosphate ester hydrolysis by dUTPase
    • Barabas O., Pongracz V., Kovari J., Wilmanns M., and Vertessy B.G. Structural insights into the catalytic mechanism of phosphate ester hydrolysis by dUTPase. J. Biol. Chem. 279 (2004) 42907-42915
    • (2004) J. Biol. Chem. , vol.279 , pp. 42907-42915
    • Barabas, O.1    Pongracz, V.2    Kovari, J.3    Wilmanns, M.4    Vertessy, B.G.5
  • 26
    • 0030587564 scopus 로고    scopus 로고
    • Human dUTP pyrophosphatase: uracil recognition by a beta hairpin and active sites formed by three separate subunits
    • Mol C.D., Harris J.M., McIntosh E.M., and Tainer J.A. Human dUTP pyrophosphatase: uracil recognition by a beta hairpin and active sites formed by three separate subunits. Structure 4 (1996) 1077-1092
    • (1996) Structure , vol.4 , pp. 1077-1092
    • Mol, C.D.1    Harris, J.M.2    McIntosh, E.M.3    Tainer, J.A.4
  • 27
    • 0033555756 scopus 로고    scopus 로고
    • Crystal structure of dUTPase from equine infectious anaemia virus; active site metal binding in a substrate analogue complex
    • Dauter Z., Persson R., Rosengren A.M., Nyman P.O., Wilson K.S., and Cedergren-Zeppezauer E.S. Crystal structure of dUTPase from equine infectious anaemia virus; active site metal binding in a substrate analogue complex. J. Mol. Biol. 285 (1999) 655-673
    • (1999) J. Mol. Biol. , vol.285 , pp. 655-673
    • Dauter, Z.1    Persson, R.2    Rosengren, A.M.3    Nyman, P.O.4    Wilson, K.S.5    Cedergren-Zeppezauer, E.S.6
  • 28
    • 0033831995 scopus 로고    scopus 로고
    • Structures of feline immunodeficiency virus dUTP pyrophosphatase and its nucleotide complexes in three crystal forms
    • Prasad G.S., Stura E.A., Elder J.H., and Stout C.D. Structures of feline immunodeficiency virus dUTP pyrophosphatase and its nucleotide complexes in three crystal forms. Acta Crystallogr., Sect. D: Biol. Crystallogr. 56 (2000) 1100-1109
    • (2000) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.56 , pp. 1100-1109
    • Prasad, G.S.1    Stura, E.A.2    Elder, J.H.3    Stout, C.D.4
  • 30
    • 13844296398 scopus 로고    scopus 로고
    • dUTPase as a platform for antimalarial drug design: structural basis for the selectivity of a class of nucleoside inhibitors
    • Whittingham J.L., Leal I., Nguyen C., Kasinathan G., Bell E., Jones A.F., et al. dUTPase as a platform for antimalarial drug design: structural basis for the selectivity of a class of nucleoside inhibitors. Structure 13 (2005) 329-338
    • (2005) Structure , vol.13 , pp. 329-338
    • Whittingham, J.L.1    Leal, I.2    Nguyen, C.3    Kasinathan, G.4    Bell, E.5    Jones, A.F.6
  • 31
    • 0035216762 scopus 로고    scopus 로고
    • Evolution of the DUT gene: horizontal transfer between host and pathogen in all three domains of life
    • McClure M.A. Evolution of the DUT gene: horizontal transfer between host and pathogen in all three domains of life. Curr. Protein Pept. Sci. 2 (2001) 313-324
    • (2001) Curr. Protein Pept. Sci. , vol.2 , pp. 313-324
    • McClure, M.A.1
  • 32
    • 0026769810 scopus 로고
    • Structure and function of a 40,000-molecular-weight protein antigen of Mycobacterium tuberculosis
    • Andersen A.B., Andersen P., and Ljungqvist L. Structure and function of a 40,000-molecular-weight protein antigen of Mycobacterium tuberculosis. Infect. Immun. 60 (1992) 2317-2323
    • (1992) Infect. Immun. , vol.60 , pp. 2317-2323
    • Andersen, A.B.1    Andersen, P.2    Ljungqvist, L.3
  • 33
    • 0014217178 scopus 로고
    • Cytidine triphosphate synthetase of Escherichia coli B. I. Purification and kinetics
    • Long C.W., and Pardee A.B. Cytidine triphosphate synthetase of Escherichia coli B. I. Purification and kinetics. J. Biol. Chem. 242 (1967) 4715-4721
    • (1967) J. Biol. Chem. , vol.242 , pp. 4715-4721
    • Long, C.W.1    Pardee, A.B.2
  • 34
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26 (1993) 795-800
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 35
    • 0000560808 scopus 로고    scopus 로고
    • MOLREP: an automated program for molecular replacement
    • Vagin A., and Teplyakov A. MOLREP: an automated program for molecular replacement. J. Appl. Crystallogr. 30 (1997) 1022-1025
    • (1997) J. Appl. Crystallogr. , vol.30 , pp. 1022-1025
    • Vagin, A.1    Teplyakov, A.2
  • 36
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • CCP4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr., Sect. D: Biol. Crystallogr. 50 (1994) 760-763
    • (1994) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.50 , pp. 760-763
    • CCP41
  • 38
    • 0032964481 scopus 로고    scopus 로고
    • Automated protein model building combined with iterative structure refinement
    • Perrakis A., Morris R., and Lamzin V.S. Automated protein model building combined with iterative structure refinement. Nat. Struct. Biol. 6 (1999) 458-463
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 458-463
    • Perrakis, A.1    Morris, R.2    Lamzin, V.S.3
  • 39
    • 0025398721 scopus 로고
    • What if-a molecular modeling and drug design program
    • Vriend G. What if-a molecular modeling and drug design program. J. Mol. Graphics 8 (1990) 52-&
    • (1990) J. Mol. Graphics , vol.8
    • Vriend, G.1
  • 40


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.