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Volumn 48, Issue 4, 2009, Pages 766-778

Dihydroorotase from the hyperthermophile Aquifiex aeolicus is activated by stoichiometric association with aspartate transcarbamoylase and forms a one-pot reactor for pyrimidine biosynthesis

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITES; AQUIFEX AEOLICUS; ASPARTATE; CARBAMOYL ASPARTATE; CARBAMOYL PHOSPHATES; CYTOSOL; DIHYDROOROTASE; DODECAMER; HEXAMER; HYPERTHERMOPHILE; ISOSTERIC; MULTIENZYME COMPLEXES; MULTIFUNCTIONAL COMPLEXES; NONCOVALENT; ONE POTS; PEPTIDE BONDS; POLYPEPTIDE CHAINS; PYRIMIDINE BIOSYNTHESIS; REACTION CHAMBERS; SYNTHETASE; THREE-DIMENSIONAL STRUCTURES; ZINC ATOMS;

EID: 60749123877     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi801831r     Document Type: Article
Times cited : (35)

References (59)
  • 1
    • 4043064372 scopus 로고    scopus 로고
    • Mammalian pyrimidine biosynthesis: Fresh insights into an ancient pathway
    • Evans, D. R., and Guy, H. I. (2004) Mammalian pyrimidine biosynthesis: fresh insights into an ancient pathway. J. Biol. Chem. 279, 33035-33038.
    • (2004) J. Biol. Chem , vol.279 , pp. 33035-33038
    • Evans, D.R.1    Guy, H.I.2
  • 2
    • 0019321917 scopus 로고
    • The overall synthesis of L-5,6-dihydroorotate by multienzymatic protein pyr1-3 from hamster cells. Kinetic studies, substrate channeling, and the effects of inhibitors
    • Christopherson, R. I., and Jones, M. E. (1980) The overall synthesis of L-5,6-dihydroorotate by multienzymatic protein pyr1-3 from hamster cells. Kinetic studies, substrate channeling, and the effects of inhibitors. J. Biol. Chem. 255, 11381-11395.
    • (1980) J. Biol. Chem , vol.255 , pp. 11381-11395
    • Christopherson, R.I.1    Jones, M.E.2
  • 3
    • 0030751062 scopus 로고    scopus 로고
    • A reciprocal allosteric mechanism for efficient transfer of labile intermediates between active sites in CAD, the mammalian pyrimidine-biosynthetic multienzyme polypeptide
    • Irvine, H. S., Shaw, S. M., Paton, A., and Carrey, E. A. (1997) A reciprocal allosteric mechanism for efficient transfer of labile intermediates between active sites in CAD, the mammalian pyrimidine-biosynthetic multienzyme polypeptide. Eur. J. Biochem. 247, 1063-1073.
    • (1997) Eur. J. Biochem , vol.247 , pp. 1063-1073
    • Irvine, H.S.1    Shaw, S.M.2    Paton, A.3    Carrey, E.A.4
  • 4
    • 0019321916 scopus 로고
    • Catalytic synergy in the multifunctional protein that initiates pyrimidine biosynthesis in Syrian hamster cells
    • Mally, M. I., Grayson, D. R., and Evans, D. R. (1980) Catalytic synergy in the multifunctional protein that initiates pyrimidine biosynthesis in Syrian hamster cells. J. Biol. Chem. 255, 11372-11380.
    • (1980) J. Biol. Chem , vol.255 , pp. 11372-11380
    • Mally, M.I.1    Grayson, D.R.2    Evans, D.R.3
  • 5
    • 0347993053 scopus 로고    scopus 로고
    • Aquifex aeolicus aspartate transcarbamoylase, an enzyme specialized for the efficient utilization of unstable carbamoyl phosphate at elevated temperature
    • Purcarea, C., Ahuja, A., Lu, T., Kovari, L., Guy, H. I., and Evans, D. R. (2003) Aquifex aeolicus aspartate transcarbamoylase, an enzyme specialized for the efficient utilization of unstable carbamoyl phosphate at elevated temperature. J. Biol. Chem. 278, 52924-52934.
    • (2003) J. Biol. Chem , vol.278 , pp. 52924-52934
    • Purcarea, C.1    Ahuja, A.2    Lu, T.3    Kovari, L.4    Guy, H.I.5    Evans, D.R.6
  • 6
    • 11144231701 scopus 로고    scopus 로고
    • Aquifex aeolicus dihydroorotase: Association with aspartate transcarbamoylase switches on catalytic activity
    • Ahuja, A., Purcarea, C., Ebert, R., Guy, H., and Evans, D. (2004) Aquifex aeolicus dihydroorotase: Association with aspartate transcarbamoylase switches on catalytic activity. J. Biol. Chem. 279, 53136-53144.
    • (2004) J. Biol. Chem , vol.279 , pp. 53136-53144
    • Ahuja, A.1    Purcarea, C.2    Ebert, R.3    Guy, H.4    Evans, D.5
  • 7
    • 0014602890 scopus 로고
    • Molecular size and feedback-regulation characteristics of bacterial aspartate transcar-bamoylases
    • Bethell, M. R., and Jones, M. E. (1969) Molecular size and feedback-regulation characteristics of bacterial aspartate transcar-bamoylases. Arch. Biochem. Biophys. 134, 352-365.
    • (1969) Arch. Biochem. Biophys , vol.134 , pp. 352-365
    • Bethell, M.R.1    Jones, M.E.2
  • 8
    • 0032866568 scopus 로고    scopus 로고
    • Streptomyces aspartate transcarbamoylase is a dodecamer with dihydroorotase activity
    • Hughes, L. E., Hooshdaran, M. Z., and GA, O. D. (1999) Streptomyces aspartate transcarbamoylase is a dodecamer with dihydroorotase activity. Curr. Microbiol. 39, 175-179.
    • (1999) Curr. Microbiol , vol.39 , pp. 175-179
    • Hughes, L.E.1    Hooshdaran, M.Z.2    GA, O.D.3
  • 9
    • 0030922432 scopus 로고    scopus 로고
    • Structure and expression of a pyrimidine gene cluster from the extreme thermophile Thermus strain ZO5
    • Van de Casteele, M., Chen, P., Roovers, M., Legrain, C., and Glansdorff, N. (1997) Structure and expression of a pyrimidine gene cluster from the extreme thermophile Thermus strain ZO5. J. Bacteriol. 179, 3470-3481.
    • (1997) J. Bacteriol , vol.179 , pp. 3470-3481
    • Van de Casteele, M.1    Chen, P.2    Roovers, M.3    Legrain, C.4    Glansdorff, N.5
  • 10
    • 0037025369 scopus 로고    scopus 로고
    • Pseudomonas aeruginosa aspartate transcarbamoylase. Characterization of its catalytic and regulatory properties
    • Vickrey, J. F., Herve, G., and Evans, D. R. (2002) Pseudomonas aeruginosa aspartate transcarbamoylase. Characterization of its catalytic and regulatory properties. J. Biol. Chem. 277, 24490-24498.
    • (2002) J. Biol. Chem , vol.277 , pp. 24490-24498
    • Vickrey, J.F.1    Herve, G.2    Evans, D.R.3
  • 11
    • 0014426672 scopus 로고
    • Crystallographic determination of symmetry of aspartate transcarbamylase
    • Wiley, D. C., and Lipscomb, W. N. (1968) Crystallographic determination of symmetry of aspartate transcarbamylase. Nature 218, 1119-1121.
    • (1968) Nature , vol.218 , pp. 1119-1121
    • Wiley, D.C.1    Lipscomb, W.N.2
  • 12
    • 0022272510 scopus 로고
    • Aspartate transcarbamylase from Bacillus subtilis
    • Brabson, J. S., Maurizi, M. R., and Switzer, R. L. (1985) Aspartate transcarbamylase from Bacillus subtilis. Methods Enzymol. 113, 627-635.
    • (1985) Methods Enzymol , vol.113 , pp. 627-635
    • Brabson, J.S.1    Maurizi, M.R.2    Switzer, R.L.3
  • 13
    • 0025058563 scopus 로고
    • Escherichia coli aspartate transcarbamoylase: The molecular basis for a concerted allosteric transition
    • Kantrowitz, E. R., and Lipscomb, W. N. (1990) Escherichia coli aspartate transcarbamoylase: the molecular basis for a concerted allosteric transition. Trends Biochem. Sci. 15, 53-59.
    • (1990) Trends Biochem. Sci , vol.15 , pp. 53-59
    • Kantrowitz, E.R.1    Lipscomb, W.N.2
  • 14
    • 0022429817 scopus 로고
    • Structure-function relationship in allosteric aspartate carbamoyltransferase from Escherichia coli. II. Involvement of the C-terminal region of the regulatory chain in homotropic and heterotropic interactions
    • Ladjimi, M. M., Ghellis, C., Feller, A., Cunin, R., Glansdorff, N., Pierard, A., and Herve, G. (1985) Structure-function relationship in allosteric aspartate carbamoyltransferase from Escherichia coli. II. Involvement of the C-terminal region of the regulatory chain in homotropic and heterotropic interactions. J. Mol. Biol. 186, 715-724.
    • (1985) J. Mol. Biol , vol.186 , pp. 715-724
    • Ladjimi, M.M.1    Ghellis, C.2    Feller, A.3    Cunin, R.4    Glansdorff, N.5    Pierard, A.6    Herve, G.7
  • 15
    • 0005552966 scopus 로고
    • In the presence of CTP, UTP becomes an allosteric inhibitor of aspartate transcarbamoylase
    • Wild, J. R., Loughrey-Chen, S. J., and Corder, T. S. (1989) In the presence of CTP, UTP becomes an allosteric inhibitor of aspartate transcarbamoylase. Proc. Natl. Acad. Sci. U.S.A. 86, 46-50.
    • (1989) Proc. Natl. Acad. Sci. U.S.A , vol.86 , pp. 46-50
    • Wild, J.R.1    Loughrey-Chen, S.J.2    Corder, T.S.3
  • 16
    • 33847797256 scopus 로고    scopus 로고
    • Thermodynamics-based metabolic flux analysis
    • Henry, C. S., Broadbelt, L. J., and Hatzimanikatis, V. (2007) Thermodynamics-based metabolic flux analysis. Biophys. J. 92, 1792-1805.
    • (2007) Biophys. J , vol.92 , pp. 1792-1805
    • Henry, C.S.1    Broadbelt, L.J.2    Hatzimanikatis, V.3
  • 17
    • 0002158478 scopus 로고    scopus 로고
    • Phylogenetic analysis and classification of dihydroorotases: A complex history for a complex enzyme
    • Fields, C., Brichta, D., Shephardson, M., Farinha, M., and O'Donovan, G. (1999) Phylogenetic analysis and classification of dihydroorotases: a complex history for a complex enzyme. Paths Pyrimidines 7, 49-63.
    • (1999) Paths Pyrimidines , vol.7 , pp. 49-63
    • Fields, C.1    Brichta, D.2    Shephardson, M.3    Farinha, M.4    O'Donovan, G.5
  • 18
    • 17844384785 scopus 로고    scopus 로고
    • Structural and catalytic diversity within the amidohydrolase superfamily
    • Seibert, C. M., and Raushel, F. M. (2005) Structural and catalytic diversity within the amidohydrolase superfamily. Biochemistry 44, 6383-6391.
    • (2005) Biochemistry , vol.44 , pp. 6383-6391
    • Seibert, C.M.1    Raushel, F.M.2
  • 19
    • 11144301188 scopus 로고    scopus 로고
    • Mechanism of the dihydroorotase reaction
    • Porter, T. N., Li, Y., and Raushel, F. M. (2004) Mechanism of the dihydroorotase reaction. Biochemistry 43, 16285-16292.
    • (2004) Biochemistry , vol.43 , pp. 16285-16292
    • Porter, T.N.1    Li, Y.2    Raushel, F.M.3
  • 20
    • 17144372272 scopus 로고    scopus 로고
    • Dihydroorotase from Escherichia coli: Loop movement and cooperativity between subunits
    • Lee, M., Chan, C. W., Mitchell Guss, J., Christopherson, R. I., and Maher, M. J. (2005) Dihydroorotase from Escherichia coli: loop movement and cooperativity between subunits. J. Mol. Biol. 348, 523-533.
    • (2005) J. Mol. Biol , vol.348 , pp. 523-533
    • Lee, M.1    Chan, C.W.2    Mitchell Guss, J.3    Christopherson, R.I.4    Maher, M.J.5
  • 21
    • 0035912842 scopus 로고    scopus 로고
    • Molecular structure of dihydroorotase: A paradigm for catalysis through the use of a binuclear metal center
    • Thoden, J. B., Phillips, G. N., Jr., Neal, T. M., Raushel, F. M., and Holden, H. M. (2001) Molecular structure of dihydroorotase: a paradigm for catalysis through the use of a binuclear metal center. Biochemistry 40, 6989-6997.
    • (2001) Biochemistry , vol.40 , pp. 6989-6997
    • Thoden, J.B.1    Phillips Jr., G.N.2    Neal, T.M.3    Raushel, F.M.4    Holden, H.M.5
  • 23
    • 0035788131 scopus 로고    scopus 로고
    • Spherically averaged phased translation function and its application to the search for molecules and fragments in electron-density maps
    • Vagin, A. A., and Isupov, M. N. (2001) Spherically averaged phased translation function and its application to the search for molecules and fragments in electron-density maps. Acta Crystallogr., Sect. D: Biol. Crystallogr. 57, 1451-1456.
    • (2001) Acta Crystallogr., Sect. D: Biol. Crystallogr , vol.57 , pp. 1451-1456
    • Vagin, A.A.1    Isupov, M.N.2
  • 25
    • 0037208360 scopus 로고    scopus 로고
    • An overview of the CCP4 project in protein crystallography: An example of a collaborative project
    • Winn, M. D. (2003) An overview of the CCP4 project in protein crystallography: an example of a collaborative project. J. Synchrotron Radiat. 10, 23-25.
    • (2003) J. Synchrotron Radiat , vol.10 , pp. 23-25
    • Winn, M.D.1
  • 28
    • 33847142225 scopus 로고    scopus 로고
    • CAVER: A new tool to explore routes from protein clefts, pockets and cavities
    • Petrek, M., Otyepka, M., Banas, P., Kosinova, P., Koca, J., and Damborsky, J. (2006) CAVER: a new tool to explore routes from protein clefts, pockets and cavities. BMC Bioinf. 7, 316.
    • (2006) BMC Bioinf , vol.7 , pp. 316
    • Petrek, M.1    Otyepka, M.2    Banas, P.3    Kosinova, P.4    Koca, J.5    Damborsky, J.6
  • 29
  • 30
    • 23444454552 scopus 로고    scopus 로고
    • Case, D. A., Cheatham, T. E., III, Darden, T, Gohlke, H., Luo, R., Merz, K. M., Jr., Onufriev, A., Simmerling, C., Wang, B., and Woods, R. J. (2005) The Amber biomolecular simulation programs. J. Comput. Chem. 26, 1668-1688.
    • Case, D. A., Cheatham, T. E., III, Darden, T, Gohlke, H., Luo, R., Merz, K. M., Jr., Onufriev, A., Simmerling, C., Wang, B., and Woods, R. J. (2005) The Amber biomolecular simulation programs. J. Comput. Chem. 26, 1668-1688.
  • 33
    • 33847034125 scopus 로고    scopus 로고
    • Assignment of polar states for protein amino acid residues using an interaction cluster decomposition algorithm and its application to high resolution protein structure modeling
    • Li, X., Jacobson, M. P., Zhu, K., Zhao, S., and Friesner, R. A. (2007) Assignment of polar states for protein amino acid residues using an interaction cluster decomposition algorithm and its application to high resolution protein structure modeling. Proteins 66, 824-837.
    • (2007) Proteins , vol.66 , pp. 824-837
    • Li, X.1    Jacobson, M.P.2    Zhu, K.3    Zhao, S.4    Friesner, R.A.5
  • 34
    • 0032128272 scopus 로고    scopus 로고
    • Rfree and the Rfree ratio. I. Derivation of expected values of cross-validation residuals used in macromolecular least-squares refinement
    • Tickle, I. J., Laskowski, R. A., and Moss, D. S. (1998) Rfree and the Rfree ratio. I. Derivation of expected values of cross-validation residuals used in macromolecular least-squares refinement. Acta Crystallogr., Sect. D: Biol. Crystallogr. 54, 547-557.
    • (1998) Acta Crystallogr., Sect. D: Biol. Crystallogr , vol.54 , pp. 547-557
    • Tickle, I.J.1    Laskowski, R.A.2    Moss, D.S.3
  • 35
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E., and Henrick, K. (2007) Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774-797.
    • (2007) J. Mol. Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 37
    • 0035081156 scopus 로고    scopus 로고
    • Aspartate transcarbamoylase from Pyrococcus abyssi
    • Purcarea, C. (2001) Aspartate transcarbamoylase from Pyrococcus abyssi. Methods Enzymol. 331, 248-270.
    • (2001) Methods Enzymol , vol.331 , pp. 248-270
    • Purcarea, C.1
  • 39
    • 0242362161 scopus 로고    scopus 로고
    • Combining local-structure, fold-recognition, and new fold methods for protein structure prediction
    • Karplus, K., Karchin, R., Draper, J., Casper, J., Mandel-Gutfreund, Y., Diekhans, M., and Hughey, R. (2003) Combining local-structure, fold-recognition, and new fold methods for protein structure prediction. Proteins 53, 491-496.
    • (2003) Proteins , vol.53 , pp. 491-496
    • Karplus, K.1    Karchin, R.2    Draper, J.3    Casper, J.4    Mandel-Gutfreund, Y.5    Diekhans, M.6    Hughey, R.7
  • 40
    • 0023819640 scopus 로고
    • Escherichia coli aspartate transcarbamylase: The relation between structure and function
    • Kantrowitz, E. R., and Lipscomb, W. N. (1988) Escherichia coli aspartate transcarbamylase: the relation between structure and function. Science 241, 669-674.
    • (1988) Science , vol.241 , pp. 669-674
    • Kantrowitz, E.R.1    Lipscomb, W.N.2
  • 41
    • 0029072769 scopus 로고
    • Domain closure in the catalytic chains of Escherichia coli aspartate transcarbamoylase influences the kinetic mechanism
    • Lee, B. H., Ley, B. W., Kantrowitz, E. R., O'Leary, M. H., and Wedler, F. C. (1995) Domain closure in the catalytic chains of Escherichia coli aspartate transcarbamoylase influences the kinetic mechanism. J. Biol. Chem. 270, 15620-15627.
    • (1995) J. Biol. Chem , vol.270 , pp. 15620-15627
    • Lee, B.H.1    Ley, B.W.2    Kantrowitz, E.R.3    O'Leary, M.H.4    Wedler, F.C.5
  • 42
    • 0033545974 scopus 로고    scopus 로고
    • Assessment of the allosteric mechanism of aspartate transcarbamoylase based on the crystalline structure of the unregulated catalytic subunit
    • Beernink, P. T., Endrizzi, J. A., Alber, T., and Schachman, H. K. (1999) Assessment of the allosteric mechanism of aspartate transcarbamoylase based on the crystalline structure of the unregulated catalytic subunit. Proc. Natl. Acad. Sci. U.S.A. 96, 5388-5393.
    • (1999) Proc. Natl. Acad. Sci. U.S.A , vol.96 , pp. 5388-5393
    • Beernink, P.T.1    Endrizzi, J.A.2    Alber, T.3    Schachman, H.K.4
  • 43
    • 0032747749 scopus 로고    scopus 로고
    • Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1 Å
    • Jin, L., Stec, B., Lipscomb, W. N., and Kantrowitz, E. R. (1999) Insights into the mechanisms of catalysis and heterotropic regulation of Escherichia coli aspartate transcarbamoylase based upon a structure of the enzyme complexed with the bisubstrate analogue N-phosphonacetyl-L-aspartate at 2.1 Å. Proteins 37, 729-742.
    • (1999) Proteins , vol.37 , pp. 729-742
    • Jin, L.1    Stec, B.2    Lipscomb, W.N.3    Kantrowitz, E.R.4
  • 44
    • 20844448232 scopus 로고    scopus 로고
    • A comprehensive and non-redundant database of protein domain movements
    • Qi, G., Lee, R., and Hayward, S. (2005) A comprehensive and non-redundant database of protein domain movements. Bioinformatics 21, 2832-2838.
    • (2005) Bioinformatics , vol.21 , pp. 2832-2838
    • Qi, G.1    Lee, R.2    Hayward, S.3
  • 45
    • 45849108388 scopus 로고    scopus 로고
    • Biochemistry. How enzymes work
    • Ringe, D., and Petsko, G. A. (2008) Biochemistry. How enzymes work. Science 320, 1428-1429.
    • (2008) Science , vol.320 , pp. 1428-1429
    • Ringe, D.1    Petsko, G.A.2
  • 46
    • 0036072433 scopus 로고    scopus 로고
    • Detection and location of the enzymes of de novo pyrimidine biosynthesis in mammalian spermatozoa
    • Carrey, E. A., Dietz, C., Glubb, D. M., Loffler, M., Lucocq, J. M., and Watson, P. F. (2002) Detection and location of the enzymes of de novo pyrimidine biosynthesis in mammalian spermatozoa. Reproduction 123, 757-768.
    • (2002) Reproduction , vol.123 , pp. 757-768
    • Carrey, E.A.1    Dietz, C.2    Glubb, D.M.3    Loffler, M.4    Lucocq, J.M.5    Watson, P.F.6
  • 47
    • 34347368461 scopus 로고    scopus 로고
    • A more complete, complexed and structured interactome
    • Devos, D., and Russell, R. B. (2007) A more complete, complexed and structured interactome. Curr. Opin. Struct. Biol. 17, 370-377.
    • (2007) Curr. Opin. Struct. Biol , vol.17 , pp. 370-377
    • Devos, D.1    Russell, R.B.2
  • 48
    • 0031763106 scopus 로고    scopus 로고
    • Iron storage in bacteria
    • Andrews, S. C. (1998) Iron storage in bacteria. Adv. Microb. Physiol. 40, 281-351.
    • (1998) Adv. Microb. Physiol , vol.40 , pp. 281-351
    • Andrews, S.C.1
  • 49
    • 34247383568 scopus 로고    scopus 로고
    • Structure of fungal fatty acid synthase and implications for iterative substrate shuttling
    • Jenni, S., Leibundgut, M., Boehringer, D., Frick, C., Mikolasek, B., and Ban, N. (2007) Structure of fungal fatty acid synthase and implications for iterative substrate shuttling. Science 316, 254-261.
    • (2007) Science , vol.316 , pp. 254-261
    • Jenni, S.1    Leibundgut, M.2    Boehringer, D.3    Frick, C.4    Mikolasek, B.5    Ban, N.6
  • 50
    • 0346220392 scopus 로고    scopus 로고
    • Molecular shredders: How proteasomes fulfill their role
    • Groll, M., and Clausen, T. (2003) Molecular shredders: how proteasomes fulfill their role. Curr. Opin. Struct. Biol. 13, 665-673.
    • (2003) Curr. Opin. Struct. Biol , vol.13 , pp. 665-673
    • Groll, M.1    Clausen, T.2
  • 51
    • 0026510711 scopus 로고
    • Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex
    • Mattevi, A., Obmolova, G., Schulze, E., Kalk, K. H., Westphal, A. H., de Kok, A., and Hol, W. G. (1992) Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex. Science 255, 1544-1550.
    • (1992) Science , vol.255 , pp. 1544-1550
    • Mattevi, A.1    Obmolova, G.2    Schulze, E.3    Kalk, K.H.4    Westphal, A.H.5    de Kok, A.6    Hol, W.G.7
  • 52
    • 0031808808 scopus 로고    scopus 로고
    • Calculated electrostatic gradients in recombinant human H-chain ferritin
    • Douglas, T., and Ripoll, D. R. (1998) Calculated electrostatic gradients in recombinant human H-chain ferritin. Protein Sci. 7, 1083-1091.
    • (1998) Protein Sci , vol.7 , pp. 1083-1091
    • Douglas, T.1    Ripoll, D.R.2
  • 53
    • 0033573917 scopus 로고    scopus 로고
    • Izard, T., Aevarsson, A., Allen, M. D., Westphal, A. H., Perham, R. N., de Kok, A., and Hol, W. G (1999) Principles of quasi-equivalence and Euclidean geometry govern the assembly of cubic and dodecahedral cores of pyruvate dehydrogenase complexes Proc. Natl. Acad. Sci. U.S.A. 96, 1240-1245.
    • Izard, T., Aevarsson, A., Allen, M. D., Westphal, A. H., Perham, R. N., de Kok, A., and Hol, W. G (1999) Principles of quasi-equivalence and Euclidean geometry govern the assembly of cubic and dodecahedral cores of pyruvate dehydrogenase complexes Proc. Natl. Acad. Sci. U.S.A. 96, 1240-1245.
  • 54
    • 0033618555 scopus 로고    scopus 로고
    • Detecting protein function and protein-protein interactions from genome sequences
    • Marcotte, E. M., Pellegrini, M., Ng, H. L., Rice, D. W., Yeates, T. O., and Eisenberg, D. (1999) Detecting protein function and protein-protein interactions from genome sequences. Science 285, 751-753.
    • (1999) Science , vol.285 , pp. 751-753
    • Marcotte, E.M.1    Pellegrini, M.2    Ng, H.L.3    Rice, D.W.4    Yeates, T.O.5    Eisenberg, D.6
  • 55
    • 0033621536 scopus 로고    scopus 로고
    • Genome evolution. Gene fusion versus gene fission
    • Snel, B., Bork, P., and Huynen, M. (2000) Genome evolution. Gene fusion versus gene fission. Trends Genet. 16, 9-11.
    • (2000) Trends Genet , vol.16 , pp. 9-11
    • Snel, B.1    Bork, P.2    Huynen, M.3
  • 56
    • 1842841205 scopus 로고
    • Oligomeric structure of the multifunctional protein CAD that initiates pyrimidine biosynthesis in mammalian cells
    • Lee, L., Kelly, R. E., Pastra-Landis, S. C., and Evans, D. R. (1985) Oligomeric structure of the multifunctional protein CAD that initiates pyrimidine biosynthesis in mammalian cells. Proc. Natl. Acad. Sci. U.S.A. 82, 6802-6806.
    • (1985) Proc. Natl. Acad. Sci. U.S.A , vol.82 , pp. 6802-6806
    • Lee, L.1    Kelly, R.E.2    Pastra-Landis, S.C.3    Evans, D.R.4
  • 57
    • 0016769310 scopus 로고
    • Reversible dissociation of a carbamoyl phosphate synthase-aspartate transcarbamoylase-dihydroorotase complex from ovarian eggs of Rana catesbeiana: Effect of uridine triphosphate and other modifiers
    • Kent, R. J., Lin, R. L., Sallach, H. J., and Cohen, P. P. (1975) Reversible dissociation of a carbamoyl phosphate synthase-aspartate transcarbamoylase-dihydroorotase complex from ovarian eggs of Rana catesbeiana: effect of uridine triphosphate and other modifiers. Proc. Natl. Acad. Sci. U.S.A. 72, 1712-1716.
    • (1975) Proc. Natl. Acad. Sci. U.S.A , vol.72 , pp. 1712-1716
    • Kent, R.J.1    Lin, R.L.2    Sallach, H.J.3    Cohen, P.P.4
  • 58
    • 0023042261 scopus 로고
    • The dihydroorotase domain of the multifunctional protein CAD. Subunit structure, zinc content, and kinetics
    • Kelly, R. E., Mally, M. I., and Evans, D. R. (1986) The dihydroorotase domain of the multifunctional protein CAD. Subunit structure, zinc content, and kinetics. J. Biol. Chem. 261, 6073-6083.
    • (1986) J. Biol. Chem , vol.261 , pp. 6073-6083
    • Kelly, R.E.1    Mally, M.I.2    Evans, D.R.3
  • 59
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E., and Henrick, K. (2007) Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372, 774-797.
    • (2007) J. Mol. Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.