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Volumn 30, Issue 3, 1998, Pages 369-378

Heterologous expression of human transketolase

Author keywords

Heterologous expression; Kinetic parameters; Protein purification; Recombinant human transketolase; Thiamin diphosphate

Indexed keywords

COCARBOXYLASE; MAGNESIUM ION; RECOMBINANT ENZYME; RIBOSE 5 PHOSPHATE; TRANSKETOLASE; UNCLASSIFIED DRUG; XYLULOSE 5 PHOSPHATE;

EID: 0031831425     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-2725(97)00154-4     Document Type: Article
Times cited : (16)

References (34)
  • 1
    • 0026664038 scopus 로고
    • Nucleotide and predicted amino acid sequence of a cDNA clone encoding part of human transketolase
    • Abedinia M., Layfield R., Jones S.M., Nixon P.F., Mattick J.S. Nucleotide and predicted amino acid sequence of a cDNA clone encoding part of human transketolase. Biochem. Biophys. Res. Commun. 183:1992;1159-1166.
    • (1992) Biochem. Biophys. Res. Commun. , vol.183 , pp. 1159-1166
    • Abedinia, M.1    Layfield, R.2    Jones, S.M.3    Nixon, P.F.4    Mattick, J.S.5
  • 2
    • 0027081210 scopus 로고
    • High control coefficient of transketolase in the nonoxidative pentose phosphate pathway of human erythrocytes: NMR, antibody, and computer simulation studies
    • Berthon H.A., Kuchel P.W., Nixon P.F. High control coefficient of transketolase in the nonoxidative pentose phosphate pathway of human erythrocytes: NMR, antibody, and computer simulation studies. Biochemistry. 31:1992;12792-12798.
    • (1992) Biochemistry , vol.31 , pp. 12792-12798
    • Berthon, H.A.1    Kuchel, P.W.2    Nixon, P.F.3
  • 3
    • 0017571187 scopus 로고
    • Abnormality of a thiamine-requiring enzyme in patients with Wernicke-Korsakoff syndrome
    • Blass J.P., Gibson G.E. Abnormality of a thiamine-requiring enzyme in patients with Wernicke-Korsakoff syndrome. N. Engl. J. Med. 297:1977;1367-1370.
    • (1977) N. Engl. J. Med. , vol.297 , pp. 1367-1370
    • Blass, J.P.1    Gibson, G.E.2
  • 4
    • 0345264908 scopus 로고
    • Ph.D. Thesis, The University of Queensland, Brisbane, Australia
    • C.K. Booth, Studies on vitamin K and thiamin, Ph.D. Thesis, The University of Queensland, Brisbane, Australia, 1991.
    • (1991) Studies on Vitamin K and Thiamin
    • Booth, C.K.1
  • 5
    • 0027369409 scopus 로고
    • Reconstitution of holotransketolase is by a thiamin-diphosphate-magnesium complex
    • Booth C.K., Nixon P.F. Reconstitution of holotransketolase is by a thiamin-diphosphate-magnesium complex. Eur. J. Biochem. 218:1993;261-265.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 261-265
    • Booth, C.K.1    Nixon, P.F.2
  • 6
    • 0000474852 scopus 로고
    • Biased codon usage: An exploration of its role in optimization of translation
    • in: W.S. Reznikoff, L. Gold (Eds.), Butterworth Publishers, New York
    • H.A. de Boer, R.A. Kastelein, Biased codon usage: An exploration of its role in optimization of translation, in: W.S. Reznikoff, L. Gold (Eds.), Maximizing Gene Expression, Butterworth Publishers, New York, 1986, pp. 225-285.
    • (1986) Maximizing Gene Expression , pp. 225-285
    • De Boer, H.A.1    Kastelein, R.A.2
  • 7
    • 0025783215 scopus 로고
    • Pyruvate decarboxylase from Zymomonas mobilis: Structure and re-activation of apoenzyme by the cofactors thiamin diphosphate and magnesium ion
    • Diefenbach R.J., Duggleby R.G. Pyruvate decarboxylase from Zymomonas mobilis: Structure and re-activation of apoenzyme by the cofactors thiamin diphosphate and magnesium ion. Biochem. J. 276:1991;439-445.
    • (1991) Biochem. J. , vol.276 , pp. 439-445
    • Diefenbach, R.J.1    Duggleby, R.G.2
  • 8
    • 0021636975 scopus 로고
    • Regression analysis of nonlinear Arrhenius plots: An empirical model and a computer program
    • Duggleby R.G. Regression analysis of nonlinear Arrhenius plots: An empirical model and a computer program. Comput. Biol. Med. 14:1984;447-455.
    • (1984) Comput. Biol. Med. , vol.14 , pp. 447-455
    • Duggleby, R.G.1
  • 9
    • 0019888067 scopus 로고
    • Transketolase kinetics: The slow reconstitution of the holoenzyme is due to rate-limiting dimerization of the subunits
    • Egan R.M., Sable H.Z. Transketolase kinetics: The slow reconstitution of the holoenzyme is due to rate-limiting dimerization of the subunits. J. Biol. Chem. 256:1981;4877-4883.
    • (1981) J. Biol. Chem. , vol.256 , pp. 4877-4883
    • Egan, R.M.1    Sable, H.Z.2
  • 10
  • 11
    • 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. 255:1989;77-82.
    • (1989) FEBS Lett. , vol.255 , pp. 77-82
    • Hawkins, C.F.1    Borges, A.2    Perham, R.N.3
  • 12
    • 0015229043 scopus 로고
    • A circular dichroism study of transketolase from baker's yeast
    • Heinrich P.C., Noack K., Wiss O. A circular dichroism study of transketolase from baker's yeast. Biochem. Biophys. Res. Commun. 44:1971;275-279.
    • (1971) Biochem. Biophys. Res. Commun. , vol.44 , pp. 275-279
    • Heinrich, P.C.1    Noack, K.2    Wiss, O.3
  • 13
    • 0015170516 scopus 로고
    • Transketolase from human erythrocyte: Purification and properties
    • Heinrich P.C., Wiss O. Transketolase from human erythrocyte: Purification and properties. Helv. Chim. Acta. 54:1971;2658-2668.
    • (1971) Helv. Chim. Acta , vol.54 , pp. 2658-2668
    • Heinrich, P.C.1    Wiss, O.2
  • 14
    • 0345696544 scopus 로고
    • Molecular cloning of human transketolase: Complementary DNA and protein sequence
    • Jung E.H., Sheu K.F.R., Blass J.P. Molecular cloning of human transketolase: Complementary DNA and protein sequence. FASEB J. 7:1993;A838.
    • (1993) FASEB J. , vol.7 , pp. 838
    • Jung, E.H.1    Sheu, K.F.R.2    Blass, J.P.3
  • 15
    • 0042492718 scopus 로고
    • Structure and mechanism of action of transketolase
    • Kochetov G.A. Structure and mechanism of action of transketolase. Biokhimiya. 51:1986;2020-2029.
    • (1986) Biokhimiya , vol.51 , pp. 2020-2029
    • Kochetov, G.A.1
  • 16
    • 0029199270 scopus 로고
    • Crystallization and preliminary X-ray crystallographic data with Escherichia coli transketolase
    • Littlechild J.A., Turner N.J., Hobbs G.R., Lilly M.D., Rawas R., Watson W. Crystallization and preliminary X-ray crystallographic data with Escherichia coli transketolase. Acta Cryst. D. 51:1995;1074-1076.
    • (1995) Acta Cryst. D , vol.51 , pp. 1074-1076
    • Littlechild, J.A.1    Turner, N.J.2    Hobbs, G.R.3    Lilly, M.D.4    Rawas, R.5    Watson, W.6
  • 17
    • 0027459038 scopus 로고
    • Cloning of human transketolase cDNAs and comparison of the nucleotide sequence of the coding region in Wernicke-Korsakoff and non-Wernicke-Korsakoff individuals
    • McCool B.A., Plonk S.G., Martin P.R., Singleton C.K. Cloning of human transketolase cDNAs and comparison of the nucleotide sequence of the coding region in Wernicke-Korsakoff and non-Wernicke-Korsakoff individuals. J. Biol. Chem. 268:1993;1397-1404.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1397-1404
    • McCool, B.A.1    Plonk, S.G.2    Martin, P.R.3    Singleton, C.K.4
  • 18
    • 0028305456 scopus 로고
    • Refined structure of transketolase from Saccharomyces cerevisiae at 2.0 Å resolution
    • Nikkola M., Lindqvist Y., Schneider G. Refined structure of transketolase from Saccharomyces cerevisiae at 2.0 Å resolution. J. Mol. Biol. 238:1994;387-404.
    • (1994) J. Mol. Biol. , vol.238 , pp. 387-404
    • Nikkola, M.1    Lindqvist, Y.2    Schneider, G.3
  • 19
  • 23
    • 0031001809 scopus 로고    scopus 로고
    • Molecular evolutionary analysis of the thiamin diphosphate-dependent enzyme, transketolase
    • Schenk G., Layfield R., Candy J.M., Duggleby R.G., Nixon P.F. Molecular evolutionary analysis of the thiamin diphosphate-dependent enzyme, transketolase. J. Mol. Evol. 44:1997;552-572.
    • (1997) J. Mol. Evol. , vol.44 , pp. 552-572
    • Schenk, G.1    Layfield, R.2    Candy, J.M.3    Duggleby, R.G.4    Nixon, P.F.5
  • 24
    • 0025857432 scopus 로고
    • Effects of increased transaldolase activity on D-xylulose and D-glucose metabolism in Saccharomyces cerevisiae cell extracts
    • Senac T., Hahn-Hägerdahl B. Effects of increased transaldolase activity on D-xylulose and D-glucose metabolism in Saccharomyces cerevisiae cell extracts. Appl. Environ. Microbiol. 57:1991;1701-1706.
    • (1991) Appl. Environ. Microbiol. , vol.57 , pp. 1701-1706
    • Senac, T.1    Hahn-Hägerdahl, B.2
  • 25
    • 0028893623 scopus 로고
    • The thiamine-dependent hysteretic behaviour of human transketolase: Implications for thiamine deficiency
    • Singleton C.K., Pekovich S.R., McCool B.A., Martin P.R. The thiamine-dependent hysteretic behaviour of human transketolase: Implications for thiamine deficiency. J. Nutr. 125:1995;189-194.
    • (1995) J. Nutr. , vol.125 , pp. 189-194
    • Singleton, C.K.1    Pekovich, S.R.2    McCool, B.A.3    Martin, P.R.4
  • 26
    • 0029770049 scopus 로고    scopus 로고
    • Conserved residues are functionally distinct within transketolases of different species
    • Singleton C.K., Wang J.J.L., Shan L., Martin P.R. Conserved residues are functionally distinct within transketolases of different species. Biochemistry. 35:1996;15865-15869.
    • (1996) Biochemistry , vol.35 , pp. 15865-15869
    • Singleton, C.K.1    Wang, J.J.L.2    Shan, L.3    Martin, P.R.4
  • 27
    • 0015086056 scopus 로고
    • A NADH-dependent transketolase assay in erythrocyte hemolysates
    • Smeets E.H.J., Muller H., de Wael J. A NADH-dependent transketolase assay in erythrocyte hemolysates. Clin. Chim. Acta. 33:1971;379-386.
    • (1971) Clin. Chim. Acta , vol.33 , pp. 379-386
    • Smeets, E.H.J.1    Muller, H.2    De Wael, J.3
  • 28
    • 0029067816 scopus 로고
    • Transketolase A of Escherichia coli K12. Purification and properties of the enzyme from recombinant strains
    • Sprenger G.A., Schörken U., Sprenger G., Sahm H. Transketolase A of Escherichia coli K12. Purification and properties of the enzyme from recombinant strains. Eur. J. Biochem. 230:1995;525-532.
    • (1995) Eur. J. Biochem. , vol.230 , pp. 525-532
    • Sprenger, G.A.1    Schörken, U.2    Sprenger, G.3    Sahm, H.4
  • 29
    • 0027515306 scopus 로고
    • Yeast TKL1 gene encodes a transketolase that is required for efficient glycolysis and biosynthesis of aromatic amino acids
    • Sundström M., Lindqvist Y., Schneider G., Hellman U., Ronne H. Yeast TKL1 gene encodes a transketolase that is required for efficient glycolysis and biosynthesis of aromatic amino acids. J. Biol. Chem. 268:1993;24346-24352.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24346-24352
    • Sundström, M.1    Lindqvist, Y.2    Schneider, G.3    Hellman, U.4    Ronne, H.5
  • 30
    • 0023114283 scopus 로고
    • Measurement of Michaelis constant for human erythrocyte transketolase and thiamin diphosphate
    • Tate J.R., Nixon P.F. Measurement of Michaelis constant for human erythrocyte transketolase and thiamin diphosphate. Anal. Biochem. 160:1987;78-87.
    • (1987) Anal. Biochem. , vol.160 , pp. 78-87
    • Tate, J.R.1    Nixon, P.F.2
  • 31
    • 0027968068 scopus 로고
    • CLUSTALW: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTALW: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acids Res. 22:1994;4673-4680.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 33
    • 0028575439 scopus 로고
    • Analysis of an invariant cofactor-protein interaction in thiamin diphosphate dependent enzymes by site-directed mutagenesis
    • Wikner C., Meshalkina L., Nilsson U., Nikkola M., Lindqvist Y., Schneider G. Analysis of an invariant cofactor-protein interaction in thiamin diphosphate dependent enzymes by site-directed mutagenesis. J. Biol. Chem. 269:1994;32144-32150.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32144-32150
    • Wikner, C.1    Meshalkina, L.2    Nilsson, U.3    Nikkola, M.4    Lindqvist, Y.5    Schneider, G.6


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