메뉴 건너뛰기




Volumn 39, Issue 8, 2006, Pages 550-557

Domain relationships in thiamine diphosphate-dependent enzymes

Author keywords

[No Author keywords available]

Indexed keywords

CARBON; CARBOXYLYASE; COCARBOXYLASE;

EID: 33748345821     PISSN: 00014842     EISSN: None     Source Type: Journal    
DOI: 10.1021/ar068022z     Document Type: Article
Times cited : (84)

References (27)
  • 2
    • 0026762799 scopus 로고
    • Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 Å resolution
    • Lindqvist, Y.; Schneider, G.; Ermler, U.; Sundström, M. Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 Å resolution. EMBO J. 1992, 11, 2373-2379.
    • (1992) EMBO J. , vol.11 , pp. 2373-2379
    • Lindqvist, Y.1    Schneider, G.2    Ermler, U.3    Sundström, M.4
  • 3
    • 0027479683 scopus 로고
    • Structure of the thiamine- And flavin-dependent enzyme pyruvate oxidase
    • Muller, Y. A.; Schulz, G. E. Structure of the thiamine- and flavin-dependent enzyme pyruvate oxidase. Science 1993, 259, 965-967.
    • (1993) Science , vol.259 , pp. 965-967
    • Muller, Y.A.1    Schulz, G.E.2
  • 4
    • 0027195094 scopus 로고
    • Catalytic centers in the thiamin diphosphate dependent enzyme pyruvate decarboxylase at 2.4-Å resolution
    • Dyda, F.; Furey, W.; Swaminathan, S.; Sax, M.; Farrenkopf, B.; Jordan, F. Catalytic centers in the thiamin diphosphate dependent enzyme pyruvate decarboxylase at 2.4-Å resolution. Biochemistry 1993, 32, 6165-6170.
    • (1993) Biochemistry , vol.32 , pp. 6165-6170
    • Dyda, F.1    Furey, W.2    Swaminathan, S.3    Sax, M.4    Farrenkopf, B.5    Jordan, F.6
  • 5
    • 28244449299 scopus 로고    scopus 로고
    • Structure and mechanism of the ThDP-dependent benzaldehyde lyase from Pseudomonas fluorescens
    • Mosbacher, T. G.; Mueller, M.; Schulz, G. E. Structure and mechanism of the ThDP-dependent benzaldehyde lyase from Pseudomonas fluorescens. FEBS J. 2005, 272, 6067-6076.
    • (2005) FEBS J. , vol.272 , pp. 6067-6076
    • Mosbacher, T.G.1    Mueller, M.2    Schulz, G.E.3
  • 8
    • 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.; Schneider, G. A thiamin diphosphate binding fold revealed by comparison of the crystal structures of transketolase, pyruvate oxidase and pyruvate decarboxylase. Structure 1993, 1, 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
  • 9
    • 0032537479 scopus 로고    scopus 로고
    • Structure and properties of pyruvate decarboxylase and site-directed mutagenesis of the Zymomonas mobilis enzyme
    • Candy, J. M.; Duggleby, R. G. Structure and properties of pyruvate decarboxylase and site-directed mutagenesis of the Zymomonas mobilis enzyme. Biochim. Biophys. Acta 1998, 1385, 323-338.
    • (1998) Biochim. Biophys. Acta , vol.1385 , pp. 323-338
    • Candy, J.M.1    Duggleby, R.G.2
  • 10
    • 0024432768 scopus 로고
    • A common structural motif in thiamin pyrophosphate-binding enzymes
    • Hawkins, C. F.; Borges, A.; Perham, R. N. A common structural motif in thiamin pyrophosphate-binding enzymes. FEBS Lett. 1989, 255, 77-82.
    • (1989) FEBS Lett. , vol.255 , pp. 77-82
    • Hawkins, C.F.1    Borges, A.2    Perham, R.N.3
  • 11
    • 0032813519 scopus 로고    scopus 로고
    • Crystal structure of 2-oxoisovalerate and dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes
    • Ævarsson, A.; Seger, K.; Turley, S.; Sokatch, J. R.; Hol, W. G. Crystal structure of 2-oxoisovalerate and dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes. Nat. Struct. Biol. 1999, 6, 785-792.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 785-792
    • Ævarsson, A.1    Seger, K.2    Turley, S.3    Sokatch, J.R.4    Hol, W.G.5
  • 12
    • 0036295208 scopus 로고    scopus 로고
    • Crystal structure of yeast acetohydroxyacid synthase: A target for herbicidal inhibitors
    • Pang, S. S.; Duggleby, R. G.; Guddat, L. W. Crystal structure of yeast acetohydroxyacid synthase: A target for herbicidal inhibitors. J. Mol. Biol. 2002, 317, 249-262.
    • (2002) J. Mol. Biol. , vol.317 , pp. 249-262
    • Pang, S.S.1    Duggleby, R.G.2    Guddat, L.W.3
  • 13
    • 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.; Furey, W. Structure of the pyruvate dehydrogenase multienzyme complex E1 component from Escherichia coli at 1.85 Å resolution. Biochemistry 2002, 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
  • 16
    • 0242321972 scopus 로고    scopus 로고
    • 146-β′ the reductive acylation reaction catalyzed by human branched-chain α-ketoacid dehydrogenase: Refined phosphorylation loop structure in the active site
    • 146-β′ the reductive acylation reaction catalyzed by human branched-chain α-ketoacid dehydrogenase: Refined phosphorylation loop structure in the active site. J. Biol. Chem. 2003, 278, 43402-43410.
    • (2003) J. Biol. Chem. , vol.278 , pp. 43402-43410
    • Wynn, R.M.1    Machius, M.2    Chuang, J.L.3    Li, J.4    Tomchick, D.R.5    Chuang, D.T.6
  • 17
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel, E.; Henrick, K. Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr., Sect. D: Biol. Crystallogr. 2004, 60, 2256-2268.
    • (2004) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 18
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-Pdb-Viewer: An environment for comparative protein modeling
    • Guex, N.; Peitsch, M. C. SWISS-MODEL and the Swiss-Pdb-Viewer: An environment for comparative protein modeling. Electrophoresis 1997, 18, 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 19
    • 0037314068 scopus 로고    scopus 로고
    • TopDraw: A sketchpad for protein structure topology cartoons
    • Bond, C. S. TopDraw: A sketchpad for protein structure topology cartoons. Bioinformatics 2003, 19, 311-312.
    • (2003) Bioinformatics , vol.19 , pp. 311-312
    • Bond, C.S.1
  • 20
    • 4644229608 scopus 로고    scopus 로고
    • Active-site conformational changes associated with hydride transfer in proton-translocating transhydrogenase
    • Mather, O. C.; Singh, A.; van Boxel, G. I.; White, S. A.; Jackson, J. B. Active-site conformational changes associated with hydride transfer in proton-translocating transhydrogenase. Biochemistry 2004, 43, 10952-10964.
    • (2004) Biochemistry , vol.43 , pp. 10952-10964
    • Mather, O.C.1    Singh, A.2    Van Boxel, G.I.3    White, S.A.4    Jackson, J.B.5
  • 21
    • 29244469942 scopus 로고    scopus 로고
    • Structural basis for activation of the thiamin diphosphate-dependent enzyme oxalyl-CoA decarboxylase by adenosine diphosphate
    • Berthold, C. L.; Moussatche, P.; Richards, N. G. J.; Lindqvist, Y. Structural basis for activation of the thiamin diphosphate-dependent enzyme oxalyl-CoA decarboxylase by adenosine diphosphate. J. Biol. Chem. 2005, 280, 41645-41654.
    • (2005) J. Biol. Chem. , vol.280 , pp. 41645-41654
    • Berthold, C.L.1    Moussatche, P.2    Richards, N.G.J.3    Lindqvist, Y.4
  • 22
    • 14044273048 scopus 로고    scopus 로고
    • Elucidating the specificity of binding of sulfonylurea herbicides to acetohydroxyacid synthase
    • McCourt, J. A.; Pang, S. S.; Duggleby, R. G.; Guddat, L. W. Elucidating the specificity of binding of sulfonylurea herbicides to acetohydroxyacid synthase. Biochemistry 2005, 44, 2330-2338.
    • (2005) Biochemistry , vol.44 , pp. 2330-2338
    • McCourt, J.A.1    Pang, S.S.2    Duggleby, R.G.3    Guddat, L.W.4
  • 23
    • 0036830233 scopus 로고    scopus 로고
    • Crystallographic and biochemical studies of DivK reveal novel features of an essential response regulator in Caulobacter crescentus
    • Guillet, V.; Ohta, N.; Cabantous, S.; Newton, A.; Samama, J. P. Crystallographic and biochemical studies of DivK reveal novel features of an essential response regulator in Caulobacter crescentus. J. Biol. Chem. 2002, 277, 42003-42010.
    • (2002) J. Biol. Chem. , vol.277 , pp. 42003-42010
    • Guillet, V.1    Ohta, N.2    Cabantous, S.3    Newton, A.4    Samama, J.P.5
  • 24
    • 0014454512 scopus 로고
    • Catalytic functions of thiamin diphosphate
    • Krampitz, L. O. Catalytic functions of thiamin diphosphate. Annu. Rev. Biochem. 1969, 38, 213-240.
    • (1969) Annu. Rev. Biochem. , vol.38 , pp. 213-240
    • Krampitz, L.O.1
  • 25
    • 0033893841 scopus 로고    scopus 로고
    • Identification of the gene encoding sulfopyruvate decarboxylase, an enzyme involved in biosynthesis of coenzyme M
    • Graupner, M.; Xu, H.; White, R. H. Identification of the gene encoding sulfopyruvate decarboxylase, an enzyme involved in biosynthesis of coenzyme M. J. Bacteriol. 2000, 782, 4862-4867.
    • (2000) J. Bacteriol. , vol.782 , pp. 4862-4867
    • Graupner, M.1    Xu, H.2    White, R.H.3
  • 26
    • 23444459343 scopus 로고    scopus 로고
    • The molecular origins of specificity in the assembly of a multienzyme complex
    • Frank, R. A. W.; Pratap, J. V.; Pei, X. Y.; Perham, R. N.; Luisi, B. F. The molecular origins of specificity in the assembly of a multienzyme complex. Structure 2005, 13, 1119-1130.
    • (2005) Structure , vol.13 , pp. 1119-1130
    • Frank, R.A.W.1    Pratap, J.V.2    Pei, X.Y.3    Perham, R.N.4    Luisi, B.F.5
  • 27
    • 0030050611 scopus 로고    scopus 로고
    • Molecular and phylogenetic characterization of pyruvate and 2-ketoisovalerate ferredoxin oxidoreductases from Pyrococcus furiosus and pyruvate ferredoxin oxidoreductase from Thermotoga maritime
    • Kletzin, A.; Adams, M. W. Molecular and phylogenetic characterization of pyruvate and 2-ketoisovalerate ferredoxin oxidoreductases from Pyrococcus furiosus and pyruvate ferredoxin oxidoreductase from Thermotoga maritime. J. Bacteriol. 1996, 178, 248-257.
    • (1996) J. Bacteriol. , vol.178 , pp. 248-257
    • Kletzin, A.1    Adams, M.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.