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Volumn 16, Issue 12, 2008, Pages 1860-1872

Snapshots of Catalysis in the E1 Subunit of the Pyruvate Dehydrogenase Multienzyme Complex

Author keywords

PROTEINS

Indexed keywords

ACETIC ACID DERIVATIVE; DIHYDROLIPOAMIDE DEHYDROGENASE; GLYCOPROTEIN E1; PROTON; PYRUVATE DEHYDROGENASE; PYRUVIC ACID; THIAMINE; THIOCTIC ACID;

EID: 57049130977     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2008.10.009     Document Type: Article
Times cited : (28)

References (56)
  • 1
    • 0032813519 scopus 로고    scopus 로고
    • Crystal structure of 2-oxoisovalerate and dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes
    • Aevarsson A., Seger K., Turley S., Sokatch J.R., and Hol W.G. Crystal structure of 2-oxoisovalerate and dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes. Nat. Struct. Biol. 6 (1999) 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
  • 2
    • 33646859093 scopus 로고    scopus 로고
    • A thiamin-bound, pre-decarboxylation reaction intermediate analogue in the pyruvate dehydrogenase E1 subunit induces large scale disorder-to-order transformations in the enzyme and reveals novel structural features in the covalently bound adduct
    • Arjunan P., Sax M., Brunskill A., Chandrasekhar K., Nemeria N., Zhang S., Jordan F., and Furey W. A thiamin-bound, pre-decarboxylation reaction intermediate analogue in the pyruvate dehydrogenase E1 subunit induces large scale disorder-to-order transformations in the enzyme and reveals novel structural features in the covalently bound adduct. J. Biol. Chem. 281 (2006) 15296-15303
    • (2006) J. Biol. Chem. , vol.281 , pp. 15296-15303
    • Arjunan, P.1    Sax, M.2    Brunskill, A.3    Chandrasekhar, K.4    Nemeria, N.5    Zhang, S.6    Jordan, F.7    Furey, W.8
  • 3
    • 35648979411 scopus 로고    scopus 로고
    • Strain and near attack conformers in enzymic thiamin catalysis: X-ray crystallographic snapshots of bacterial transketolase in covalent complex with donor ketoses xylulose 5-phosphate and fructose 6-phosphate, and in noncovalent complex with acceptor aldose ribose 5-phosphate
    • Asztalos P., Parthier C., Golbik R., Kleinschmidt M., Hubner G., Weiss M.S., Friedemann R., Wille G., and Tittmann K. Strain and near attack conformers in enzymic thiamin catalysis: X-ray crystallographic snapshots of bacterial transketolase in covalent complex with donor ketoses xylulose 5-phosphate and fructose 6-phosphate, and in noncovalent complex with acceptor aldose ribose 5-phosphate. Biochemistry 46 (2007) 12037-12052
    • (2007) Biochemistry , vol.46 , pp. 12037-12052
    • Asztalos, P.1    Parthier, C.2    Golbik, R.3    Kleinschmidt, M.4    Hubner, G.5    Weiss, M.S.6    Friedemann, R.7    Wille, G.8    Tittmann, K.9
  • 4
    • 0030789108 scopus 로고    scopus 로고
    • 2-Oxo acid dehydrogenase multienzyme complexes. The central role of the lipoyl domain
    • Berg A., and de Kok A. 2-Oxo acid dehydrogenase multienzyme complexes. The central role of the lipoyl domain. Biol. Chem. 378 (1997) 617-634
    • (1997) Biol. Chem. , vol.378 , pp. 617-634
    • Berg, A.1    de Kok, A.2
  • 5
    • 34447260286 scopus 로고    scopus 로고
    • Crystallographic snapshots of oxalyl-CoA decarboxylase give new insights into catalysis by non-oxidative ThDP-dependent decarboxylases
    • Berthold C.L., Toyota C.G., Moussatche P., Wood M.D., Leeper F.J., Richards N.G.J., and Lindqvist Y. Crystallographic snapshots of oxalyl-CoA decarboxylase give new insights into catalysis by non-oxidative ThDP-dependent decarboxylases. Structure 15 (2007) 853-861
    • (2007) Structure , vol.15 , pp. 853-861
    • Berthold, C.L.1    Toyota, C.G.2    Moussatche, P.3    Wood, M.D.4    Leeper, F.J.5    Richards, N.G.J.6    Lindqvist, Y.7
  • 6
    • 0000260773 scopus 로고
    • Rapid deuterium exchange in thiazolium salts
    • Breslow R. Rapid deuterium exchange in thiazolium salts. J. Am. Chem. Soc. 79 (1957) 1762-1763
    • (1957) J. Am. Chem. Soc. , vol.79 , pp. 1762-1763
    • Breslow, R.1
  • 8
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • CCP4 (Collaborative Computational Project, Number 4)
    • CCP4 (Collaborative Computational Project, Number 4). The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50 (1994) 760-763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 9
    • 33750356686 scopus 로고    scopus 로고
    • Active-site changes in the pyruvate dehydrogenase multienzyme complex E1 apoenzyme component from Escherichia coli observed at 2.32 A resolution
    • Chandrasekhar K., Arjunan P., Sax M., Nemeria N., Jordan F., and Furey W. Active-site changes in the pyruvate dehydrogenase multienzyme complex E1 apoenzyme component from Escherichia coli observed at 2.32 A resolution. Acta Crystallogr. D Biol. Crystallogr. 62 (2006) 1382-1386
    • (2006) Acta Crystallogr. D Biol. Crystallogr. , vol.62 , pp. 1382-1386
    • Chandrasekhar, K.1    Arjunan, P.2    Sax, M.3    Nemeria, N.4    Jordan, F.5    Furey, W.6
  • 10
    • 0034533110 scopus 로고    scopus 로고
    • Sites of limited proteolysis in the pyruvate decarboxylase component of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus and their role in catalysis
    • Chauhan H.J., Domingo G.J., Jung H.I., and Perham R.N. Sites of limited proteolysis in the pyruvate decarboxylase component of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus and their role in catalysis. Eur. J. Biochem. 267 (2000) 7158-7169
    • (2000) Eur. J. Biochem. , vol.267 , pp. 7158-7169
    • Chauhan, H.J.1    Domingo, G.J.2    Jung, H.I.3    Perham, R.N.4
  • 11
    • 0017201999 scopus 로고
    • Evidence for two lipoic acid residues per lipoate acetyltransferase chain in the pyruvate dehydrogenase multienzyme complex of Escherichia coli
    • Danson M.J., and Perham R.N. Evidence for two lipoic acid residues per lipoate acetyltransferase chain in the pyruvate dehydrogenase multienzyme complex of Escherichia coli. Biochem. J. 159 (1976) 677-682
    • (1976) Biochem. J. , vol.159 , pp. 677-682
    • Danson, M.J.1    Perham, R.N.2
  • 12
    • 0032537589 scopus 로고    scopus 로고
    • The pyruvate dehydrogenase multi-enzyme complex from Gram-negative bacteria
    • de Kok A., Hengeveld A.F., Martin A., and Westphal A.H. The pyruvate dehydrogenase multi-enzyme complex from Gram-negative bacteria. Biochim. Biophys. Acta 1385 (1998) 353-366
    • (1998) Biochim. Biophys. Acta , vol.1385 , pp. 353-366
    • de Kok, A.1    Hengeveld, A.F.2    Martin, A.3    Westphal, A.H.4
  • 14
    • 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. A molecular switch and proton wire synchronize the active sites in thiamine enzymes. Science 306 (2004) 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
  • 15
    • 23444459343 scopus 로고    scopus 로고
    • The molecular origins of specificity in the assembly of a multienzyme complex
    • Frank R.A., Pratap J.V., Pei X.Y., Perham R.N., and Luisi B.F. The molecular origins of specificity in the assembly of a multienzyme complex. Structure 13 (2005) 1119-1130
    • (2005) Structure , vol.13 , pp. 1119-1130
    • Frank, R.A.1    Pratap, J.V.2    Pei, X.Y.3    Perham, R.N.4    Luisi, B.F.5
  • 16
    • 34247143709 scopus 로고    scopus 로고
    • Structure, mechanism and catalytic duality of thiamine-dependent enzymes
    • Frank R.A., Leeper F.J., and Luisi B.F. Structure, mechanism and catalytic duality of thiamine-dependent enzymes. Cell. Mol. Life Sci. 64 (2007) 892-905
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 892-905
    • Frank, R.A.1    Leeper, F.J.2    Luisi, B.F.3
  • 17
    • 0038470825 scopus 로고    scopus 로고
    • Reaction mechanism of the heterotetrameric (α2β2) E1 component of 2-oxo acid dehydrogenase multienzyme complexes
    • Fries M., Jung H.I., and Perham R.N. Reaction mechanism of the heterotetrameric (α2β2) E1 component of 2-oxo acid dehydrogenase multienzyme complexes. Biochemistry 42 (2003) 6996-7002
    • (2003) Biochemistry , vol.42 , pp. 6996-7002
    • Fries, M.1    Jung, H.I.2    Perham, R.N.3
  • 19
    • 0033573917 scopus 로고    scopus 로고
    • Principles of quasi-equivalence and Euclidean geometry govern the assembly of cubic and dodecahedral cores of pyruvate dehydrogenase complexes
    • Izard T., Aevarsson A., Allen M.D., Westphal A.H., Perham R.N., de Kok A., and Hol W.G. Principles of quasi-equivalence and Euclidean geometry govern the assembly of cubic and dodecahedral cores of pyruvate dehydrogenase complexes. Proc. Natl. Acad. Sci. USA 96 (1999) 1240-1245
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 1240-1245
    • Izard, T.1    Aevarsson, A.2    Allen, M.D.3    Westphal, A.H.4    Perham, R.N.5    de Kok, A.6    Hol, W.G.7
  • 20
    • 38749121746 scopus 로고    scopus 로고
    • The role of loop and beta-turn residues as structural and functional determinants for the lipoyl domain from the Escherichia coli 2-oxoglutarate dehydrogenase complex
    • Jones D.D., and Perham R.N. The role of loop and beta-turn residues as structural and functional determinants for the lipoyl domain from the Escherichia coli 2-oxoglutarate dehydrogenase complex. Biochem. J. 409 (2008) 357-366
    • (2008) Biochem. J. , vol.409 , pp. 357-366
    • Jones, D.D.1    Perham, R.N.2
  • 21
    • 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. Recognition of the lipoyl domain is the ultimate determinant of substrate channelling in the pyruvate dehydrogenase multienzyme complex. J. Mol. Biol. 305 (2001) 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
  • 22
    • 0037391206 scopus 로고    scopus 로고
    • Current mechanistic understanding of thiamin diphosphate-dependent enzymatic reactions
    • Jordan F. Current mechanistic understanding of thiamin diphosphate-dependent enzymatic reactions. Nat. Prod. Rep. 20 (2003) 184-201
    • (2003) Nat. Prod. Rep. , vol.20 , pp. 184-201
    • Jordan, F.1
  • 23
    • 0344442892 scopus 로고    scopus 로고
    • Interactions of the peripheral subunit-binding domain of the dihydrolipoyl acetyltransferase component in the assembly of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus
    • Jung H.I., Cooper A., and Perham R.N. Interactions of the peripheral subunit-binding domain of the dihydrolipoyl acetyltransferase component in the assembly of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus. Eur. J. Biochem. 270 (2003) 4488-4496
    • (2003) Eur. J. Biochem. , vol.270 , pp. 4488-4496
    • Jung, H.I.1    Cooper, A.2    Perham, R.N.3
  • 24
    • 0344464847 scopus 로고    scopus 로고
    • Prediction of the binding site on E1 in the assembly of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus
    • Jung H.I., and Perham R.N. Prediction of the binding site on E1 in the assembly of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus. FEBS Lett. 555 (2003) 405-410
    • (2003) FEBS Lett. , vol.555 , pp. 405-410
    • Jung, H.I.1    Perham, R.N.2
  • 25
    • 34948872723 scopus 로고    scopus 로고
    • A dynamic loop at the active center of the Escherichia coli pyruvate dehydrogenase complex E1 component modulates substrate utilization and chemical communication with the E2 component
    • Kale S., Arjunan P., Furey W., and Jordan F. A dynamic loop at the active center of the Escherichia coli pyruvate dehydrogenase complex E1 component modulates substrate utilization and chemical communication with the E2 component. J. Biol. Chem. 282 (2007) 28106-28116
    • (2007) J. Biol. Chem. , vol.282 , pp. 28106-28116
    • Kale, S.1    Arjunan, P.2    Furey, W.3    Jordan, F.4
  • 26
    • 39549122002 scopus 로고    scopus 로고
    • Efficient coupling of catalysis and dynamics in the E1 component of Escherichia coli pyruvate dehydrogenase multienzyme complex
    • Kale S., Ulas G., Song J., Brudvig G.W., Furey W., and Jordan F. Efficient coupling of catalysis and dynamics in the E1 component of Escherichia coli pyruvate dehydrogenase multienzyme complex. Proc. Natl. Acad. Sci. USA 105 (2008) 1158-1163
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 1158-1163
    • Kale, S.1    Ulas, G.2    Song, J.3    Brudvig, G.W.4    Furey, W.5    Jordan, F.6
  • 28
    • 0017624125 scopus 로고
    • Study of the kinetic mechanism of the pyruvate-2,6-dichlorophenolindophenol reductase activity of muscle pyruvate dehydrogenase
    • Khailova L.S., Bernkhardt R., and Khiubner G. Study of the kinetic mechanism of the pyruvate-2,6-dichlorophenolindophenol reductase activity of muscle pyruvate dehydrogenase. Biokhimiia 42 (1977) 113-117
    • (1977) Biokhimiia , vol.42 , pp. 113-117
    • Khailova, L.S.1    Bernkhardt, R.2    Khiubner, G.3
  • 32
    • 57049133548 scopus 로고    scopus 로고
    • Lessard, I.A. (1995). Protein-protein interaction and the molecular self-assembly of the pyruvate dehydrogenase multienzyme complex. PhD thesis. Cambridge University, Cambridge.
    • Lessard, I.A. (1995). Protein-protein interaction and the molecular self-assembly of the pyruvate dehydrogenase multienzyme complex. PhD thesis. Cambridge University, Cambridge.
  • 34
    • 0030464497 scopus 로고    scopus 로고
    • Competitive interaction of component enzymes with the peripheral subunit-binding domain of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus: kinetic analysis using surface plasmon resonance detection
    • Lessard I.A., Fuller C., and Perham R.N. Competitive interaction of component enzymes with the peripheral subunit-binding domain of the pyruvate dehydrogenase multienzyme complex of Bacillus stearothermophilus: kinetic analysis using surface plasmon resonance detection. Biochemistry 35 (1996) 16863-16870
    • (1996) Biochemistry , vol.35 , pp. 16863-16870
    • Lessard, I.A.1    Fuller, C.2    Perham, R.N.3
  • 35
    • 34249651308 scopus 로고    scopus 로고
    • The two active sites in human branched-chain alpha-keto acid dehydrogenase operate independently without an obligatory alternating-site mechanism
    • Li J., Machius M., Chuang J.L., Wynn R.M., and Chuang D.T. The two active sites in human branched-chain alpha-keto acid dehydrogenase operate independently without an obligatory alternating-site mechanism. J. Biol. Chem. 282 (2007) 11904-11913
    • (2007) J. Biol. Chem. , vol.282 , pp. 11904-11913
    • Li, J.1    Machius, M.2    Chuang, J.L.3    Wynn, R.M.4    Chuang, D.T.5
  • 37
    • 3042826869 scopus 로고    scopus 로고
    • Inhibition of thiamin diphosphate dependent enzymes by 3-deazathiamin diphosphate
    • Mann S., Perez Melero C., Hawksley D., and Leeper F.J. Inhibition of thiamin diphosphate dependent enzymes by 3-deazathiamin diphosphate. Org. Biomol. Chem. 2 (2004) 1732-1741
    • (2004) Org. Biomol. Chem. , vol.2 , pp. 1732-1741
    • Mann, S.1    Perez Melero, C.2    Hawksley, D.3    Leeper, F.J.4
  • 40
    • 0027918180 scopus 로고
    • A thiamin diphosphate binding fold revealed by comparison of the crystal structures of transketolase, pyruvate oxidase and pyruvate decarboxylase
    • Muller Y.A., Lindqvist Y., Furey W., Schulz G.E., Jordan F., and Schneider G. A thiamin diphosphate binding fold revealed by comparison of the crystal structures of transketolase, pyruvate oxidase and pyruvate decarboxylase. Structure 1 (1993) 95-103
    • (1993) Structure , vol.1 , pp. 95-103
    • Muller, Y.A.1    Lindqvist, Y.2    Furey, W.3    Schulz, G.E.4    Jordan, F.5    Schneider, G.6
  • 42
    • 1642355234 scopus 로고    scopus 로고
    • Ligand-induced conformational changes and a reaction intermediate in branched-chain 2-oxo acid dehydrogenase (E1) from Thermus thermophilus HB8, as revealed by X-ray crystallography
    • Nakai T., Nakagawa N., Maoka N., Masui R., Kuraitsu S., and Kamiya N. Ligand-induced conformational changes and a reaction intermediate in branched-chain 2-oxo acid dehydrogenase (E1) from Thermus thermophilus HB8, as revealed by X-ray crystallography. J. Mol. Biol. 337 (2004) 1011-1033
    • (2004) J. Mol. Biol. , vol.337 , pp. 1011-1033
    • Nakai, T.1    Nakagawa, N.2    Maoka, N.3    Masui, R.4    Kuraitsu, S.5    Kamiya, N.6
  • 43
    • 0037207107 scopus 로고    scopus 로고
    • Histidine 407, a phantom residue in the E1 subunit of the Escherichia coli pyruvate dehydrogenase complex, activates reductive acetylation of lipoamide on the E2 subunit. An explanation for conservation of active sites between the E1 subunit and transketolase
    • Nemeria N., Arjunan P., Brunskill A., Sheibani F., Wei W., Yan Y., Zhang S., Jordan F., and Furey W. Histidine 407, a phantom residue in the E1 subunit of the Escherichia coli pyruvate dehydrogenase complex, activates reductive acetylation of lipoamide on the E2 subunit. An explanation for conservation of active sites between the E1 subunit and transketolase. Biochemistry 41 (2002) 15459-15467
    • (2002) Biochemistry , vol.41 , pp. 15459-15467
    • Nemeria, N.1    Arjunan, P.2    Brunskill, A.3    Sheibani, F.4    Wei, W.5    Yan, Y.6    Zhang, S.7    Jordan, F.8    Furey, W.9
  • 44
    • 2542557579 scopus 로고    scopus 로고
    • Tetrahedral intermediates in thiamin diphosphate-dependent decarboxylations exist as a 1′,4′-imino tautomeric form of the coenzyme, unlike the michaelis complex or the free coenzyme
    • Nemeria N., Baykal A., Joseph E., Zhang S., Yan Y., Furey W., and Jordan F. Tetrahedral intermediates in thiamin diphosphate-dependent decarboxylations exist as a 1′,4′-imino tautomeric form of the coenzyme, unlike the michaelis complex or the free coenzyme. Biochemistry 43 (2004) 6565-6575
    • (2004) Biochemistry , vol.43 , pp. 6565-6575
    • Nemeria, N.1    Baykal, A.2    Joseph, E.3    Zhang, S.4    Yan, Y.5    Furey, W.6    Jordan, F.7
  • 45
    • 34548671397 scopus 로고    scopus 로고
    • Elucidation of the chemistry of enzyme-bound thiamine diphosphate prior to substrate binding: defining internal equilibria among tautomeric and ionization states
    • Nemeria N., Korotchkina L., McLeish M.J., Kenyon G.L., Patel M.S., and Jordan F. Elucidation of the chemistry of enzyme-bound thiamine diphosphate prior to substrate binding: defining internal equilibria among tautomeric and ionization states. Biochemistry 46 (2007) 10739-10744
    • (2007) Biochemistry , vol.46 , pp. 10739-10744
    • Nemeria, N.1    Korotchkina, L.2    McLeish, M.J.3    Kenyon, G.L.4    Patel, M.S.5    Jordan, F.6
  • 46
    • 33846041174 scopus 로고    scopus 로고
    • The 1′,4′-iminopyrimidine tautomer of thiamin diphosphate is poised for catalysis in asymmetric active centers on enzymes
    • Nemeria N., Chakraborty S., Baykal A., Korotchkina L.G., Patel M.S., and Jordan F. The 1′,4′-iminopyrimidine tautomer of thiamin diphosphate is poised for catalysis in asymmetric active centers on enzymes. Proc. Natl. Acad. Sci. USA 104 (2007) 78-82
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 78-82
    • Nemeria, N.1    Chakraborty, S.2    Baykal, A.3    Korotchkina, L.G.4    Patel, M.S.5    Jordan, F.6
  • 47
    • 0029050640 scopus 로고
    • Alpha-keto acid dehydrogenase complexes: nutrient control, gene regulation and genetic defects. Overview
    • Patel M.S., and Harris R.A. Alpha-keto acid dehydrogenase complexes: nutrient control, gene regulation and genetic defects. Overview. J. Nutr. 125 (1995) 1744S-1745S
    • (1995) J. Nutr. , vol.125
    • Patel, M.S.1    Harris, R.A.2
  • 48
    • 0028979684 scopus 로고
    • Mammalian alpha-keto acid dehydrogenase complexes: gene regulation and genetic defects
    • Patel M.S., and Harris R.A. Mammalian alpha-keto acid dehydrogenase complexes: gene regulation and genetic defects. FASEB J. 9 (1995) 1164-1172
    • (1995) FASEB J. , vol.9 , pp. 1164-1172
    • Patel, M.S.1    Harris, R.A.2
  • 49
    • 0026079562 scopus 로고
    • Domains, motifs, and linkers in 2-oxo acid dehydrogenase multienzyme complexes: a paradigm in the design of a multifunctional protein
    • Perham R.N. Domains, motifs, and linkers in 2-oxo acid dehydrogenase multienzyme complexes: a paradigm in the design of a multifunctional protein. Biochemistry 30 (1991) 8501-8512
    • (1991) Biochemistry , vol.30 , pp. 8501-8512
    • Perham, R.N.1
  • 50
    • 0033790516 scopus 로고    scopus 로고
    • Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions
    • Perham R.N. Swinging arms and swinging domains in multifunctional enzymes: catalytic machines for multistep reactions. Annu. Rev. Biochem. 69 (2000) 961-1004
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 961-1004
    • Perham, R.N.1
  • 51
    • 0032537590 scopus 로고    scopus 로고
    • Sixty years of thiamin diphosphate biochemistry
    • Schellenberger A. Sixty years of thiamin diphosphate biochemistry. Biochim. Biophys. Acta 1385 (1998) 177-186
    • (1998) Biochim. Biophys. Acta , vol.1385 , pp. 177-186
    • Schellenberger, A.1
  • 52
    • 7544226311 scopus 로고    scopus 로고
    • PRODRG: a tool for high-throughput crystallography of protein-ligand complexes
    • Schuttelkopf A.W., and van Aalten D.M. PRODRG: a tool for high-throughput crystallography of protein-ligand complexes. Acta Crystallogr. D Biol. Crystallogr. 60 (2004) 1355-1363
    • (2004) Acta Crystallogr. D Biol. Crystallogr. , vol.60 , pp. 1355-1363
    • Schuttelkopf, A.W.1    van Aalten, D.M.2
  • 53
    • 34249702932 scopus 로고    scopus 로고
    • Phosphorylation of serine 264 impedes active site accessibility in the E1 component of the human pyruvate dehydrogenase multienzyme complex
    • Seifert F., Ciszak E., Korotchkina L., Golbik R., Spinka M., Dominiak P., Sidhu S., Brauer J., Patel M.S., and Tittmann K. Phosphorylation of serine 264 impedes active site accessibility in the E1 component of the human pyruvate dehydrogenase multienzyme complex. Biochemistry 46 (2007) 6277-6287
    • (2007) Biochemistry , vol.46 , pp. 6277-6287
    • Seifert, F.1    Ciszak, E.2    Korotchkina, L.3    Golbik, R.4    Spinka, M.5    Dominiak, P.6    Sidhu, S.7    Brauer, J.8    Patel, M.S.9    Tittmann, K.10
  • 54
    • 33750370889 scopus 로고    scopus 로고
    • Direct kinetic evidence for half-of-the-sites reactivity in the E1 component of the human pyruvate dehydrogenase multienzyme complex through alternating sites cofactor activation
    • Seifert F., Golbik R., Brauer J., Lilie H., Schroder-Tittmann K., Hinze E., Korotchkina L.G., Patel M.S., and Tittmann K. Direct kinetic evidence for half-of-the-sites reactivity in the E1 component of the human pyruvate dehydrogenase multienzyme complex through alternating sites cofactor activation. Biochemistry 45 (2006) 12775-12785
    • (2006) Biochemistry , vol.45 , pp. 12775-12785
    • Seifert, F.1    Golbik, R.2    Brauer, J.3    Lilie, H.4    Schroder-Tittmann, K.5    Hinze, E.6    Korotchkina, L.G.7    Patel, M.S.8    Tittmann, K.9
  • 55
    • 0029876191 scopus 로고    scopus 로고
    • Long-distance potentials: an approach to the multiple-minima problem in ligand-receptor interaction
    • Vakser I.A. Long-distance potentials: an approach to the multiple-minima problem in ligand-receptor interaction. Protein Eng. 9 (1996) 37-41
    • (1996) Protein Eng. , vol.9 , pp. 37-41
    • Vakser, I.A.1
  • 56
    • 33646894143 scopus 로고    scopus 로고
    • The catalytic cycle of a thiamin diphosphate enzyme examined by cryocrystallography
    • Wille G., Meyer D., Steinmetz A., Hinze E., Golbik R., and Tittmann K. The catalytic cycle of a thiamin diphosphate enzyme examined by cryocrystallography. Nat. Chem. Biol. 2 (2006) 324-328
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 324-328
    • Wille, G.1    Meyer, D.2    Steinmetz, A.3    Hinze, E.4    Golbik, R.5    Tittmann, K.6


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