메뉴 건너뛰기




Volumn 49, Issue 48, 2010, Pages 10319-10328

Catalytic role of the conformational change in succinyl-coa:3-oxoacid CoA transferase on binding CoA

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE CENTER; AMIDE GROUPS; CATALYTIC ROLE; CONFORMATIONAL CHANGE; COVALENTLY BOUND; FREEFORMS; STABILIZING INTERACTIONS; THIOESTERS; TRANSITION STATE; X-RAY DIFFRACTION DATA;

EID: 78650882297     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100659s     Document Type: Article
Times cited : (12)

References (40)
  • 1
    • 0014669443 scopus 로고
    • Identification of an enzyme-γ-glutamyl coenzyme A intermediate from coenzyme A transferase
    • Solomon, F., and Jencks, W. P. (1969) Identification of an enzyme-γ-glutamyl coenzyme A intermediate from coenzyme A transferase. J. Biol. Chem. 244, 1079-1081.
    • (1969) J. Biol. Chem. , vol.244 , pp. 1079-1081
    • Solomon, F.1    Jencks, W.P.2
  • 2
    • 0028307726 scopus 로고
    • Identification of glutamate344 as the catalytic residue in the active site of pig heart CoAtransferase
    • Rochet, J. C., and Bridger, W. A. (1994) Identification of glutamate344 as the catalytic residue in the active site of pig heart CoAtransferase. Protein Sci. 3, 975-981.
    • (1994) Protein Sci. , vol.3 , pp. 975-981
    • Rochet, J.C.1    Bridger, W.A.2
  • 3
    • 34648861883 scopus 로고
    • Studies concerning themechanism of action of acetoacetyl succinic thiophorase by use of O
    • Falcone, A. B., and Boyer, P. D. (1959) Studies concerning themechanism of action of acetoacetyl succinic thiophorase by use of O, Arch. BioChem. Biophys. 83, 337-344.
    • (1959) Arch. BioChem. Biophys. , vol.83 , pp. 337-344
    • Falcone, A.B.1    Boyer, P.D.2
  • 4
    • 0014670009 scopus 로고
    • The participation of anenzyme-bound oxygen group in a coenzyme A transferase reaction
    • Benson, R. W., and Boyer, P. D. (1969) The participation of anenzyme-bound oxygen group in a coenzyme A transferase reaction. J. Biol. Chem. 244, 2366-2371.
    • (1969) J. Biol. Chem. , vol.244 , pp. 2366-2371
    • Benson, R.W.1    Boyer, P.D.2
  • 5
    • 44449097276 scopus 로고    scopus 로고
    • Reinvestigation of the catalytic mechanism of formyl-CoAtransferase, a class III CoA-transferase
    • Berthold, C. L., Toyota, C. G., Richards, N. G., and Lindqvist, Y.(2008) Reinvestigation of the catalytic mechanism of formyl-CoAtransferase, a class III CoA-transferase. J. Biol. Chem. 283, 6519-6529.
    • (2008) J. Biol. Chem. , vol.283 , pp. 6519-6529
    • Berthold, C.L.1    Toyota, C.G.2    Richards, N.G.3    Lindqvist, Y.4
  • 6
    • 0029083357 scopus 로고
    • Role of bindingenergy with coenzyme A in catalysis by 3-oxoacid coenzyme Atransferase
    • Whitty, A., Fierke, C. A., and Jencks, W. P. (1995) Role of bindingenergy with coenzyme A in catalysis by 3-oxoacid coenzyme Atransferase. Biochemistry 34, 11678-11689.
    • (1995) Biochemistry , vol.34 , pp. 11678-11689
    • Whitty, A.1    Fierke, C.A.2    Jencks, W.P.3
  • 7
    • 0020491196 scopus 로고
    • Formation of active site thiolesters of CoA transferase and the dependence of catalysis on specificbinding interactions
    • Moore, S. A., and Jencks, W. P. (1982) Formation of active site thiolesters of CoA transferase and the dependence of catalysis on specificbinding interactions. J. Biol. Chem. 257, 10893-10907.
    • (1982) J. Biol. Chem. , vol.257 , pp. 10893-10907
    • Moore, S.A.1    Jencks, W.P.2
  • 8
    • 0023002427 scopus 로고
    • Two functional domains ofcoenzyme A activate catalysis by coenzyme A transferase
    • Fierke, C. A., and Jencks, W. P. (1986) Two functional domains ofcoenzyme A activate catalysis by coenzyme A transferase. J. Biol. Chem. 261, 7603-7606.
    • (1986) J. Biol. Chem. , vol.261 , pp. 7603-7606
    • Fierke, C.A.1    Jencks, W.P.2
  • 9
    • 0017295718 scopus 로고
    • Utilization of theinactivation rate of coenzyme A trasferase by thiol reagents todetermine properties of the enzyme-CoA intermediate
    • White, H., Solomon, F., and Jencks, W. P. (1976) Utilization of theinactivation rate of coenzyme A trasferase by thiol reagents todetermine properties of the enzyme-CoA intermediate. J. Biol. Chem. 251, 1700-1707.
    • (1976) J. Biol. Chem. , vol.251 , pp. 1700-1707
    • White, H.1    Solomon, F.2    Jencks, W.P.3
  • 10
    • 0019616523 scopus 로고
    • Modification and inactivationof CoA transferase by 2-nitro-5- (thiocyanato) benzoate
    • Kindman, L. A., and Jencks, W. P. (1981) Modification and inactivationof CoA transferase by 2-nitro-5-(thiocyanato) benzoate. Biochemistry 20, 5183-5187.
    • (1981) Biochemistry , vol.20 , pp. 5183-5187
    • Kindman, L.A.1    Jencks, W.P.2
  • 12
    • 2242445271 scopus 로고    scopus 로고
    • Structure of the mammalian CoA transferase from pig heart
    • Bateman, K. S., Brownie, E. R., Wolodko, W. T., and Fraser, M. E.(2002) Structure of the mammalian CoA transferase from pig heart.Biochemistry 41, 14455-14462.
    • (2002) Biochemistry , vol.41 , pp. 14455-14462
    • Bateman, K.S.1    Brownie, E.R.2    Wolodko, W.T.3    Fraser, M.E.4
  • 13
    • 16644387198 scopus 로고    scopus 로고
    • Structure of the CoA transferase from pig heart to 1.7 A resolution
    • Coros, A. M., Swenson, L., Wolodko, W. T., and Fraser, M. E. (2004) Structure of the CoA transferase from pig heart to 1.7 A resolution.Acta Crystallogr. D 60, 1717-1725.
    • (2004) Acta Crystallogr. D , vol.60 , pp. 1717-1725
    • Coros, A.M.1    Swenson, L.2    Wolodko, W.T.3    Fraser, M.E.4
  • 14
    • 34648836742 scopus 로고    scopus 로고
    • Identificationof the cysteine residue exposed by the conformational change in pigheart succinyl-CoA:3-ketoacid coenzyme A transferase on bindingcoenzyme A
    • Tammam, S. D., Rochet, J. C., and Fraser, M. E. (2007) Identificationof the cysteine residue exposed by the conformational change in pigheart succinyl-CoA:3-ketoacid coenzyme A transferase on bindingcoenzyme A. Biochemistry 46, 10852-10863.
    • (2007) Biochemistry , vol.46 , pp. 10852-10863
    • Tammam, S.D.1    Rochet, J.C.2    Fraser, M.E.3
  • 15
    • 0022632387 scopus 로고
    • Mechanism-based fragmentation of coenzyme A transferase. Comparisonof alpha 2-macroglobulin and coenzyme A transferase thiolester reactions
    • Howard, J. B., Zieske, L., Clarkson, J., and Rathe, L. (1986) Mechanism-based fragmentation of coenzyme A transferase. Comparisonof alpha 2-macroglobulin and coenzyme A transferase thiolester reactions. J. Biol. Chem. 261, 60-65.
    • (1986) J. Biol. Chem. , vol.261 , pp. 60-65
    • Howard, J.B.1    Zieske, L.2    Clarkson, J.3    Rathe, L.4
  • 16
    • 0017184389 scopus 로고
    • A rapid and sensitive method for thequantitation of microgram quantities of protein utilizing the principleof protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for thequantitation of microgram quantities of protein utilizing the principleof protein-dye binding. Anal. BioChem. 72, 248-254.
    • (1976) Anal. BioChem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 18
    • 1242274650 scopus 로고    scopus 로고
    • Automated protein crystal structuredetermination using ELVES
    • Holton, J., and Alber, T. (2004) Automated protein crystal structuredetermination using ELVES. Proc. Natl. Acad. Sci. U.S.A. 101, 1537-1542.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 1537-1542
    • Holton, J.1    Alber, T.2
  • 19
    • 0028103275 scopus 로고
    • The CCP4 suite:Programs for protein crystallography
    • Collaborative Computational Project N.
    • Collaborative Computational Project, N. (1994) The CCP4 suite:Programs for protein crystallography. Acta Crystallogr. D50, 760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 21
    • 33846426122 scopus 로고    scopus 로고
    • Solving structures of protein complexes bymolecular replacement with Phaser
    • McCoy, A. J. (2007) Solving structures of protein complexes bymolecular replacement with Phaser. Acta Crystallogr., Sect. D: Biol. Crystallogr. 63, 32-41.
    • (2007) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.63 , pp. 32-41
    • McCoy, A.J.1
  • 22
    • 84920325457 scopus 로고
    • AMoRe: An automated package for molecularreplacement
    • Navaza, J. (1994) AMoRe: an automated package for molecularreplacement. Acta Crystallogr. A50, 157-163.
    • (1994) Acta Crystallogr. A , vol.50 , pp. 157-163
    • Navaza, J.1
  • 27
    • 33744459472 scopus 로고    scopus 로고
    • Toward the structural genomics of complexes:crystal structure of a PE/PPE protein complex from Mycobacteriumtuberculosis
    • Strong, M., Sawaya, M. R., Wang, S., Phillips, M., Cascio, D., and Eisenberg, D. (2006) Toward the structural genomics of complexes:crystal structure of a PE/PPE protein complex from Mycobacteriumtuberculosis. Proc. Natl. Acad. Sci. U.S.A. 103, 8060-8065.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 8060-8065
    • Strong, M.1    Sawaya, M.R.2    Wang, S.3    Phillips, M.4    Cascio, D.5    Eisenberg, D.6
  • 28
    • 33645158291 scopus 로고    scopus 로고
    • TLSMDweb server for the generationof multi-group TLS models
    • Painter, J., and Merritt, E. A. (2006) TLSMDweb server for the generationof multi-group TLS models. J. Appl. Crystallogr. 39, 109-111.
    • (2006) J. Appl. Crystallogr. , vol.39 , pp. 109-111
    • Painter, J.1    Merritt, E.A.2
  • 29
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modelling
    • Guex, N., and Peitsch, M. C. (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modelling.Electrophoresis 18, 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 30
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density mapsand the location of errors in thesemodels
    • Jones, T. A., Zou, J.-Y., Cowan, S. W., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density mapsand the location of errors in thesemodels. Acta Crystallogr.A47, 110-119.
    • (1991) Acta Crystallogr.A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 31
    • 0032006209 scopus 로고    scopus 로고
    • Systematic analysis of domainmotions in proteins from conformational change; New results on citratesynthase and T4 lysozyme
    • Hayward, S., and Berendsen, H. J.C. (1998) Systematic analysis of domainmotions in proteins from conformational change; new results on citratesynthase and T4 lysozyme. Proteins: Struct., Funct., Genet. 30, 144-154.
    • (1998) Proteins: Struct., Funct., Genet. , vol.30 , pp. 144-154
    • Hayward, S.1    Berendsen, H.J.C.2
  • 32
    • 0042011224 scopus 로고    scopus 로고
    • Matthews coefficientprobabilities: Improved estimates for unit cell contents of proteins, DNA, and protein-nucleic acid complex crystals
    • Kantardjieff, K. A., and Rupp, B. (2003) Matthews coefficientprobabilities: improved estimates for unit cell contents of proteins, DNA, and protein-nucleic acid complex crystals. Protein Sci. 12, 1865-1871.
    • (2003) Protein Sci. , vol.12 , pp. 1865-1871
    • Kantardjieff, K.A.1    Rupp, B.2
  • 33
    • 0014432781 scopus 로고
    • Solvent content of protein crystals
    • Matthews, B. W. (1968) Solvent content of protein crystals. J. Mol.Biol. 33, 491-497.
    • (1968) J. Mol.Biol. , vol.33 , pp. 491-497
    • Matthews, B.W.1
  • 34
    • 0035957052 scopus 로고    scopus 로고
    • Dimeric pig heartsuccinate-coenzyme A transferase uses only one subunit to supportcatalysis
    • Lloyd, A. J., and Shoolingin-Jordan, P. M. (2001) Dimeric pig heartsuccinate-coenzyme A transferase uses only one subunit to supportcatalysis. Biochemistry 40, 2455-2467.
    • (2001) Biochemistry , vol.40 , pp. 2455-2467
    • Lloyd, A.J.1    Shoolingin-Jordan, P.M.2
  • 35
    • 0031569327 scopus 로고    scopus 로고
    • Glutaconate CoA-transferase from Acidaminococcusfermentans: The crystal structure reveals homology withother CoA-transferases
    • Jacob, U., Mack, M., Clausen, T., Huber, R., Buckel, W., and Messerschmidt, A. (1997) Glutaconate CoA-transferase from Acidaminococcusfermentans: the crystal structure reveals homology withother CoA-transferases. Structure 5, 415-426.
    • (1997) Structure , vol.5 , pp. 415-426
    • Jacob, U.1    MacK, M.2    Clausen, T.3    Huber, R.4    Buckel, W.5    Messerschmidt, A.6
  • 36
    • 77955451055 scopus 로고    scopus 로고
    • Thenitrated proteome in heart mitochondria of the db/db mouse model:characterization of nitrated tyrosine residues in SCOT
    • Wang, Y., Peng, F., Tong, W., Sun, H., Xu, N., and Liu, S. (2010) Thenitrated proteome in heart mitochondria of the db/db mouse model:characterization of nitrated tyrosine residues in SCOT, J. ProteomeRes. (in press) .
    • (2010) J. ProteomeRes. (In Press)
    • Wang, Y.1    Peng, F.2    Tong, W.3    Sun, H.4    Xu, N.5    Liu, S.6
  • 39
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce bothdetailed and schematic plots of protein structures
    • Kraulis, P. J. (1991) MOLSCRIPT: a program to produce bothdetailed and schematic plots of protein structures. J. Appl. Crystallogr.24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 40
    • 0030815133 scopus 로고    scopus 로고
    • Raster3D: Photorealisticmolecular graphics
    • (Carter, C. W., Jr., and Sweet, R. M., Eds.), Academic Press, New York
    • Merritt, E. A., and Bacon, D. J. (1997) Raster3D: photorealisticmolecular graphics, in Methods in Enzymology (Carter, C. W., Jr., and Sweet, R. M., Eds.) pp 505-524, Academic Press, New York.
    • (1997) Methods in Enzymology , pp. 505-524
    • Merritt, E.A.1    Bacon, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.