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Volumn 409, Issue 2, 2008, Pages 357-366

The role of loop and β-turn residues as structural and functional determinants for the lipoyl domain from the Escherichia coli 2-oxoglutarate dehydrogenase complex

Author keywords

2 oxoglutarate dehydrogenase; Lipoyl domain; Post translational modification; Protein misfolding; Protein protein interaction; Substrate channelling

Indexed keywords

ACETYLATION; AMINO ACIDS; ESCHERICHIA COLI; PROTEINS;

EID: 38749121746     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20071119     Document Type: Article
Times cited : (14)

References (45)
  • 2
    • 0026079562 scopus 로고
    • Domains, motifs, and linkers in 2-oxo acid dehydrogenase multienzyme complexes: A paradigm in the design of a multifunctional enzyme
    • Perham, R. N. (1991) Domains, motifs, and linkers in 2-oxo acid dehydrogenase multienzyme complexes: a paradigm in the design of a multifunctional enzyme. Biochemistry 30, 8501-8512
    • (1991) Biochemistry , vol.30 , pp. 8501-8512
    • Perham, R.N.1
  • 3
    • 0025370816 scopus 로고
    • Structure-function relationships in dihydrolipoamide acyltransferases
    • Reed, L. J. and Hackert, M. L. (1990) Structure-function relationships in dihydrolipoamide acyltransferases. J. Biol. Chem. 265, 8971-8974
    • (1990) J. Biol. Chem , vol.265 , pp. 8971-8974
    • Reed, L.J.1    Hackert, M.L.2
  • 4
    • 0033790516 scopus 로고    scopus 로고
    • Swinging arms and swinging domains in multifunctional enzymes: Catalytic machines for multistep reactions
    • Perham, R. N. (2000) Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Ann. Rev. Biochem. 69, 961-1004
    • (2000) Ann. Rev. Biochem , vol.69 , pp. 961-1004
    • Perham, R.N.1
  • 5
    • 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. J. (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.J.7
  • 7
    • 0029071184 scopus 로고
    • Three dimensional structure of a lipoyl domain from the dihydrolipoyl acetyltransferase component of the pyruvate dehydrogenase multienzyme complex of Escherichia coli
    • Green, J. D. F., Laue, E. D., Perham, R. N., Ali, S. T. and Guest, J. R. (1995) Three dimensional structure of a lipoyl domain from the dihydrolipoyl acetyltransferase component of the pyruvate dehydrogenase multienzyme complex of Escherichia coli. J. Mol. Biol. 248, 328-343
    • (1995) J. Mol. Biol , vol.248 , pp. 328-343
    • Green, J.D.F.1    Laue, E.D.2    Perham, R.N.3    Ali, S.T.4    Guest, J.R.5
  • 8
    • 0034713840 scopus 로고    scopus 로고
    • Restricted motion of the lipoyl-lysine swinging arm in the pyruvate dehydrogenase complex of Escherichia coli
    • Jones, D. D., Stott, K. M., Howard, M. J. and Perham, R. N. (2000) Restricted motion of the lipoyl-lysine swinging arm in the pyruvate dehydrogenase complex of Escherichia coli. Biochemistry 39, 8448-8459
    • (2000) Biochemistry , vol.39 , pp. 8448-8459
    • Jones, D.D.1    Stott, K.M.2    Howard, M.J.3    Perham, R.N.4
  • 9
    • 0030598366 scopus 로고    scopus 로고
    • 3D structure of the lipoyl domain from the dihydrolipoyl succinyltransferase component of the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli
    • Ricaud, P. M., Howard, M. J., Roberts, E. L., Broadhurst, R. W. and Perham, R. N. (1996) 3D structure of the lipoyl domain from the dihydrolipoyl succinyltransferase component of the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli. J. Mol. Biol. 264, 179-190
    • (1996) J. Mol. Biol , vol.264 , pp. 179-190
    • Ricaud, P.M.1    Howard, M.J.2    Roberts, E.L.3    Broadhurst, R.W.4    Perham, R.N.5
  • 10
    • 0031053675 scopus 로고    scopus 로고
    • Three-dimensional structure in solution of the N-terminal lipoyl domain of the pyruvate dehydrogenase complex from Azotobacter vinelandii
    • Berg, A., Vervoort, J. and de Kok, A. (1997) Three-dimensional structure in solution of the N-terminal lipoyl domain of the pyruvate dehydrogenase complex from Azotobacter vinelandii. Euro. J. Biochem. 244, 352-360
    • (1997) Euro. J. Biochem , vol.244 , pp. 352-360
    • Berg, A.1    Vervoort, J.2    de Kok, A.3
  • 11
    • 0030598920 scopus 로고    scopus 로고
    • Solution structure of the lipoyl domain of the 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii
    • Berg, A., Vervoort, J. and de Kok, A. (1996) Solution structure of the lipoyl domain of the 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. J. Mol. Biol. 261, 432-442
    • (1996) J. Mol. Biol , vol.261 , pp. 432-442
    • Berg, A.1    Vervoort, J.2    de Kok, A.3
  • 13
    • 0037013207 scopus 로고    scopus 로고
    • Solution structure and dynamics of the lipoic acid-bearing domain of human mitochondrial branched-chain α-keto acid dehydrogenase complex
    • Chang, C. F., Chou, H. T., Chuang, J. L., Chuang, D. T. and Huang, T. H. (2002) Solution structure and dynamics of the lipoic acid-bearing domain of human mitochondrial branched-chain α-keto acid dehydrogenase complex. J. Biol. Chem. 277, 15865-15873
    • (2002) J. Biol. Chem , vol.277 , pp. 15865-15873
    • Chang, C.F.1    Chou, H.T.2    Chuang, J.L.3    Chuang, D.T.4    Huang, T.H.5
  • 14
    • 0029148130 scopus 로고
    • Purification and properties of the lipoate protein ligase of Escherichia coli
    • Green, D. E., Morris, T. W., Green, J., Cronan, J. E. and Guest, J. R. (1995) Purification and properties of the lipoate protein ligase of Escherichia coli. Biochem. J. 309, 853-862
    • (1995) Biochem. J , vol.309 , pp. 853-862
    • Green, D.E.1    Morris, T.W.2    Green, J.3    Cronan, J.E.4    Guest, J.R.5
  • 15
    • 0028821293 scopus 로고
    • Lipoic acid metabolism in Escherichia coli: The lplA and lipB genes define redundant pathways for ligation of lipoyl groups to apoprotein
    • Morris, T. W., Reed, K. E. and Cronan, Jr, J. E., (1995) Lipoic acid metabolism in Escherichia coli: the lplA and lipB genes define redundant pathways for ligation of lipoyl groups to apoprotein. J. Bacteriol. 177, 1-10
    • (1995) J. Bacteriol , vol.177 , pp. 1-10
    • Morris, T.W.1    Reed, K.E.2    Cronan Jr, J.E.3
  • 16
    • 0024560461 scopus 로고
    • Kinetics and specificity of reductive acylation of lipoyl domains from 2-oxo acid dehydrogenase complexes
    • Graham, L. D., Packman, L. C. and Perham, R. N. (1989) Kinetics and specificity of reductive acylation of lipoyl domains from 2-oxo acid dehydrogenase complexes. Biochemistry 28, 1574-1581
    • (1989) Biochemistry , vol.28 , pp. 1574-1581
    • Graham, L.D.1    Packman, L.C.2    Perham, R.N.3
  • 17
    • 84961044156 scopus 로고
    • Studies on a lipoic acid-activating system
    • Reed, L. J., Leach, F. R. and Koike, M. (1958) Studies on a lipoic acid-activating system. J. Biol. Chem. 232, 123-142
    • (1958) J. Biol. Chem , vol.232 , pp. 123-142
    • Reed, L.J.1    Leach, F.R.2    Koike, M.3
  • 18
    • 0032519817 scopus 로고    scopus 로고
    • Kinetics and specificity of reductive acylation of wild-type and mutated lipoyl domains of 2-oxo-acid dehydrogenase complexes from Azotobacter vinelandii
    • Berg, A., Westphal, A. H., Bosma, H. J. and de Kok, A. (1998) Kinetics and specificity of reductive acylation of wild-type and mutated lipoyl domains of 2-oxo-acid dehydrogenase complexes from Azotobacter vinelandii. Euro. J. Biochem. 252, 45-50
    • (1998) Euro. J. Biochem , vol.252 , pp. 45-50
    • Berg, A.1    Westphal, A.H.2    Bosma, H.J.3    de Kok, A.4
  • 19
    • 0025252199 scopus 로고
    • Interactions of lipoyl domains with the Elp subunit of the pyruvate dehydrogenase multienzyme complex from Escherichia coli
    • Graham, L. D. and Perham, R. N. (1990) Interactions of lipoyl domains with the Elp subunit of the pyruvate dehydrogenase multienzyme complex from Escherichia coli. FEBS Lett. 262, 241-244
    • (1990) FEBS Lett , vol.262 , pp. 241-244
    • Graham, L.D.1    Perham, R.N.2
  • 20
    • 0034645769 scopus 로고    scopus 로고
    • Structural determinants of post-translational modification and catalytic specificity for the lipoyl domains of the pyruvate dehydrogenase multienzyme complex of Escherichia coli
    • Jones, D. D., Horne, H. J., Reche, P. A. and Perham, R. N. (2000) Structural determinants of post-translational modification and catalytic specificity for the lipoyl domains of the pyruvate dehydrogenase multienzyme complex of Escherichia coli. J. Mol. Biol. 295, 289-306
    • (2000) J. Mol. Biol , vol.295 , pp. 289-306
    • Jones, D.D.1    Horne, H.J.2    Reche, P.A.3    Perham, R.N.4
  • 21
    • 0030789108 scopus 로고    scopus 로고
    • 2-Oxo acid dehydrogenase multienzyme complexes. The central role of the lipoyl domain
    • Berg, A. and de Kok, A. (1997) 2-Oxo acid dehydrogenase multienzyme complexes. The central role of the lipoyl domain. Biol. Chem. 378, 617-634
    • (1997) Biol. Chem , vol.378 , pp. 617-634
    • Berg, A.1    de Kok, A.2
  • 22
    • 0036545372 scopus 로고    scopus 로고
    • Substrate channelling in 2-oxo acid dehydrogenase multienzyme complexes
    • Perham, R. N., Jones, D. D., Chauhan, H. J. and Howard, M. J. (2002) Substrate channelling in 2-oxo acid dehydrogenase multienzyme complexes. Biochem. Soc. Trans. 30, 47-51
    • (2002) Biochem. Soc. Trans , vol.30 , pp. 47-51
    • Perham, R.N.1    Jones, D.D.2    Chauhan, H.J.3    Howard, M.J.4
  • 23
    • 0037161258 scopus 로고    scopus 로고
    • Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 Å resolution
    • Arjunan, P., Nemeria, N., Brunskill, A., Chandrasekhar, K., Sax, M., Yan, Y., Jordan, F., Guest, J. R. and Furey, W. (2002) Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 Å resolution. Biochemistry 41, 5213-5221
    • (2002) Biochemistry , vol.41 , pp. 5213-5221
    • Arjunan, P.1    Nemeria, N.2    Brunskill, A.3    Chandrasekhar, K.4    Sax, M.5    Yan, Y.6    Jordan, F.7    Guest, J.R.8    Furey, W.9
  • 24
    • 0038418364 scopus 로고    scopus 로고
    • Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase
    • Ciszak, E. M., Korotchkina, L. G., Dominiak, P. M., Sidhu, S. and Patel, M. S. (2003) Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase. J. Biol. Chem. 278, 21240-21246
    • (2003) J. Biol. Chem , vol.278 , pp. 21240-21246
    • Ciszak, E.M.1    Korotchkina, L.G.2    Dominiak, P.M.3    Sidhu, S.4    Patel, M.S.5
  • 25
    • 7444244483 scopus 로고    scopus 로고
    • A molecular switch and proton wire synchronize the active sites in thiamine enzymes
    • Frank, R. A., Titman, C. M., Pratap, J. V., Luisi, B. F. and Perham, R. N. (2004) A molecular switch and proton wire synchronize the active sites in thiamine enzymes. Science 306, 872-876
    • (2004) Science , vol.306 , pp. 872-876
    • Frank, R.A.1    Titman, C.M.2    Pratap, J.V.3    Luisi, B.F.4    Perham, R.N.5
  • 26
    • 34047185249 scopus 로고    scopus 로고
    • Crystal structure of the E1 component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex
    • Frank, R. A., Price, A. J., Northrop, F. D., Perham, R. N. and Luisi, B. F. (2007) Crystal structure of the E1 component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex. J. Mol. Biol. 368, 639-651
    • (2007) J. Mol. Biol , vol.368 , pp. 639-651
    • Frank, R.A.1    Price, A.J.2    Northrop, F.D.3    Perham, R.N.4    Luisi, B.F.5
  • 27
    • 0032813519 scopus 로고    scopus 로고
    • Crystal structure of 2-oxoisovalerate dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes
    • Aevarsson, A., Seger, K., Turley, S., Sokatch, J. R. and Hol, W. G. (1999) Crystal structure of 2-oxoisovalerate dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes. Nat. Struct. Biol. 6, 785-792
    • (1999) Nat. Struct. Biol , vol.6 , pp. 785-792
    • Aevarsson, A.1    Seger, K.2    Turley, S.3    Sokatch, J.R.4    Hol, W.G.5
  • 28
    • 0035808415 scopus 로고    scopus 로고
    • Recognition of the lipoyl domain is the ultimate determinant of substrate channelling in the pyruvate dehydrogenase multienzyme complex
    • Jones, D. D., Stott, K. M., Reche, P. A. and Perham, R. N. (2001) Recognition of the lipoyl domain is the ultimate determinant of substrate channelling in the pyruvate dehydrogenase multienzyme complex. J. Mol. Biol. 305, 49-60
    • (2001) J. Mol. Biol , vol.305 , pp. 49-60
    • Jones, D.D.1    Stott, K.M.2    Reche, P.A.3    Perham, R.N.4
  • 29
    • 0030298405 scopus 로고    scopus 로고
    • Recognition of a surface loop of the lipoyl domain underlies substrate channelling in the pyruvate dehydrogenase mutlienzyme complex
    • Wallis, N. G., Allen, M. D., Broadhurst, R. W., Lessard, I. A. D. and Perham, R. N. (1996) Recognition of a surface loop of the lipoyl domain underlies substrate channelling in the pyruvate dehydrogenase mutlienzyme complex. J. Mol. Biol. 263, 436-474
    • (1996) J. Mol. Biol , vol.263 , pp. 436-474
    • Wallis, N.G.1    Allen, M.D.2    Broadhurst, R.W.3    Lessard, I.A.D.4    Perham, R.N.5
  • 30
    • 0028221946 scopus 로고
    • Structural dependence of post-translational modification and reductive acetylation of the lipoyl domain of the pyruvate dehydrogenase multienzyme complex
    • Wallis, N. G. and Perham, R. N. (1994) Structural dependence of post-translational modification and reductive acetylation of the lipoyl domain of the pyruvate dehydrogenase multienzyme complex. J. Mol. Biol. 236, 209-216
    • (1994) J. Mol. Biol , vol.236 , pp. 209-216
    • Wallis, N.G.1    Perham, R.N.2
  • 31
    • 0032007565 scopus 로고    scopus 로고
    • Selectivity of post-translational modification in biotinylated proteins: The carboxy carrier protein of the acetyl-CoA carboxylase of Escherichia coli
    • Reche, P., Li, Y. L., Fuller, C., Eichhorn, K. and Perham, R. N. (1998) Selectivity of post-translational modification in biotinylated proteins: the carboxy carrier protein of the acetyl-CoA carboxylase of Escherichia coli. Biochem. J. 329, 589-596
    • (1998) Biochem. J , vol.329 , pp. 589-596
    • Reche, P.1    Li, Y.L.2    Fuller, C.3    Eichhorn, K.4    Perham, R.N.5
  • 32
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K. and Pease, L. R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 51-59
    • (1989) Gene , vol.77 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 33
    • 0024556150 scopus 로고
    • Engineering hybrid genes without the use of restriction enzymes: Gene-splicing by overlap extension
    • Horton, R. M., Hunt, H. D., Ho, S. N., Pullen, J. K. and Pease, L. R. (1989) Engineering hybrid genes without the use of restriction enzymes: gene-splicing by overlap extension. Gene 77, 61-68
    • (1989) Gene , vol.77 , pp. 61-68
    • Horton, R.M.1    Hunt, H.D.2    Ho, S.N.3    Pullen, J.K.4    Pease, L.R.5
  • 34
    • 0025285116 scopus 로고
    • Expression in Escherichia coli of a sub-gene encoding the lipoyl domain of the pyruvate dehydrogenase complex of Bacillus stearothermophilus
    • Dardel, F., Packman, L. C. and Perham, R. N. (1990) Expression in Escherichia coli of a sub-gene encoding the lipoyl domain of the pyruvate dehydrogenase complex of Bacillus stearothermophilus. FEBS Lett. 264, 206-210
    • (1990) FEBS Lett , vol.264 , pp. 206-210
    • Dardel, F.1    Packman, L.C.2    Perham, R.N.3
  • 35
    • 0343359244 scopus 로고
    • Investigation of the exchange processes by two-dimensional NMR spectroscopy
    • Jeener, J., Meier, J., Bachmann, P. and Ernst, R. R. (1979) Investigation of the exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 71, 323-341
    • (1979) J. Chem. Phys , vol.71 , pp. 323-341
    • Jeener, J.1    Meier, J.2    Bachmann, P.3    Ernst, R.R.4
  • 36
    • 0019327003 scopus 로고
    • A two-dimensional nuclear Overhauser enhancement experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules
    • Kumar, A., Ernst, R. R. and Wuthrich, K. (1980) A two-dimensional nuclear Overhauser enhancement experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res. Commun. 95, 1-6
    • (1980) Biochem. Biophys. Res. Commun , vol.95 , pp. 1-6
    • Kumar, A.1    Ernst, R.R.2    Wuthrich, K.3
  • 37
    • 0001250026 scopus 로고
    • ANSIG - a program for the assignment of protein H-1 2D NMR spectra by interactive computer graphics
    • Kraulis, P. J. (1989) ANSIG - a program for the assignment of protein H-1 2D NMR spectra by interactive computer graphics. J. Mag. Res. 84, 627-633
    • (1989) J. Mag. Res , vol.84 , pp. 627-633
    • Kraulis, P.J.1
  • 38
    • 0029915259 scopus 로고    scopus 로고
    • Expression, lipoylation and structure determination of recombinant pea H-protein in Escherichia coli
    • Macherel, D., Bourguignon, J., Forest, E., Faure, M., Cohen Addad, C. and Douce, R. (1996) Expression, lipoylation and structure determination of recombinant pea H-protein in Escherichia coli. Euro. J. Biochem. 236, 27-33
    • (1996) Euro. J. Biochem , vol.236 , pp. 27-33
    • Macherel, D.1    Bourguignon, J.2    Forest, E.3    Faure, M.4    Cohen Addad, C.5    Douce, R.6
  • 39
    • 0027463576 scopus 로고
    • Expression and lipoylation in Escherichia coli of the inner lipoyl domain of the E2-component of the human pyruvate dehydrogenase complex
    • Quinn, J., Diamond, A. G., Masters, A. K., Brookfield, D. E., Wallis, N. G. and Yeaman, S. J. (1993) Expression and lipoylation in Escherichia coli of the inner lipoyl domain of the E2-component of the human pyruvate dehydrogenase complex. Biochem. J. 289, 81-85
    • (1993) Biochem. J , vol.289 , pp. 81-85
    • Quinn, J.1    Diamond, A.G.2    Masters, A.K.3    Brookfield, D.E.4    Wallis, N.G.5    Yeaman, S.J.6
  • 40
    • 0034792592 scopus 로고    scopus 로고
    • Solution structure of the lipoyl domain of the chimeric dihydrolipoyl dehydrogenase P64K from Neisseria meningitidis
    • Tozawa, K., Broadhurst, R. W., Raine, A. R., Fuller, C., Alvarez, A., Guillen, G., Padron, G. and Perham, R. N. (2001) Solution structure of the lipoyl domain of the chimeric dihydrolipoyl dehydrogenase P64K from Neisseria meningitidis. Eur. J. Biochem. 268, 4908-4917
    • (2001) Eur. J. Biochem , vol.268 , pp. 4908-4917
    • Tozawa, K.1    Broadhurst, R.W.2    Raine, A.R.3    Fuller, C.4    Alvarez, A.5    Guillen, G.6    Padron, G.7    Perham, R.N.8
  • 41
    • 0034723135 scopus 로고    scopus 로고
    • Protein-protein interaction revealed by NMR T(2) relaxation experiments: The lipoyl domain and E1 component of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus
    • Howard, M. J., Chauhan, H. J., Domingo, G. J., Fuller, C. and Perham, R. N. (2000) Protein-protein interaction revealed by NMR T(2) relaxation experiments: the lipoyl domain and E1 component of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus. J. Mol. Biol. 295, 1023-1037
    • (2000) J. Mol. Biol , vol.295 , pp. 1023-1037
    • Howard, M.J.1    Chauhan, H.J.2    Domingo, G.J.3    Fuller, C.4    Perham, R.N.5
  • 42
    • 0029646091 scopus 로고
    • Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing
    • Athappilly, F. K. and Hendrickson, W. A. (1995) Structure of the biotinyl domain of acetyl-coenzyme A carboxylase determined by MAD phasing. Structure 3, 1407-1419
    • (1995) Structure , vol.3 , pp. 1407-1419
    • Athappilly, F.K.1    Hendrickson, W.A.2
  • 43
    • 0033586767 scopus 로고    scopus 로고
    • Solution structures of apo and holo biotinyl domains from acetyl coenzyme A carboxylase of Escherichia coli determined by triple-resonance nuclear magnetic resonance spectroscopy
    • Roberts, E. L., Shu, N., Howard, M. J., Broadhurst, R. W., Chapman-Smith, A., Wallace, J. C., Morris, T., Cronan, Jr, J. E. and Perham, R. N. (1999) Solution structures of apo and holo biotinyl domains from acetyl coenzyme A carboxylase of Escherichia coli determined by triple-resonance nuclear magnetic resonance spectroscopy. Biochemistry 38, 5045-5053
    • (1999) Biochemistry , vol.38 , pp. 5045-5053
    • Roberts, E.L.1    Shu, N.2    Howard, M.J.3    Broadhurst, R.W.4    Chapman-Smith, A.5    Wallace, J.C.6    Morris, T.7    Cronan Jr, J.E.8    Perham, R.N.9
  • 44
    • 0000041171 scopus 로고    scopus 로고
    • High resolution solution structure of the 1.3 S subunit of transcarboxylase from Propionibacterium shermanii
    • Reddy, D. V., Shenoy, B. C., Carey, P. R. and Sonnichsen, F. D. (2000) High resolution solution structure of the 1.3 S subunit of transcarboxylase from Propionibacterium shermanii. Biochemistry 39, 2509-2516
    • (2000) Biochemistry , vol.39 , pp. 2509-2516
    • Reddy, D.V.1    Shenoy, B.C.2    Carey, P.R.3    Sonnichsen, F.D.4
  • 45
    • 0030668421 scopus 로고    scopus 로고
    • Structure of the carboxy-terminal fragment of the apo-biotin carboxyl carrier subunit of Escherichia coli acetyl-CoA carboxylase
    • Yao, X., Wei, D., Soden, Jr, C., Summers, M. F. and Beckett, D. (1997) Structure of the carboxy-terminal fragment of the apo-biotin carboxyl carrier subunit of Escherichia coli acetyl-CoA carboxylase. Biochemistry 36, 15089-15100
    • (1997) Biochemistry , vol.36 , pp. 15089-15100
    • Yao, X.1    Wei, D.2    Soden Jr, C.3    Summers, M.F.4    Beckett, D.5


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