메뉴 건너뛰기




Volumn 52, Issue 3, 2013, Pages 488-496

Characterizing the importance of the biotin carboxylase domain dimer for staphylococcus aureus pyruvate carboxylase catalysis

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ANALYTICAL ULTRACENTRIFUGATION; BIOTIN CARBOXYLASE; CONFORMATIONAL CHANGE; DIMER INTERFACE; E. COLI; GEL FILTRATION; LONG-RANGE COMMUNICATIONS; MUTATION SITES; PYRUVATE CARBOXYLASE; SITE-SPECIFIC; STAPHYLOCOCCUS AUREUS; TETRAMERS;

EID: 84872760508     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi301294d     Document Type: Article
Times cited : (14)

References (42)
  • 2
    • 0036018143 scopus 로고    scopus 로고
    • Multi-subunit acetyl-CoA carboxylases
    • Cronan, J. E., Jr. and Waldrop, G. L. (2002) Multi-subunit acetyl-CoA carboxylases Prog. Lipid Res. 41, 407-435
    • (2002) Prog. Lipid Res. , vol.41 , pp. 407-435
    • Cronan Jr., J.E.1    Waldrop, G.L.2
  • 3
    • 23944509003 scopus 로고    scopus 로고
    • Acetyl-coenzyme A carboxylase: Crucial metabolic enzyme and attractive target for drug discovery
    • Tong, L. (2005) Acetyl-coenzyme A carboxylase: Crucial metabolic enzyme and attractive target for drug discovery Cell. Mol. Life Sci. 62, 1784-1803
    • (2005) Cell. Mol. Life Sci. , vol.62 , pp. 1784-1803
    • Tong, L.1
  • 5
    • 84873724816 scopus 로고    scopus 로고
    • Structure and function of biotin-dependent carboxylases
    • 101007/s00018-012-1096-0
    • Tong, L. (2012) Structure and function of biotin-dependent carboxylases Cell. Mol. Life Sci. 10.1007/s00018-012-1096-0
    • (2012) Cell. Mol. Life Sci.
    • Tong, L.1
  • 6
    • 0024315260 scopus 로고
    • The mechanism of biotin-dependent enzymes
    • Knowles, J. R. (1989) The mechanism of biotin-dependent enzymes Annu. Rev. Biochem. 58, 195-221
    • (1989) Annu. Rev. Biochem. , vol.58 , pp. 195-221
    • Knowles, J.R.1
  • 7
    • 0016285541 scopus 로고
    • Acetyl coenzyme A carboxylase system from Escherichia coli. Purification and properties of the biotin carboxylase, carboxyltransferase, and carboxyl carrier protein components
    • Guchhait, R. B., Polakis, S. E., Dimroth, P., Stoll, E., Moss, J., and Lane, M. D. (1974) Acetyl coenzyme A carboxylase system from Escherichia coli. Purification and properties of the biotin carboxylase, carboxyltransferase, and carboxyl carrier protein components J. Biol. Chem. 249, 6633-6645
    • (1974) J. Biol. Chem. , vol.249 , pp. 6633-6645
    • Guchhait, R.B.1    Polakis, S.E.2    Dimroth, P.3    Stoll, E.4    Moss, J.5    Lane, M.D.6
  • 8
    • 0023885546 scopus 로고
    • Catalytic mechanism of biotin carboxylase: Steady-state kinetic investigations
    • Tipton, P. A. and Cleland, W. W. (1988) Catalytic mechanism of biotin carboxylase: Steady-state kinetic investigations Biochemistry 27, 4317-4325
    • (1988) Biochemistry , vol.27 , pp. 4317-4325
    • Tipton, P.A.1    Cleland, W.W.2
  • 9
    • 0033574251 scopus 로고    scopus 로고
    • Mutations at four active site residues of biotin carboxylase abolish substrate-induced synergism by biotin
    • Blanchard, C. Z., Lee, Y. M., Frantom, P. A., and Waldrop, G. L. (1999) Mutations at four active site residues of biotin carboxylase abolish substrate-induced synergism by biotin Biochemistry 38, 3393-3400
    • (1999) Biochemistry , vol.38 , pp. 3393-3400
    • Blanchard, C.Z.1    Lee, Y.M.2    Frantom, P.A.3    Waldrop, G.L.4
  • 10
    • 0035816606 scopus 로고    scopus 로고
    • Site-directed mutagenesis of ATP binding residues of biotin carboxylase
    • Sloane, V., Blanchard, C. Z., Guillot, F., and Waldrop, G. L. (2001) Site-directed mutagenesis of ATP binding residues of biotin carboxylase J. Biol. Chem. 276, 24991-24996
    • (2001) J. Biol. Chem. , vol.276 , pp. 24991-24996
    • Sloane, V.1    Blanchard, C.Z.2    Guillot, F.3    Waldrop, G.L.4
  • 11
    • 0028085434 scopus 로고
    • Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase
    • Waldrop, G. L., Rayment, I., and Holden, H. M. (1994) Three-dimensional structure of the biotin carboxylase subunit of acetyl-CoA carboxylase Biochemistry 33, 10249-10256
    • (1994) Biochemistry , vol.33 , pp. 10249-10256
    • Waldrop, G.L.1    Rayment, I.2    Holden, H.M.3
  • 12
    • 0034717247 scopus 로고    scopus 로고
    • Movement of the biotin carboxylase B-domain as a result of ATP binding
    • Thoden, J. B., Blanchard, C. Z., Holden, H. M., and Waldrop, G. L. (2000) Movement of the biotin carboxylase B-domain as a result of ATP binding J. Biol. Chem. 275, 16183-16190
    • (2000) J. Biol. Chem. , vol.275 , pp. 16183-16190
    • Thoden, J.B.1    Blanchard, C.Z.2    Holden, H.M.3    Waldrop, G.L.4
  • 13
    • 52949102964 scopus 로고    scopus 로고
    • Structural evidence for substrate-induced synergism and half-sites reactivity in biotin carboxylase
    • Mochalkin, I., Miller, J. R., Evdokimov, A., Lightle, S., Yan, C., Stover, C. K., and Waldrop, G. L. (2008) Structural evidence for substrate-induced synergism and half-sites reactivity in biotin carboxylase Protein Sci. 17, 1706-1718
    • (2008) Protein Sci. , vol.17 , pp. 1706-1718
    • Mochalkin, I.1    Miller, J.R.2    Evdokimov, A.3    Lightle, S.4    Yan, C.5    Stover, C.K.6    Waldrop, G.L.7
  • 14
    • 66349100742 scopus 로고    scopus 로고
    • Crystal structure of biotin carboxylase in complex with substrates and implications for its catalytic mechanism
    • Chou, C.-Y., Yu, L. P. C., and Tong, L. (2009) Crystal structure of biotin carboxylase in complex with substrates and implications for its catalytic mechanism J. Biol. Chem. 284, 11690-11697
    • (2009) J. Biol. Chem. , vol.284 , pp. 11690-11697
    • Chou, C.-Y.1    Yu, L.P.C.2    Tong, L.3
  • 15
    • 0035839589 scopus 로고    scopus 로고
    • Function of Escherichia coli biotin carboxylase requires catalytic activity of both subunits of the homodimer
    • Janiyani, K., Bordelon, T., Waldrop, G. L., and Cronan, J. E., Jr. (2001) Function of Escherichia coli biotin carboxylase requires catalytic activity of both subunits of the homodimer J. Biol. Chem. 276, 29864-29870
    • (2001) J. Biol. Chem. , vol.276 , pp. 29864-29870
    • Janiyani, K.1    Bordelon, T.2    Waldrop, G.L.3    Cronan Jr., J.E.4
  • 16
    • 34047271417 scopus 로고    scopus 로고
    • Modeling and numerical simulation of biotin carboxylase kinetics: Implications for half-sites reactivity
    • de Queiroz, M. S. and Waldrop, G. L. (2007) Modeling and numerical simulation of biotin carboxylase kinetics: Implications for half-sites reactivity J. Theor. Biol. 246, 167-175
    • (2007) J. Theor. Biol. , vol.246 , pp. 167-175
    • De Queiroz, M.S.1    Waldrop, G.L.2
  • 17
    • 10944226843 scopus 로고    scopus 로고
    • A mechanism for the potent inhibition of eukaryotic acetyl-coenzyme A carboxylase by soraphen A, a macrocyclic polyketide natural product
    • Shen, Y., Volrath, S. L., Weatherly, S. C., Elich, T. D., and Tong, L. (2004) A mechanism for the potent inhibition of eukaryotic acetyl-coenzyme A carboxylase by soraphen A, a macrocyclic polyketide natural product Mol. Cell 16, 881-891
    • (2004) Mol. Cell , vol.16 , pp. 881-891
    • Shen, Y.1    Volrath, S.L.2    Weatherly, S.C.3    Elich, T.D.4    Tong, L.5
  • 18
    • 2642540877 scopus 로고    scopus 로고
    • Expression and characterization of recombinant fungal acetyl-CoA carboxylase and isolation of a soraphen-binding domain
    • Weatherly, S. C., Volrath, S. L., and Elich, T. D. (2004) Expression and characterization of recombinant fungal acetyl-CoA carboxylase and isolation of a soraphen-binding domain Biochem. J. 380, 105-110
    • (2004) Biochem. J. , vol.380 , pp. 105-110
    • Weatherly, S.C.1    Volrath, S.L.2    Elich, T.D.3
  • 19
    • 33745200041 scopus 로고    scopus 로고
    • Is dimerization required for the catalytic activity of bacterial biotin carboxylase?
    • Shen, Y., Chou, C.-Y., Chang, G.-G., and Tong, L. (2006) Is dimerization required for the catalytic activity of bacterial biotin carboxylase? Mol. Cell 22, 807-818
    • (2006) Mol. Cell , vol.22 , pp. 807-818
    • Shen, Y.1    Chou, C.-Y.2    Chang, G.-G.3    Tong, L.4
  • 20
    • 79959888192 scopus 로고    scopus 로고
    • Structural and biochemical studies on the regulation of biotin carboxylase by substrate inhibition and dimerization
    • Chou, C.-Y. and Tong, L. (2011) Structural and biochemical studies on the regulation of biotin carboxylase by substrate inhibition and dimerization J. Biol. Chem. 286, 24417-24425
    • (2011) J. Biol. Chem. , vol.286 , pp. 24417-24425
    • Chou, C.-Y.1    Tong, L.2
  • 21
    • 77955874035 scopus 로고    scopus 로고
    • Crystal structure of the a6b6 holoenzyme of propionyl-coenzyme A carboxylase
    • Huang, C. S., Sadre-Bazzaz, K., Shen, Y., Deng, B., Zhou, Z. H., and Tong, L. (2010) Crystal structure of the a6b6 holoenzyme of propionyl-coenzyme A carboxylase Nature 466, 1001-1005
    • (2010) Nature , vol.466 , pp. 1001-1005
    • Huang, C.S.1    Sadre-Bazzaz, K.2    Shen, Y.3    Deng, B.4    Zhou, Z.H.5    Tong, L.6
  • 22
    • 84855759432 scopus 로고    scopus 로고
    • An unanticipated architecture of the 750-kDa a6b6 holoezyme of 3-methylcrotonyl-CoA carboxylase
    • Huang, C. S., Ge, P., Zhou, Z. H., and Tong, L. (2012) An unanticipated architecture of the 750-kDa a6b6 holoezyme of 3-methylcrotonyl-CoA carboxylase Nature 481, 219-223
    • (2012) Nature , vol.481 , pp. 219-223
    • Huang, C.S.1    Ge, P.2    Zhou, Z.H.3    Tong, L.4
  • 23
    • 84858595979 scopus 로고    scopus 로고
    • Crystal structure of urea carboxylase provides insights into the carboxyltransfer reaction
    • Fan, C., Chou, C.-Y., Tong, L., and Xiang, S. (2012) Crystal structure of urea carboxylase provides insights into the carboxyltransfer reaction J. Biol. Chem. 287, 9389-9398
    • (2012) J. Biol. Chem. , vol.287 , pp. 9389-9398
    • Fan, C.1    Chou, C.-Y.2    Tong, L.3    Xiang, S.4
  • 25
    • 40949154700 scopus 로고    scopus 로고
    • Crystal structures of human and Staphylococcus aureus pyruvate carboxylase and molecular insights into the carboxyltransfer reaction
    • Xiang, S. and Tong, L. (2008) Crystal structures of human and Staphylococcus aureus pyruvate carboxylase and molecular insights into the carboxyltransfer reaction Nat. Struct. Mol. Biol. 15, 295-302
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 295-302
    • Xiang, S.1    Tong, L.2
  • 26
    • 66349116676 scopus 로고    scopus 로고
    • A symmetrical tetramer for S. aureus pyruvate carboxylase in complex with coenzyme A
    • Yu, L. P. C., Xiang, S., Lasso, G., Gil, D., Valle, M., and Tong, L. (2009) A symmetrical tetramer for S. aureus pyruvate carboxylase in complex with coenzyme A Structure 17, 823-832
    • (2009) Structure , vol.17 , pp. 823-832
    • Yu, L.P.C.1    Xiang, S.2    Lasso, G.3    Gil, D.4    Valle, M.5    Tong, L.6
  • 27
    • 80755174401 scopus 로고    scopus 로고
    • Interaction between the biotin carboxyl carrier domain and the biotin carboxylase domain in pyruvate carboxylase from Rhizobium etli
    • Lietzan, A. D., Menefee, A. L., Zeczycki, T. N., Kumar, S., Attwood, P. V., Wallace, J. C., Cleland, W. W., and St. Maurice, M. (2011) Interaction between the biotin carboxyl carrier domain and the biotin carboxylase domain in pyruvate carboxylase from Rhizobium etli Biochemistry 50, 9708-9723
    • (2011) Biochemistry , vol.50 , pp. 9708-9723
    • Lietzan, A.D.1    Menefee, A.L.2    Zeczycki, T.N.3    Kumar, S.4    Attwood, P.V.5    Wallace, J.C.6    Cleland, W.W.7    St. Maurice, M.8
  • 28
    • 0042855798 scopus 로고    scopus 로고
    • On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation
    • Schuck, P. (2003) On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation Anal. Biochem. 320, 104-124
    • (2003) Anal. Biochem. , vol.320 , pp. 104-124
    • Schuck, P.1
  • 29
    • 33744809773 scopus 로고    scopus 로고
    • Macromolecular size-and-shape distributions by sedimentation velocity analytical ultracentrifugation
    • Brown, P. H. and Schuck, P. (2006) Macromolecular size-and-shape distributions by sedimentation velocity analytical ultracentrifugation Biophys. J. 90, 4651-4661
    • (2006) Biophys. J. , vol.90 , pp. 4651-4661
    • Brown, P.H.1    Schuck, P.2
  • 30
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling
    • Schuck, P. (2000) Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and Lamm equation modeling Biophys. J. 78, 1606-1619
    • (2000) Biophys. J. , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 31
    • 0028786959 scopus 로고
    • Acetyl-CoA-dependent pyruvate carboxylase from the photosynthetic bacterium Rhodobacter capsulatus: Rapid and efficient purification using dye-ligand affinity chromatography
    • Modak, H. V. and Kelly, D. J. (1995) Acetyl-CoA-dependent pyruvate carboxylase from the photosynthetic bacterium Rhodobacter capsulatus: Rapid and efficient purification using dye-ligand affinity chromatography Microbiology 141, 2619-2628
    • (1995) Microbiology , vol.141 , pp. 2619-2628
    • Modak, H.V.1    Kelly, D.J.2
  • 32
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski, Z. and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode Methods Enzymol. 276, 307-326
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 33
    • 0034907074 scopus 로고    scopus 로고
    • COMO: A program for combined molecular replacement
    • Jogl, G., Tao, X., Xu, Y., and Tong, L. (2001) COMO: A program for combined molecular replacement Acta Crystallogr. D57, 1127-1134
    • (2001) Acta Crystallogr. , vol.57 , pp. 1127-1134
    • Jogl, G.1    Tao, X.2    Xu, Y.3    Tong, L.4
  • 35
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Refinement of macromolecular structures by the maximum-likelihood method Acta Crystallogr. D53, 240-255
    • (1997) Acta Crystallogr. , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 36
    • 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., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallogr. A47, 110-119
    • (1991) Acta Crystallogr. , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 37
    • 13244281317 scopus 로고    scopus 로고
    • Coot: Model-building tools for molecular graphics
    • Emsley, P. and Cowtan, K. D. (2004) Coot: Model-building tools for molecular graphics Acta Crystallogr. D60, 2126-2132
    • (2004) Acta Crystallogr. , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.D.2
  • 38
    • 7444221151 scopus 로고    scopus 로고
    • Structure of the biotin carboxylase subunit of pyruvate carboxylase from Aquifex aeolicus at 2.2 Å resolution
    • Kondo, S., Nakajima, Y., Sugio, S., Yong-Biao, J., Sueda, S., and Kondo, H. (2004) Structure of the biotin carboxylase subunit of pyruvate carboxylase from Aquifex aeolicus at 2.2 Å resolution Acta Crystallogr. D60, 486-492
    • (2004) Acta Crystallogr. , vol.60 , pp. 486-492
    • Kondo, S.1    Nakajima, Y.2    Sugio, S.3    Yong-Biao, J.4    Sueda, S.5    Kondo, H.6
  • 39
    • 34447633045 scopus 로고    scopus 로고
    • Structure of the biotin carboxylase domain of pyruvate carboxylase from Bacillus thermodenitrificans
    • Kondo, S., Nakajima, Y., Sugio, S., Sueda, S., Islam, M. N., and Kondo, H. (2007) Structure of the biotin carboxylase domain of pyruvate carboxylase from Bacillus thermodenitrificans Acta Crystallogr. D63, 885-890
    • (2007) Acta Crystallogr. , vol.63 , pp. 885-890
    • Kondo, S.1    Nakajima, Y.2    Sugio, S.3    Sueda, S.4    Islam, M.N.5    Kondo, H.6
  • 40
    • 1942455754 scopus 로고    scopus 로고
    • Protein engineering of pyruvate carboxylase. Investigation on the function of acetyl-CoA and the quaternary structure
    • Sueda, S., Islam, M. N., and Kondo, H. (2004) Protein engineering of pyruvate carboxylase. Investigation on the function of acetyl-CoA and the quaternary structure Eur. J. Biochem. 271, 1391-1400
    • (2004) Eur. J. Biochem. , vol.271 , pp. 1391-1400
    • Sueda, S.1    Islam, M.N.2    Kondo, H.3
  • 41
    • 17644385815 scopus 로고    scopus 로고
    • Construction of new forms of pyruvate carboxylase to assess the allosteric regulation by acetyl-CoA
    • Islam, M. N., Sueda, S., and Kondo, H. (2005) Construction of new forms of pyruvate carboxylase to assess the allosteric regulation by acetyl-CoA Protein Eng. 18, 71-78
    • (2005) Protein Eng. , vol.18 , pp. 71-78
    • Islam, M.N.1    Sueda, S.2    Kondo, H.3
  • 42
    • 84862945858 scopus 로고    scopus 로고
    • Dimerization of the bacterial biotin carboxylase subunit is required for acetyl coenzyme A carboxylase activity in vivo
    • Smith, A. C. and Cronan, J. E. (2012) Dimerization of the bacterial biotin carboxylase subunit is required for acetyl coenzyme A carboxylase activity in vivo J. Bacteriol. 194, 72-78
    • (2012) J. Bacteriol. , vol.194 , pp. 72-78
    • Smith, A.C.1    Cronan, J.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.