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Volumn 30, Issue 12, 1998, Pages 1297-1318

Properties and functions of the thiamin diphosphate dependent enzyme transketolase

Author keywords

Kinetics; Pentose phosphate pathway; Thiamin deficiency; Thiamin diphosphate; Transketolase

Indexed keywords

THIAMINE DERIVATIVE; TRANSKETOLASE;

EID: 0032423288     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-2725(98)00095-8     Document Type: Review
Times cited : (211)

References (187)
  • 1
    • 0026664038 scopus 로고
    • Nucleotide and predicted amino acid sequence of a cDNA clone encoding part of human transketolase
    • M. Abedinia, R. Layfield, S.M. Jones, P.P. Nixon, J.S. Mattick, 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.P.4    Mattick, J.S.5
  • 3
    • 0029967678 scopus 로고    scopus 로고
    • Crystal structure of the thiamin diphosphate-dependent enzyme pyruvate decarboxylase from the yeast Saccharomyces cerevisiae at 2.3 Å resolution
    • P. Arjunan, T. Umland, F. Dyda, S. Swaminathan, W. Furey, M. Sax, B. Farrenkopf, Y. Gao, D. Zhang, F. Jordan, Crystal structure of the thiamin diphosphate-dependent enzyme pyruvate decarboxylase from the yeast Saccharomyces cerevisiae at 2.3 Å resolution, J. Mol. Biol. 256 (1996) 590-600.
    • (1996) J. Mol. Biol. , vol.256 , pp. 590-600
    • Arjunan, P.1    Umland, T.2    Dyda, F.3    Swaminathan, S.4    Furey, W.5    Sax, M.6    Farrenkopf, B.7    Gao, Y.8    Zhang, D.9    Jordan, F.10
  • 4
    • 0028819199 scopus 로고
    • The transketolase gene family of the resurrection plant Craterostigma plantaglneum: Differential expression during the rehydration phase
    • G. Bernacchia, G. Schwall, F. Lottspeich, F. Salamini, D. Bartels, The transketolase gene family of the resurrection plant Craterostigma plantaglneum: differential expression during the rehydration phase, EMBO J. 14 (1995) 610-618.
    • (1995) EMBO J. , vol.14 , pp. 610-618
    • Bernacchia, G.1    Schwall, G.2    Lottspeich, F.3    Salamini, F.4    Bartels, D.5
  • 5
    • 0027081210 scopus 로고
    • High control coefficient of transketolase in the nonoxidative pentose phosphate pathway of human erythrocytes: NMR, anti-body, and computer simulation studies
    • H.A. Berthon, P.W. Kuchel, P.F. Nixon, High control coefficient of transketolase in the nonoxidative pentose phosphate pathway of human erythrocytes: NMR, anti-body, 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
  • 6
    • 0025991946 scopus 로고
    • No transketolase abnormalities in Wernicke-Korsakoff patients
    • B.A. Blansjaar, R. Zwang, B.G. Blijenberg, No transketolase abnormalities in Wernicke-Korsakoff patients, J. Neurol. Sci. 106 (1991) 88-90.
    • (1991) J. Neurol. Sci. , vol.106 , pp. 88-90
    • Blansjaar, B.A.1    Zwang, R.2    Blijenberg, B.G.3
  • 7
    • 0017571187 scopus 로고
    • Abnormality of a thiamine-requiring enzyme in patients with Wernicke-Korsakoff syndrome
    • J.P. Blass, G.E. Gibson, 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
  • 10
    • 0345264908 scopus 로고
    • PhD Thesis, The University of Queensland, Brisbane, Australia
    • C. K. Booth, Studies on vitamin K and thiamin. PhD Thesis, The University of Queensland, Brisbane, Australia, 1991.
    • (1991) Studies on Vitamin K and Thiamin
    • Booth, C.K.1
  • 11
    • 0027369409 scopus 로고
    • Reconstitution of holotransketolase is by a thiamin-diphosphate-magnesium complex
    • C.K. Booth, P.P. Nixon, 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.P.2
  • 12
    • 3142640259 scopus 로고
    • Mechanisms of thiamine action. Evidence from studies on model systems
    • R. Breslow, Mechanisms of thiamine action. Evidence from studies on model systems, J. Am. Chem. Soc. 80 (1958) 3719-3726.
    • (1958) J. Am. Chem. Soc. , vol.80 , pp. 3719-3726
    • Breslow, R.1
  • 13
    • 0001070024 scopus 로고
    • Studies on model systems for thiamine action. Synthesis of reactive intermediates and evidence on the function of the pyrimidine ring
    • R. Breslow, E. McNelis, Studies on model systems for thiamine action. Synthesis of reactive intermediates and evidence on the function of the pyrimidine ring, J. Am. Chem. Soc. 81 (1959) 3080-3082.
    • (1959) J. Am. Chem. Soc. , vol.81 , pp. 3080-3082
    • Breslow, R.1    McNelis, E.2
  • 14
    • 0000796042 scopus 로고
    • The mechanism of thiamine action: Prediction from model experiments
    • R. Breslow, The mechanism of thiamine action: prediction from model experiments, Ann. N.Y. Acad. Sci. 98 (1962) 445-452.
    • (1962) Ann. N.Y. Acad. Sci. , vol.98 , pp. 445-452
    • Breslow, R.1
  • 15
  • 16
    • 0022395355 scopus 로고
    • Activities of thiamine-dependent enzymes in two experimental models of thiamine-deficiency encephalopathy: 1. the pyruvate dehydrogenase complex
    • R.F. Butterworth, J.F. Giguère, A.M. Besnard, Activities of thiamine-dependent enzymes in two experimental models of thiamine-deficiency encephalopathy: 1. the pyruvate dehydrogenase complex, Neurochem. Res. 10 (1985) 1417-1428.
    • (1985) Neurochem. Res. , vol.10 , pp. 1417-1428
    • Butterworth, R.F.1    Giguère, J.F.2    Besnard, A.M.3
  • 17
    • 0022492048 scopus 로고
    • Activities of thiamine-dependent enzymes in two experimental models of thiamine-deficiency encephalopathy: 2. α-ketoglutarate dehydrogenase
    • R.F. Butterworth, J.F. Giguère, A.M. Besnard, Activities of thiamine-dependent enzymes in two experimental models of thiamine-deficiency encephalopathy: 2. α-ketoglutarate dehydrogenase, Neurochem. Res. 11 (1986) 567-577.
    • (1986) Neurochem. Res. , vol.11 , pp. 567-577
    • Butterworth, R.F.1    Giguère, J.F.2    Besnard, A.M.3
  • 18
    • 0028198915 scopus 로고
    • Investigation of the cofactor-binding site of Zymomonas mobilis pyruvate decarboxylase by site-directed mutagenesis
    • J.M. Candy, R.G. Duggleby, Investigation of the cofactor-binding site of Zymomonas mobilis pyruvate decarboxylase by site-directed mutagenesis, Biochem. J. 300 (1994) 7-13.
    • (1994) Biochem. J. , vol.300 , pp. 7-13
    • Candy, J.M.1    Duggleby, R.G.2
  • 19
    • 0010426612 scopus 로고    scopus 로고
    • Site-directed mutagenesis of E50, F496 and His113 in Zymomonas mobilis pyruvate decarboxylase
    • H. Bisswanger, A. Schellenberger (Eds.), Wissenschaftlicher Verlag, Prien, Germany
    • J. M. Candy, P. F. Nixon, R. England, G. Schenk, J. Koga, R. G. Duggleby, Site-directed mutagenesis of E50, F496 and His113 in Zymomonas mobilis pyruvate decarboxylase. in: H. Bisswanger, A. Schellenberger (Eds.), Biochemistry and Physiology of Thiamin Diphosphate Enzymes, A and C Intemann, Wissenschaftlicher Verlag, Prien, Germany, 1996, pp. 82-102.
    • (1996) Biochemistry and Physiology of Thiamin Diphosphate Enzymes, a and C Intemann , pp. 82-102
    • Candy, J.M.1    Nixon, P.F.2    England, R.3    Schenk, G.4    Koga, J.5    Duggleby, R.G.6
  • 20
    • 0016726177 scopus 로고
    • Enzymes of penlose biosynthesis. the quaternary structure and reacting form of transketolase from baker's yeast
    • S.W. Cavalieri, K.E. Neat, H.Z. Sable, Enzymes of penlose biosynthesis. The quaternary structure and reacting form of transketolase from baker's yeast, Arch. Biochem. Biophys. 171 (1975) 527-532.
    • (1975) Arch. Biochem. Biophys. , vol.171 , pp. 527-532
    • Cavalieri, S.W.1    Neat, K.E.2    Sable, H.Z.3
  • 22
    • 50549159930 scopus 로고
    • The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations
    • W.W. Cleland, The kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations, Biochim. Biophys. Acta 67 (1963) 104-137.
    • (1963) Biochim. Biophys. Acta , vol.67 , pp. 104-137
    • Cleland, W.W.1
  • 23
    • 0029976005 scopus 로고    scopus 로고
    • Molecular cloning of tissue-specific transcripts of a transketolase-related gene: Implications for the evolution of new vertebrate genes
    • J.F. Coy, S. Dübel, P. Kioschis, K. Thomas, G. Micklem, H. Delius, A. Poustka, Molecular cloning of tissue-specific transcripts of a transketolase-related gene: implications for the evolution of new vertebrate genes, Genomics 32 (1996) 309-316.
    • (1996) Genomics , vol.32 , pp. 309-316
    • Coy, J.F.1    Dübel, S.2    Kioschis, P.3    Thomas, K.4    Micklem, G.5    Delius, H.6    Poustka, A.7
  • 24
    • 70349629097 scopus 로고
    • Mechanism of action of transketolase
    • A.G. Datta, E. Racker, Mechanism of action of transketolase, J. Biol. Chem. 236 (1961) 617-623.
    • (1961) J. Biol. Chem. , vol.236 , pp. 617-623
    • Datta, A.G.1    Racker, E.2
  • 25
    • 0000843320 scopus 로고
    • Crystalline transketolase from baker's yeast. Isolation and properties
    • G. de la Haba, LG. Leder, E. Racker, Crystalline transketolase from baker's yeast. Isolation and properties, J. Biol. Chem. 214 (1955) 409-426.
    • (1955) J. Biol. Chem. , vol.214 , pp. 409-426
    • De La Haba, G.1    Leder, L.G.2    Racker, E.3
  • 27
    • 0025831993 scopus 로고
    • Enzyme-catalyzed synthesis of carbohydrates: Synthetic potential of transketolase
    • C. Demuynck, J. Bolte, L. Hecquet, V. Dalmas, Enzyme-catalyzed synthesis of carbohydrates: synthetic potential of transketolase, Tetrahedron Lett. 32 (1991) 5085-5088.
    • (1991) Tetrahedron Lett. , vol.32 , pp. 5085-5088
    • Demuynck, C.1    Bolte, J.2    Hecquet, L.3    Dalmas, V.4
  • 28
    • 0026598760 scopus 로고
    • Effects of substitution of aspartate-440 and tryptophan-487 in the thiamin diphosphate binding region of pyruvate decarboxylase from Zymomonas mobilis
    • R.J. Diefenbach, J.M. Candy, J.S. Mattick, R.G. Duggleby, Effects of substitution of aspartate-440 and tryptophan-487 in the thiamin diphosphate binding region of pyruvate decarboxylase from Zymomonas mobilis, FEBS Lett. 296 (1992) 95-98.
    • (1992) FEBS Lett. , vol.296 , pp. 95-98
    • Diefenbach, R.J.1    Candy, J.M.2    Mattick, J.S.3    Duggleby, R.G.4
  • 30
    • 0027195094 scopus 로고
    • Catalytic centers in the thiamin diphosphate dependent enzyme pyruvate decarboxylase at 2.4 Aresolution
    • F. Dyda, W. Furey, S. Swaminathan, M. Sax, B. Farrenkopf, F. Jordan, Catalytic centers in the thiamin diphosphate dependent enzyme pyruvate decarboxylase at 2.4 Aresolution, Biochemistry 32 (1993) 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
  • 31
    • 0026785918 scopus 로고
    • Preparation of optically pure L-2-hydroxyaldehydes with yeast transketolase
    • F. Effenberger, V. Null, T. Ziegler, Preparation of optically pure L-2-hydroxyaldehydes with yeast transketolase, Tetrahedron Lett. 33 (1992) 5157-5160.
    • (1992) Tetrahedron Lett. , vol.33 , pp. 5157-5160
    • Effenberger, F.1    Null, V.2    Ziegler, T.3
  • 32
    • 0019888067 scopus 로고
    • Transketolase kinetics: The slow reconstitution of the holoenzyme is due to rate-limiting dimerization of the subunits
    • R.M. Egan, H.Z. Sable, 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
  • 33
    • 0000715324 scopus 로고
    • Dubois, Kinetics and thermodynamics of the structural transformations of thiamine in neutral and basic aqueous media. the UV spectrum of the tetrahedral pseudobase intermediate
    • J.M. El Hage, Chahine, J.E. Dubois, Kinetics and thermodynamics of the structural transformations of thiamine in neutral and basic aqueous media. The UV spectrum of the tetrahedral pseudobase intermediate, J. Am. Chem. Soc. 105 (1983) 2335-2340.
    • (1983) J. Am. Chem. Soc. , vol.105 , pp. 2335-2340
    • El Hage, J.M.1    Chahine, J.E.2
  • 34
    • 0020612907 scopus 로고
    • Expression of naphthalene oxidation genes in Escherichia coli: Results in the biosynthesis of indigo
    • B.D. Ensley, B.J. Ratzkin, T.D. Osslund, M.J. Simon, L.P. Wackelt, D.T. Gibson, Expression of naphthalene oxidation genes in Escherichia coli: results in the biosynthesis of indigo, Science 222 (1983) 167-169.
    • (1983) Science , vol.222 , pp. 167-169
    • Ensley, B.D.1    Ratzkin, B.J.2    Osslund, T.D.3    Simon, M.J.4    Wackelt, L.P.5    Gibson, D.T.6
  • 35
    • 0027447438 scopus 로고
    • Exchange reactions catalysed by grouptransferring enzymes oppose the quantitation and the unravelling of the identity of the pentose pathway
    • I. Flanigan, J.G. Collins, K.K. Arora, J.K. MacLeod, J.F. Williams, Exchange reactions catalysed by grouptransferring enzymes oppose the quantitation and the unravelling of the identity of the pentose pathway, Eur. J. Biochem. 213 (1993) 477-485.
    • (1993) Eur. J. Biochem. , vol.213 , pp. 477-485
    • Flanigan, I.1    Collins, J.G.2    Arora, K.K.3    MacLeod, J.K.4    Williams, J.F.5
  • 36
    • 0030294746 scopus 로고    scopus 로고
    • Molecular characterization of transketolase (EC 2.2.1.1) active in the Calvin cycle of spinach chloroplasts
    • A. Flechner, U. Dressen, P. Westhoff, K. Henze, C. Schnarrenberger, W. Martin, Molecular characterization of transketolase (EC 2.2.1.1) active in the Calvin cycle of spinach chloroplasts, Plant Mol. Biol. 32 (1996) 475-484.
    • (1996) Plant Mol. Biol. , vol.32 , pp. 475-484
    • Flechner, A.1    Dressen, U.2    Westhoff, P.3    Henze, K.4    Schnarrenberger, C.5    Martin, W.6
  • 38
    • 0010507308 scopus 로고
    • Structural and mechanistic aspects of catalysis by thiamin
    • E. E. van Tamelen (Eds.), Academic Press, New York
    • A. A. Gallo, J. J. Mieyal, H. Z. Sable, Structural and mechanistic aspects of catalysis by thiamin. in: E. E. van Tamelen (Eds.), Bioorganic chemistry, 4, Academic Press, New York, 1978, pp. 147-177.
    • (1978) Bioorganic Chemistry , vol.4 , pp. 147-177
    • Gallo, A.A.1    Mieyal, J.J.2    Sable, H.Z.3
  • 39
    • 0000641993 scopus 로고
    • From glucose to aromatics: Recent developments in natural products of the shikimic acid pathway
    • B. Ganem, From glucose to aromatics: recent developments in natural products of the shikimic acid pathway, Tetrahedron 34 (1978) 3353-3383.
    • (1978) Tetrahedron , vol.34 , pp. 3353-3383
    • Ganem, B.1
  • 40
    • 0344176792 scopus 로고
    • The mechanism of pentose phosphate conversion to hexose monophosphate. II: With pea leaf and pea root preparations
    • M. Gibbs, B.L. Horecker, The mechanism of pentose phosphate conversion to hexose monophosphate. II: with pea leaf and pea root preparations, J. Biol. Chem. 208 (1954) 813-820.
    • (1954) J. Biol. Chem. , vol.208 , pp. 813-820
    • Gibbs, M.1    Horecker, B.L.2
  • 41
    • 0021169712 scopus 로고
    • Correlations of enzymatic, metabolic, and behavioral deficits in thiamine deficiency and its reversal
    • G.E. Gibson, H. Ksiezak-Reding, K.F.R. Sheu, V. Mykytyn, J.P. Blass, Correlations of enzymatic, metabolic, and behavioral deficits in thiamine deficiency and its reversal, Neurochem. Res. 9 (1984) 803-814.
    • (1984) Neurochem. Res. , vol.9 , pp. 803-814
    • Gibson, G.E.1    Ksiezak-Reding, H.2    Sheu, K.F.R.3    Mykytyn, V.4    Blass, J.P.5
  • 42
    • 0023732664 scopus 로고
    • Reduced activities of thiamine-dependent enzymes in brains and peripheral tissues of Alzheimer's patients
    • G.E. Gibson, K.F.R. Sheu, A.C. Baker, K.C. Carlson, B. Harding, P. Perrino, J.P. Blass, Reduced activities of thiamine-dependent enzymes in brains and peripheral tissues of Alzheimer's patients, Arch. Neurol. 45 (1988) 836-840.
    • (1988) Arch. Neurol. , vol.45 , pp. 836-840
    • Gibson, G.E.1    Sheu, K.F.R.2    Baker, A.C.3    Carlson, K.C.4    Harding, B.5    Perrino, P.6    Blass, J.P.7
  • 43
    • 0024552754 scopus 로고
    • Regionally selective alterations in enzymatic activities and metabolic fluxes during thiamine deficiency
    • G.E. Gibson, P. Nielsen, V. Mykytyn, K. Carlson, J.P. Blass, Regionally selective alterations in enzymatic activities and metabolic fluxes during thiamine deficiency, Neurochem. Res. 14 (1989) 17-24.
    • (1989) Neurochem. Res. , vol.14 , pp. 17-24
    • Gibson, G.E.1    Nielsen, P.2    Mykytyn, V.3    Carlson, K.4    Blass, J.P.5
  • 44
    • 0023155048 scopus 로고
    • Activities of thiamine-dependent enzymes in two experimental models of thiamine-deficiency encephalopathy: 3 Transketolase
    • J.F. Giguere, R.F. Butterworth, Activities of thiamine-dependent enzymes in two experimental models of thiamine-deficiency encephalopathy: 3 Transketolase, Neurochem. Res. 12 (1987) 305-310.
    • (1987) Neurochem. Res. , vol.12 , pp. 305-310
    • Giguere, J.F.1    Butterworth, R.F.2
  • 47
    • 0029764209 scopus 로고    scopus 로고
    • A direct comparison of approaches for increasing carbon flow to aromatic biosynthesis in Escherlchla coll
    • G. Gösset, J. Yong-Xiao, A. Berry, A direct comparison of approaches for increasing carbon flow to aromatic biosynthesis in Escherlchla coll, J. Ind. Microbiol. 17 (1996) 47-52.
    • (1996) J. Ind. Microbiol. , vol.17 , pp. 47-52
    • Gösset, G.1    Yong-Xiao, J.2    Berry, A.3
  • 48
    • 0024539228 scopus 로고
    • Pyruvate decarboxylase is like acetolactate synthase (ILV2) and not like the pyruvate dehydrogenase El subunit
    • J.B.A. Green, Pyruvate decarboxylase is like acetolactate synthase (ILV2) and not like the pyruvate dehydrogenase El subunit, FEBS Lett. 246 (1989) 1-5.
    • (1989) FEBS Lett. , vol.246 , pp. 1-5
    • Green, J.B.A.1
  • 49
    • 0030991563 scopus 로고    scopus 로고
    • Heterogeneous expression of transketolase in ocular tissues
    • J. Guo, C.M. Sax, J. Piatigorsky, F.X. Yu, Heterogeneous expression of transketolase in ocular tissues, Curr. Eye Res. 16 (1997) 467-474.
    • (1997) Curr. Eye Res. , vol.16 , pp. 467-474
    • Guo, J.1    Sax, C.M.2    Piatigorsky, J.3    Yu, F.X.4
  • 50
    • 0031081566 scopus 로고    scopus 로고
    • Kinetics of overexpressed transketolase from Escherichia cou JM 107/pQR 700
    • M. Gyamerah, A.J. Willetts, Kinetics of overexpressed transketolase from Escherichia cou JM 107/pQR 700, Enzyme Microbial Technol. 20 (1997) 127-134.
    • (1997) Enzyme Microbial Technol. , vol.20 , pp. 127-134
    • Gyamerah, M.1    Willetts, A.J.2
  • 51
    • 0032516465 scopus 로고    scopus 로고
    • The crystal structure of benzoylformate decarboxylase at 1.6 Å resolution: Diversity of catalytic residues in thiamin diphosphate-dependent enzymes
    • M. S. Hasson, A. Museale, M. J. McLeish, L. S. Polovnikova, J. A. Gerlt, G. L. Kenyon, G. A. Petsko, D. Ringe, The crystal structure of benzoylformate decarboxylase at 1.6 Å resolution: diversity of catalytic residues in thiamin diphosphate-dependent enzymes, Biochemistry 37 (1998) 9918-9930.
    • (1998) Biochemistry , vol.37 , pp. 9918-9930
    • Hasson, M.S.1    Museale, A.2    McLeish, M.J.3    Polovnikova, L.S.4    Gerlt, J.A.5    Kenyon, G.L.6    Petsko, G.A.7    Ringe, D.8
  • 52
    • 0024432768 scopus 로고
    • A common structural motif in thiamin pyrophosphate-binding enzymes
    • C.F. Hawkins, A. Borges, R.N. Perham, 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
  • 53
    • 0028050130 scopus 로고
    • Chemoenzymatic synthesis of 6-deoxy-D-fructose and 6-deoxy-L-sorbose using transketolase
    • L. Hecquet, J. Bolte, C. Demuynck, Chemoenzymatic synthesis of 6-deoxy-D-fructose and 6-deoxy-L-sorbose using transketolase, Tetrahedron 50 (1994) 8677-8684.
    • (1994) Tetrahedron , vol.50 , pp. 8677-8684
    • Hecquet, L.1    Bolte, J.2    Demuynck, C.3
  • 54
    • 0029931442 scopus 로고    scopus 로고
    • Enzymatic synthesis of "natural-labeled" 6-deoxy-L-sorbose, precursor of an important food flavour
    • L. Hecquet, J. Bolte, C. Demuynck, Enzymatic synthesis of "natural-labeled" 6-deoxy-L-sorbose, precursor of an important food flavour, Tetrahedron 52 (1996) 8223-8232.
    • (1996) Tetrahedron , vol.52 , pp. 8223-8232
    • Hecquet, L.1    Bolte, J.2    Demuynck, C.3
  • 55
    • 0015229043 scopus 로고
    • A circular dichroism study of transketolase from baker's yeast
    • P.C. Heinrich, K. Noack, O. Wiss, 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
  • 56
    • 0015170516 scopus 로고
    • Transketolase from human erythrocyte: Purification and properties
    • P.C. Heinrich, O. Wiss, 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
  • 57
    • 0015497426 scopus 로고
    • Studies on the reconstitution of apotransketolase with thiamine pyrophosphate and analogs of the coenzyme
    • P.C. Heinrich, H. Steffen, P. Janser, O. Wiss, Studies on the reconstitution of apotransketolase with thiamine pyrophosphate and analogs of the coenzyme, Eur. J. Biochem. 30 (1972) 533-541.
    • (1972) Eur. J. Biochem. , vol.30 , pp. 533-541
    • Heinrich, P.C.1    Steffen, H.2    Janser, P.3    Wiss, O.4
  • 58
    • 0023760712 scopus 로고
    • Isolation of transketolase from human erythrocytes
    • S.D. Himmo, M. Thompson, C.J. Gubler, Isolation of transketolase from human erythrocytes, Prep. Biochem. 18 (1988) 261-276.
    • (1988) Prep. Biochem. , vol.18 , pp. 261-276
    • Himmo, S.D.1    Thompson, M.2    Gubler, C.J.3
  • 60
    • 0343182984 scopus 로고    scopus 로고
    • Enzyme-catalysed carbon-carbon bond formation: Large-scale production of Escherichia coll transketolase
    • G.R. Hobbs, R.K. Mitra, R.P. Chauhan, J.M. Woodley, M.D. Lilly, Enzyme-catalysed carbon-carbon bond formation: large-scale production of Escherichia coll transketolase, J. Biotechnol. 45 (1996) 173-179.
    • (1996) J. Biotechnol. , vol.45 , pp. 173-179
    • Hobbs, G.R.1    Mitra, R.K.2    Chauhan, R.P.3    Woodley, J.M.4    Lilly, M.D.5
  • 62
    • 0002168048 scopus 로고
    • Thiamin catalysis. 2. Kinetics and mechanism of the generation of the yellow form of thiamin
    • R.F.W. Hopmann, G.P. Brugnoni, B. Fol, Thiamin catalysis. 2. Kinetics and mechanism of the generation of the yellow form of thiamin, J. Am. Chem. Soc. 104 (1982) 1341-1344.
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 1341-1344
    • Hopmann, R.F.W.1    Brugnoni, G.P.2    Fol, B.3
  • 63
    • 0041845391 scopus 로고
    • The formation of sedoheptulose phosphate from pentose phosphate
    • B.L. Horecker, P.Z. Smyrniotis, H.J. Klenow, The formation of sedoheptulose phosphate from pentose phosphate, J. Biol. Chem. 205 (1953) 661-682.
    • (1953) J. Biol. Chem. , vol.205 , pp. 661-682
    • Horecker, B.L.1    Smyrniotis, P.Z.2    Klenow, H.J.3
  • 64
    • 0343498281 scopus 로고
    • The mechanism of pentose phosphate conversion to hexose monophosphate
    • B.L. Horecker, M. Gibbs, H. Klenow, P.Z. Smyrniotis, The mechanism of pentose phosphate conversion to hexose monophosphate, J. Biol. Chem. 207 (1954) 393-403.
    • (1954) J. Biol. Chem. , vol.207 , pp. 393-403
    • Horecker, B.L.1    Gibbs, M.2    Klenow, H.3    Smyrniotis, P.Z.4
  • 65
    • 33646276561 scopus 로고
    • The role of xylulose 5-phosphate in the transketolase reaction
    • B.L. Horecker, P.Z. Smyrniotis, J. Hurwitz, The role of xylulose 5-phosphate in the transketolase reaction, J. Biol. Chem. 223 (1956) 1009-1019.
    • (1956) J. Biol. Chem. , vol.223 , pp. 1009-1019
    • Horecker, B.L.1    Smyrniotis, P.Z.2    Hurwitz, J.3
  • 66
    • 0020332669 scopus 로고
    • Occurrence and significance of octulose phosphates in liver
    • B.L. Horecker, F. Paoletti, J.F. Williams, Occurrence and significance of octulose phosphates in liver, Ann. NY Acad. Sci. 378 (1982) 215-224.
    • (1982) Ann. NY Acad. Sci. , vol.378 , pp. 215-224
    • Horecker, B.L.1    Paoletti, F.2    Williams, J.F.3
  • 67
    • 37049072050 scopus 로고
    • Synthesis of enantiomerically pure α-hydroxyaldehydes from the corresponding α-hydroxycarboxylic acids: Novel substrates for Eschevlchla coll transketolase
    • A.J. Humphrey, N.J. Turner, R. McCague, S.J.C. Taylor, Synthesis of enantiomerically pure α-hydroxyaldehydes from the corresponding α-hydroxycarboxylic acids: novel substrates for Eschevlchla coll transketolase, J. Chem. Soc., Chem. Commun. (1995) 2475-2476.
    • (1995) J. Chem. Soc., Chem. Commun. , pp. 2475-2476
    • Humphrey, A.J.1    Turner, N.J.2    McCague, R.3    Taylor, S.J.C.4
  • 68
    • 0027218063 scopus 로고
    • Identification and characterization of the tktB gene encoding a second transketolase in Eschevlchla coli K-12
    • A. Iida, S. Teshiba, K. Mizobuchi, Identification and characterization of the tktB gene encoding a second transketolase in Eschevlchla coli K-12, J. Bacteriol. 175 (1993) 5375-5383.
    • (1993) J. Bacteriol. , vol.175 , pp. 5375-5383
    • Iida, A.1    Teshiba, S.2    Mizobuchi, K.3
  • 69
    • 0031039891 scopus 로고    scopus 로고
    • Analysis of a transketolase gene from Kluyveromyces lactis reveals that the yeast enzymes are more related to transketolases of prokaryotic origins than those of higher eukaryotes
    • J.J. Jacoby, J.J. Heinisch, Analysis of a transketolase gene from Kluyveromyces lactis reveals that the yeast enzymes are more related to transketolases of prokaryotic origins than those of higher eukaryotes, Curr. Genet. 31 (1997) 15-21.
    • (1997) Curr. Genet. , vol.31 , pp. 15-21
    • Jacoby, J.J.1    Heinisch, J.J.2
  • 70
    • 0022422652 scopus 로고
    • Cloning and characterisation of DAS gene encoding the major methanol assimilatory enzyme from the methylotrophic yeast Hansenula polymorpha
    • Z.A. Janowicz, M.R. Eckart, C. Drewke, R.O. Roggenkamp, C.P. Hollenberg, Cloning and characterisation of DAS gene encoding the major methanol assimilatory enzyme from the methylotrophic yeast Hansenula polymorpha, Nucl. Acids Res. 13 (1985) 3043-3062.
    • (1985) Nucl. Acids Res. , vol.13 , pp. 3043-3062
    • Janowicz, Z.A.1    Eckart, M.R.2    Drewke, C.3    Roggenkamp, R.O.4    Hollenberg, C.P.5
  • 72
    • 33646276883 scopus 로고
    • The isolation of the anti beri beri vitamin
    • Reprinted as: The isolation of the anti beri beri vitamin, Nutr. Rev., 40, (1982) 53-55.
    • (1982) Nutr. Rev. , vol.40 , pp. 53-55
  • 73
    • 0024245077 scopus 로고
    • Studies on the nature of thiamin pyrophosphate binding and dependency on divalent cations of transketolase from human erythrocytes
    • E.H. Jung, T. Takeuchi, K. Nishino, Y. Itokawa, Studies on the nature of thiamin pyrophosphate binding and dependency on divalent cations of transketolase from human erythrocytes, Int. J. Biochem. 20 (1988) 1255-1259.
    • (1988) Int. J. Biochem. , vol.20 , pp. 1255-1259
    • Jung, E.H.1    Takeuchi, T.2    Nishino, K.3    Itokawa, Y.4
  • 74
    • 0020586198 scopus 로고
    • Variants of transketolase from human erythrocytes
    • M.J. Kaczmarek, P.P. Nixon, Variants of transketolase from human erythrocytes, Clin. Chim. Acta 130 (1983) 349-356.
    • (1983) Clin. Chim. Acta , vol.130 , pp. 349-356
    • Kaczmarek, M.J.1    Nixon, P.P.2
  • 75
    • 0019972145 scopus 로고
    • Purification and properties of a transketolase responsible for formaldehyde fixation in a methanol-utilising yeast, Candida boidinii (Kloeckera sp No. 2201)
    • N. Kato, T. Higuchi, C. Sakazawa, T. Nishizawa, Y. Tani, H. Yamada, Purification and properties of a transketolase responsible for formaldehyde fixation in a methanol-utilising yeast, Candida boidinii (Kloeckera sp No. 2201), Biochim. Biophys. Acta 715 (1982) 143-150.
    • (1982) Biochim. Biophys. Acta , vol.715 , pp. 143-150
    • Kato, N.1    Higuchi, T.2    Sakazawa, C.3    Nishizawa, T.4    Tani, Y.5    Yamada, H.6
  • 76
    • 0023122461 scopus 로고
    • Human erythrocyte transketolase: No evidence for variants
    • A. Kaufmann, S. Uhlhaas, W. Friedl, P. Propping, Human erythrocyte transketolase: no evidence for variants, Clin. Chim. Acta 162 (1987) 215-219.
    • (1987) Clin. Chim. Acta , vol.162 , pp. 215-219
    • Kaufmann, A.1    Uhlhaas, S.2    Friedl, W.3    Propping, P.4
  • 77
    • 0022966556 scopus 로고
    • The rapid decline in erythrocyte transketolase on cessation of high-dose thiamine administration in Korsakoff patients
    • R.A. Kerr, A.E. Clague, D.J. Morris, J. Price, The rapid decline in erythrocyte transketolase on cessation of high-dose thiamine administration in Korsakoff patients, Alcohol Alcohol 21 (1986) 257-262.
    • (1986) Alcohol Alcohol , vol.21 , pp. 257-262
    • Kerr, R.A.1    Clague, A.E.2    Morris, D.J.3    Price, J.4
  • 78
    • 0014501523 scopus 로고
    • The purification of transketolase from Candida utilis
    • M.E. Kiely, E.L. Tan, T. Wood, The purification of transketolase from Candida utilis, Can. J. Biochem. 47 (1969) 455-460.
    • (1969) Can. J. Biochem. , vol.47 , pp. 455-460
    • Kiely, M.E.1    Tan, E.L.2    Wood, T.3
  • 79
    • 0002730564 scopus 로고
    • Pathways of glucose metabolism in corneal epithelium
    • J.H. Kinoshita, T. Masurat, M. Helfant, Pathways of glucose metabolism in corneal epithelium, Science 122 (1955) 72-73.
    • (1955) Science , vol.122 , pp. 72-73
    • Kinoshita, J.H.1    Masurat, T.2    Helfant, M.3
  • 80
    • 0017610323 scopus 로고
    • Purification and properties of transketolase from Candida utilis, Hoppe-Seyler's
    • H. Klein, K. Brand, Purification and properties of transketolase from Candida utilis, Hoppe-Seyler's Z. Physiol. Chem. 358 (1977) 1325-1337.
    • (1977) Z. Physiol. Chem. , vol.358 , pp. 1325-1337
    • Klein, H.1    Brand, K.2
  • 81
    • 33845283300 scopus 로고
    • Thiamine diphosphate: A mechanistic update on enzymic and nonenzymic catalysis of decarboxylation
    • R. Kluger, Thiamine diphosphate: a mechanistic update on enzymic and nonenzymic catalysis of decarboxylation, Chem. Rev. 87 (1987) 863-876.
    • (1987) Chem. Rev. , vol.87 , pp. 863-876
    • Kluger, R.1
  • 82
    • 0018195667 scopus 로고
    • Isolation of transketolase from the rat liver and some of its properties
    • G.A. Kochetov, A.A. Minin, Isolation of transketolase from the rat liver and some of its properties, Biokhimiya 43 (1978) 1631-1635.
    • (1978) Biokhimiya , vol.43 , pp. 1631-1635
    • Kochetov, G.A.1    Minin, A.A.2
  • 83
    • 0020393767 scopus 로고
    • Transketolase from yeast, rat liver and pig liver
    • G.A. Kochetov, Transketolase from yeast, rat liver and pig liver, Methods. Enzymol. 90 (1982) 209-223.
    • (1982) Methods. Enzymol. , vol.90 , pp. 209-223
    • Kochetov, G.A.1
  • 84
    • 0042492718 scopus 로고
    • Structure and mechanism of action of transketolase
    • G.A. Kochetov, Structure and mechanism of action of transketolase, Biokhimiya 51 (1986) 2020-2029.
    • (1986) Biokhimiya , vol.51 , pp. 2020-2029
    • Kochetov, G.A.1
  • 85
    • 0028292158 scopus 로고
    • Specificity of coenzyme binding in thiamin diphosphate-dependent enzymes
    • S. König, A. Schellenberger, H. Neef, G. Schneider, Specificity of coenzyme binding in thiamin diphosphate-dependent enzymes, J. Biol. Chem. 269 (1994) 10879-10882.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10879-10882
    • König, S.1    Schellenberger, A.2    Neef, H.3    Schneider, G.4
  • 86
  • 88
    • 0018916632 scopus 로고
    • Determination of half-life for the key enzymes of the pentose phosphate pathway-glucose 6-phosphate dehydrogenase and trans-ketolase
    • G.V. Kudryavtseva, I.I. Denisova, Determination of half-life for the key enzymes of the pentose phosphate pathway-glucose 6-phosphate dehydrogenase and trans-ketolase, Biokhimiya 45 (1980) 118-123.
    • (1980) Biokhimiya , vol.45 , pp. 118-123
    • Kudryavtseva, G.V.1    Denisova, I.I.2
  • 89
    • 0344176774 scopus 로고
    • Quantitative histochemical changes in the development of the rat lens and cornea
    • R.E. Kuhlman, R.A. Resnick, Quantitative histochemical changes in the development of the rat lens and cornea, Am. J. Ophthal. 46 (1958) 47-55.
    • (1958) Am. J. Ophthal. , vol.46 , pp. 47-55
    • Kuhlman, R.E.1    Resnick, R.A.2
  • 91
    • 0027687871 scopus 로고
    • Crystallization of three forms of baker's yeast transketolase
    • A.N. Kuimov, N.V. Konareva, M.Y. Filippov, Crystallization of three forms of baker's yeast transketolase, Biokhimiya 58 (1994) 1820-1829.
    • (1994) Biokhimiya , vol.58 , pp. 1820-1829
    • Kuimov, A.N.1    Konareva, N.V.2    Filippov, M.Y.3
  • 92
    • 0021028796 scopus 로고
    • The pentose cycle in animal tissues: Evidence for the classical and against the "L-type" pathway, Trends
    • B.R. Landau, H.G. Wood, The pentose cycle in animal tissues: evidence for the classical and against the "L-type" pathway, Trends Biochem. Sci 8 (1983) 292-296.
    • (1983) Biochem. Sci , vol.8 , pp. 292-296
    • Landau, B.R.1    Wood, H.G.2
  • 94
    • 0026762799 scopus 로고
    • Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 Å resolution
    • Y. Lindqvist, G. Schneider, U. Ermler, M. Sundström, Three-dimensional structure of transketolase, a thiamine diphosphate dependent enzyme, at 2.5 Å resolution, EMBO J. 11 (1992) 2373-2379.
    • (1992) EMBO J. , vol.11 , pp. 2373-2379
    • Lindqvist G, Y.1    Schneider, U.2    Ermler, M.3    Sundström4
  • 95
    • 0029199270 scopus 로고
    • Crystallization and preliminary X-ray crystallographic data with Escherlchla coll trans-ketolase
    • J.A. Littlechild, N.J. Turner, G.R. Hobbs, M.D. Lilly, R. Rawas, W. Watson, Crystallization and preliminary X-ray crystallographic data with Escherlchla coll trans-ketolase, Acta Cryst. D51 (1995) 1074-1076.
    • (1995) Acta Cryst. , vol.D51 , 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
  • 96
    • 0000268064 scopus 로고
    • Über das Vorkommen der Adenin-Nukleotide in den Geweben. I Das Vorkommen in der quergestreiften Muskulatur von Wirbeltieren und Wirbellosen
    • K. Lohmann, P. Schuster, Über das Vorkommen der Adenin-Nukleotide in den Geweben. I Das Vorkommen in der quergestreiften Muskulatur von Wirbeltieren und Wirbellosen, Biochem. Z. 294 (1937) 188-214.
    • (1937) Biochem. Z. , vol.294 , pp. 188-214
    • Lohmann, K.1    Schuster, P.2
  • 97
    • 0031013443 scopus 로고    scopus 로고
    • Metabolic engineering and control analysis for production of aromatics: Role of transaldolase
    • J.L. Lu, J.C. Liao, Metabolic engineering and control analysis for production of aromatics: role of transaldolase, Biotechnol. Bioeng. 53 (1997) 132-138.
    • (1997) Biotechnol. Bioeng. , vol.53 , pp. 132-138
    • Lu, J.L.1    Liao, J.C.2
  • 98
    • 33947462225 scopus 로고
    • Structures of thiamine in basic solution
    • G.D. Maier, D.E. Metzler, Structures of thiamine in basic solution, J. Am. Chem. Soc. 79 (1957) 4386-4391.
    • (1957) J. Am. Chem. Soc. , vol.79 , pp. 4386-4391
    • Maier, G.D.1    Metzler, D.E.2
  • 99
    • 0023778790 scopus 로고
    • Isolation of transketolase from rabbit liver and comparison of some of its kinetic properties with transketolase from other sources
    • S.W. Masri, M. Ali, C.J. Gubler, Isolation of transketolase from rabbit liver and comparison of some of its kinetic properties with transketolase from other sources, Comp. Biochem. Physiol. 90B (1988) 167-172.
    • (1988) Comp. Biochem. Physiol. , vol.90 B , pp. 167-172
    • Masri, S.W.1    Ali, M.2    Gubler, C.J.3
  • 100
    • 0014341180 scopus 로고
    • Encephalopathy of thiamine deficiency: Studies of intracerebral mechanisms
    • D.W. McCandless, S. Schenker, Encephalopathy of thiamine deficiency: studies of intracerebral mechanisms, J. Clin. Invest. 47 (1968) 2268-2280.
    • (1968) J. Clin. Invest. , vol.47 , pp. 2268-2280
    • McCandless, D.W.1    Schenker, S.2
  • 101
    • 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
    • B.A. McCool, S.G. Plonk, P.R. Martin, C.K. Singleton, 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
  • 102
    • 0031039575 scopus 로고    scopus 로고
    • Examination of the thiamin diphosphate binding site in yeast transketolase by site-directed mutagenesis
    • L. Meshalkina, U. Nilsson, C. Wikner, T. Kostikowa, G. Schneider, Examination of the thiamin diphosphate binding site in yeast transketolase by site-directed mutagenesis, Eur. J. Biochem. 244 (1997) 646-652.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 646-652
    • Meshalkina, L.1    Nilsson, U.2    Wikner, C.3    Kostikowa, T.4    Schneider, G.5
  • 103
    • 0028029844 scopus 로고
    • Isolation and characterization of the Pichia stipitis transketolase gene and expression in a xylose-utilising Saccharomyces cerevisiae transformant
    • M.H. Metzger, C.P. Hollenberg, Isolation and characterization of the Pichia stipitis transketolase gene and expression in a xylose-utilising Saccharomyces cerevisiae transformant, Appl. Microbiol. Biotechnol. 42 (1994) 319-325.
    • (1994) Appl. Microbiol. Biotechnol. , vol.42 , pp. 319-325
    • Metzger, M.H.1    Hollenberg, C.P.2
  • 104
    • 0031973750 scopus 로고    scopus 로고
    • Escherichia coli transketolase-catalyzed carbon-carbon bond formation: Biotransformation characterization for reactor evaluation and selection
    • R.K. Mitra, J.M. Woodley, M.D. Lilly, Escherichia coli transketolase-catalyzed carbon-carbon bond formation: biotransformation characterization for reactor evaluation and selection, Enzyme Microb. Technol. 22 (1998) 64-70.
    • (1998) Enzyme Microb. Technol. , vol.22 , pp. 64-70
    • Mitra, R.K.1    Woodley, J.M.2    Lilly, M.D.3
  • 105
    • 0001417463 scopus 로고
    • Mechanism of thiamine-catalysed reactions
    • S. Mizuhara, P. Handler, Mechanism of thiamine-catalysed reactions, J. Am. Chem. Soc. 76 (1954) 571-573.
    • (1954) J. Am. Chem. Soc. , vol.76 , pp. 571-573
    • Mizuhara, S.1    Handler, P.2
  • 106
    • 0024514172 scopus 로고
    • Transketolase from human leukocytes. Isolation, properties and induction of polyclonal antibodies
    • A. Mocali, F. Paoletti, Transketolase from human leukocytes. Isolation, properties and induction of polyclonal antibodies, Eur. J. Biochem. 180 (1989) 213-219.
    • (1989) Eur. J. Biochem. , vol.180 , pp. 213-219
    • Mocali, A.1    Paoletti, F.2
  • 107
    • 0030220903 scopus 로고    scopus 로고
    • Transketolase from Escherlchla coli: A practical procedure for using the biocatalyst for asymmetric carbon-carbon bond synthesis
    • K.G. Morris, M.E.B. Smith, N.J. Turner, M.D. Lilly, R.K. Mitra, J.M. Woodley, Transketolase from Escherlchla coli: a practical procedure for using the biocatalyst for asymmetric carbon-carbon bond synthesis, Tetrahedron: Asymmetry 7 (1996) 2185-2188.
    • (1996) Tetrahedron: Asymmetry , vol.7 , pp. 2185-2188
    • Morris, K.G.1    Smith, M.E.B.2    Turner, N.J.3    Lilly, M.D.4    Mitra, R.K.5    Woodley, J.M.6
  • 109
    • 0027479683 scopus 로고
    • Structure of the thiamineand flavin-dependent enzyme pyruvate oxidase
    • Y.A. Müller, G.E. Schulz, Structure of the thiamineand flavin-dependent enzyme pyruvate oxidase, Science 259 (1993) 965-967.
    • (1993) Science , vol.259 , pp. 965-967
    • Müller, Y.A.1    Schulz, G.E.2
  • 110
    • 0027918180 scopus 로고
    • A thiamin diphosphate binding fold revealed by comparison of the crystal structures of transketolase, pyruvate oxidase and pyruvate decarboxylase
    • Y.A. Müller, Y. Lindqvist, W. Furey, G.E. Schulz, F. Jordan, G. Schneider, 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
    • Müller, Y.A.1    Lindqvist, Y.2    Furey, W.3    Schulz, G.E.4    Jordan, F.5    Schneider, G.6
  • 112
    • 0028305456 scopus 로고
    • Refined structure of transketolase from Saccharomyces cerevisiae at 2.0 Å resolution
    • M. Nikkola, Y. Lindqvist, G. Schneider, 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
  • 113
    • 0031029945 scopus 로고    scopus 로고
    • Examination of substrate binding in thiamin diphosphate-dependent transketolase by protein crystallography and site-directed mutagenesis
    • U. Nilsson, L. Meshalkina, Y. Lindqvist, G. Schneider, Examination of substrate binding in thiamin diphosphate-dependent transketolase by protein crystallography and site-directed mutagenesis, J. Biol. Chem. 272 (1997) 1864-1869.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1864-1869
    • Nilsson, U.1    Meshalkina, L.2    Lindqvist, Y.3    Schneider, G.4
  • 114
    • 0021195980 scopus 로고
    • An erythrocyte transketolase isoenzyme pattern associated with the Wernicke-Korsakoff syndrome
    • P.P. Nixon, M.J. Kaczmareck, J.R. Tate, R.A. Kerr, J. Price, An erythrocyte transketolase isoenzyme pattern associated with the Wernicke-Korsakoff syndrome, Eur. J. Clin. Invest. 14 (1984) 278-281.
    • (1984) Eur. J. Clin. Invest. , vol.14 , pp. 278-281
    • Nixon, P.P.1    Kaczmareck, M.J.2    Tate, J.R.3    Kerr, R.A.4    Price, J.5
  • 115
    • 0025010544 scopus 로고
    • The relationship between erythrocyte trans-ketolase activity and the "TPP effect" in Wernicke's encephalopathy and other thiamine deficiency states
    • P.F. Nixon, J. Price, M. Norman-Hick, G.M. Williams, R.A. Kerr, The relationship between erythrocyte trans-ketolase activity and the "TPP effect" in Wernicke's encephalopathy and other thiamine deficiency states, Clin. Chim. Acta 192 (1990) 89-98.
    • (1990) Clin. Chim. Acta , vol.192 , pp. 89-98
    • Nixon, P.F.1    Price, J.2    Norman-Hick, M.3    Williams, G.M.4    Kerr, R.A.5
  • 116
    • 0021103912 scopus 로고
    • Purification and properties of transketolase from fresh rat liver
    • P. Paoletti, Purification and properties of transketolase from fresh rat liver, Arch. Biochem. Biophys. 222 (1983) 489-496.
    • (1983) Arch. Biochem. Biophys. , vol.222 , pp. 489-496
    • Paoletti, P.1
  • 117
    • 0022453792 scopus 로고
    • Immunoaffinity purification of rat liver transketolase: Evidence for multiple forms of the enzyme
    • P. Paoletti, D. Aldinucci, Immunoaffinity purification of rat liver transketolase: evidence for multiple forms of the enzyme, Arch. Biochem. Biophys. 245 (1986) 212-219.
    • (1986) Arch. Biochem. Biophys. , vol.245 , pp. 212-219
    • Paoletti, P.1    Aldinucci, D.2
  • 118
    • 0025183676 scopus 로고
    • Occurrence of transketolase abnormalities in extracts of foreskin fibroblasts from patients with Alzheimer's disease
    • P. Paoletti, A. Mocali, M. Marchi, S. Sorbi, S. Piacentini, Occurrence of transketolase abnormalities in extracts of foreskin fibroblasts from patients with Alzheimer's disease, Biochem. Biophys. Res. Commun. 172 (1990) 396-401.
    • (1990) Biochem. Biophys. Res. Commun. , vol.172 , pp. 396-401
    • Paoletti, P.1    Mocali, A.2    Marchi, M.3    Sorbi, S.4    Piacentini, S.5
  • 119
    • 0030788993 scopus 로고    scopus 로고
    • Cysteine proteinases are responsible for characteristic transketolase alterations in Alzheimer fibroblasts
    • P. Paoletti, A. Mocali, D. Tombaccini, Cysteine proteinases are responsible for characteristic transketolase alterations in Alzheimer fibroblasts, J. Cell. Physiol. 172 (1997) 63-68.
    • (1997) J. Cell. Physiol. , vol.172 , pp. 63-68
    • Paoletti, P.1    Mocali, A.2    Tombaccini, D.3
  • 120
    • 0030014522 scopus 로고    scopus 로고
    • Thiamine pyrophosphate-requiring enzymes are altered during pyrithiamine-induced thiamine deficiency in cultured human lymphoblasts
    • S.R. Pekovich, P.R. Martin, C.K. Singleton, Thiamine pyrophosphate-requiring enzymes are altered during pyrithiamine-induced thiamine deficiency in cultured human lymphoblasts, J. Nutr. 126 (1996) 1791-1798.
    • (1996) J. Nutr. , vol.126 , pp. 1791-1798
    • Pekovich, S.R.1    Martin, P.R.2    Singleton, C.K.3
  • 122
    • 0001037029 scopus 로고
    • Biosynthesis of the aromatic amino acids
    • F.C. Neidhardt (Ed.), Chapter 24, American Society of Microbiology, Washington, DC
    • A. J. Pittard, Biosynthesis of the aromatic amino acids. In: F.C. Neidhardt (Ed.), Escherichia coli and Salmonella typhimurium, Vol. 1, Chapter 24, American Society of Microbiology, Washington, DC, 1987.
    • (1987) Escherichia Coli and Salmonella Typhimurium , vol.1
    • Pittard, A.J.1
  • 123
    • 0030630059 scopus 로고    scopus 로고
    • Protein design on pyruvate decarboxylase (PDC) by site-directed mutagenesis. Application to mechanistical investigations, and tailoring PDC for the use in organic synthesis
    • M. Pohl, Protein design on pyruvate decarboxylase (PDC) by site-directed mutagenesis. Application to mechanistical investigations, and tailoring PDC for the use in organic synthesis, Adv. Biochem. Eng./Biotechnol. 58 (1997) 15-43.
    • (1997) Adv. Biochem. Eng./Biotechnol. , vol.58 , pp. 15-43
    • Pohl, M.1
  • 124
    • 0026008875 scopus 로고
    • In thiamine deficiency, activation of erythrocyte transketolase by thiamine in vivo exceeds activation by cofactor in vitro
    • J. Price, A.E. Clague, R.A. Kerr, P.P. Nixon, In thiamine deficiency, activation of erythrocyte transketolase by thiamine in vivo exceeds activation by cofactor in vitro, Clin. Chim. Acta 202 (1991) 39-45.
    • (1991) Clin. Chim. Acta , vol.202 , pp. 39-45
    • Price, J.1    Clague, A.E.2    Kerr, R.A.3    Nixon, P.P.4
  • 125
    • 0001382345 scopus 로고
    • Thiaminpyrophosphate, a coenzyme of transketolase
    • E. Racker, G. de la Haba, J.G. Leder, Thiaminpyrophosphate, a coenzyme of transketolase, J. Am. Chem. Soc. 75 (1953) 1010-1011.
    • (1953) J. Am. Chem. Soc. , vol.75 , pp. 1010-1011
    • Racker, E.1    De La Haba, G.2    Leder, J.G.3
  • 126
    • 0001619883 scopus 로고
    • Transketolase
    • P. D. Boyer, H. Lardy, E. Myrback (Eds.), V, Academic Press, New York
    • E. Racker, Transketolase. in: P. D. Boyer, H. Lardy, E. Myrback (Eds.), The Enzymes, V, Academic Press, New York, 1961, pp. 397-406.
    • (1961) The Enzymes , pp. 397-406
    • Racker, E.1
  • 127
    • 0025299079 scopus 로고
    • Genetic transformation in Streptococcus pneumonias: Nucleotide sequence and predicted amino acid sequence of recP
    • B.A. Radnis, D.K. Rhee, D.A. Morrison, Genetic transformation in Streptococcus pneumonias: nucleotide sequence and predicted amino acid sequence of recP, J. Bacteriol. 172 (1990) 3669-3674.
    • (1990) J. Bacteriol. , vol.172 , pp. 3669-3674
    • Radnis, B.A.1    Rhee, D.K.2    Morrison, D.A.3
  • 128
    • 0024040341 scopus 로고
    • Comparison of the structural genes for pyruvate decarboxylase in different Zymomonas strains
    • M. Reynen, H. Sahm, Comparison of the structural genes for pyruvate decarboxylase in different Zymomonas strains, J. Bacteriol. 170 (1988) 3310-3313.
    • (1988) J. Bacteriol. , vol.170 , pp. 3310-3313
    • Reynen, M.1    Sahm, H.2
  • 129
    • 0030930082 scopus 로고    scopus 로고
    • Dihydroxyacetone synthase from a methanol-utilizing carboxydobacterium, Acetinobacter sp. strain JC1 DSM 3803
    • Y.T. Ro, C.Y. Eom, T. Song, J.W. Cho, Y.M. Kim, Dihydroxyacetone synthase from a methanol-utilizing carboxydobacterium, Acetinobacter sp. strain JC1 DSM 3803, J. Bacteriol. 179 (1997) 6041-6047.
    • (1997) J. Bacteriol. , vol.179 , pp. 6041-6047
    • Ro, Y.T.1    Eom, C.Y.2    Song, T.3    Cho, J.W.4    Kim, Y.M.5
  • 130
    • 0027265567 scopus 로고
    • The relationship between transketolase, yeast pyruvate decarboxylase and pyruvate dehydrogenase of the pyruvate dehydrogenase complex
    • B.H. Robinson, K. Chun, The relationship between transketolase, yeast pyruvate decarboxylase and pyruvate dehydrogenase of the pyruvate dehydrogenase complex, FEBS Lett. 328 (1993) 99-102.
    • (1993) FEBS Lett. , vol.328 , pp. 99-102
    • Robinson, B.H.1    Chun, K.2
  • 131
    • 0015978190 scopus 로고
    • The purification and some properties of brewer's yeast apotransketolase
    • S. Saitou, T. Ozawa, I. Tomita, The purification and some properties of brewer's yeast apotransketolase, FEBS Lett. 40 (1974) 114-118.
    • (1974) FEBS Lett. , vol.40 , pp. 114-118
    • Saitou, S.1    Ozawa, T.2    Tomita, I.3
  • 132
    • 0030463225 scopus 로고    scopus 로고
    • Transketolase: A cornea crystallin which is abundantly and differentially expressed in the developing mouse cornea
    • C.M. Sax, C. Salmon, W. Keys, J. Guo, F.X. Yu, J. Piatigorsky, Transketolase: a cornea crystallin which is abundantly and differentially expressed in the developing mouse cornea, J. Biol. Chem. 271 (1996) 33568-33574.
    • (1996) J. Biol. Chem. , vol.271 , pp. 33568-33574
    • Sax, C.M.1    Salmon, C.2    Keys, W.3    Guo, J.4    Yu, F.X.5    Piatigorsky, J.6
  • 133
    • 0027494279 scopus 로고
    • Pentosephosphate pathway in Saccharomyces cerevisiae: Analysis of deletion mutants for transketolase, transaldolase, and glucose 6-phosphate dehydrogenase
    • I. Schaaf-Gerstenschläger, F.K. Zimmermann, Pentosephosphate pathway in Saccharomyces cerevisiae: analysis of deletion mutants for transketolase, transaldolase, and glucose 6-phosphate dehydrogenase, Curr Genet 24 (1993) 373-376.
    • (1993) Curr Genet , vol.24 , pp. 373-376
    • Schaaf-Gerstenschläger, I.1    Zimmermann, F.K.2
  • 135
    • 0027433252 scopus 로고
    • The cbb operons of the facultative chemoautotroph Alcaligenes eutrophus encode phosphoglycolate phosphatase
    • J. Schäferjohann, J.G. Yoo, B. Kusian, B. Bowien, The cbb operons of the facultative chemoautotroph Alcaligenes eutrophus encode phosphoglycolate phosphatase, J. Bacteriol. 175 (1993) 7329-7340.
    • (1993) J. Bacteriol. , vol.175 , pp. 7329-7340
    • Schäferjohann, J.1    Yoo, J.G.2    Kusian, B.3    Bowien, B.4
  • 137
    • 0000170889 scopus 로고
    • Die Funktion der 4′-Aminopyrimidin-Komponente im Katalysemechanismus von Thiaminpyrophosphat-Enzymen aus heutiger Sicht
    • A. Schellenberger, Die Funktion der 4′-Aminopyrimidin-Komponente im Katalysemechanismus von Thiaminpyrophosphat-Enzymen aus heutiger Sicht, Chem. Ber. 123 (1990) 1489-1494.
    • (1990) Chem. Ber. , vol.123 , pp. 1489-1494
    • Schellenberger, A.1
  • 139
    • 0031001809 scopus 로고    scopus 로고
    • Molecular evolutionary analysis of the thiamin diphosphate-dependent enzyme, transketolase
    • G. Schenk, R. Layfield, J.M. Candy, R.G. Duggleby, P.P. Nixon, 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.P.5
  • 140
    • 0030874266 scopus 로고    scopus 로고
    • The role of His 113 and His 114 in pyruvate decarboxylase from Zymomonas mobilis
    • G. Schenk, F.J. Leeper, R. England, P.F. Nixon, R.G. Duggleby, The role of His 113 and His 114 in pyruvate decarboxylase from Zymomonas mobilis, Eur. J. Biochem. 248 (1997) 63-71.
    • (1997) Eur. J. Biochem. , vol.248 , pp. 63-71
    • Schenk, G.1    Leeper, F.J.2    England, R.3    Nixon, P.F.4    Duggleby, R.G.5
  • 142
    • 0029962793 scopus 로고    scopus 로고
    • Amplification of the transketolase gene in desensitization-resistant mutant Y1 mouse adrenocortical tumor cells
    • B.P. Schimmer, J. Tsao, W. Czerwinski, Amplification of the transketolase gene in desensitization-resistant mutant Y1 mouse adrenocortical tumor cells, J. Biol. Chem. 271 (1996) 4993-4998.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4993-4998
    • Schimmer, B.P.1    Tsao, J.2    Czerwinski, W.3
  • 143
    • 0027280383 scopus 로고
    • Enzymatic thiamine catalysis: Mechanistic implications from the three-dimensional structure of transketolase
    • G. Schneider, Y. Lindqvist, Enzymatic thiamine catalysis: mechanistic implications from the three-dimensional structure of transketolase, Bioorg. Chem 21 (1993) 109-117.
    • (1993) Bioorg. Chem , vol.21 , pp. 109-117
    • Schneider, G.1    Lindqvist, Y.2
  • 144
    • 0031111906 scopus 로고    scopus 로고
    • Determination of constants of substrate primary binding with baker's yeast transketolase by kinetic modelling
    • V.A. Selivanov, L.M. Meshalkina, M.V. Kovina, G.A. Kochetov, Determination of constants of substrate primary binding with baker's yeast transketolase by kinetic modelling, Biokhimiya 62 (1997) 425-432.
    • (1997) Biokhimiya , vol.62 , pp. 425-432
    • Selivanov, V.A.1    Meshalkina, L.M.2    Kovina, M.V.3    Kochetov, G.A.4
  • 145
    • 0025857432 scopus 로고
    • Effects of increased transaldolase activity on D-xylulose and D-glucose metabolism in Saccharomyces cerevisiae cell extracts
    • T. Senac, B. Hahn-Hägerdahl, 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
  • 147
  • 148
    • 33646302561 scopus 로고
    • Preparation and properties of transketolase from pork liver
    • F. Simpson, Preparation and properties of transketolase from pork liver, Can. J. Biochem. Physiol. 38 (1960) 115-124.
    • (1960) Can. J. Biochem. Physiol. , vol.38 , pp. 115-124
    • Simpson, F.1
  • 149
    • 0028893623 scopus 로고
    • The thiamine-dependent hysteretic behaviour of human transketolase: Implications for thiamine deficiency
    • C.K. Singleton, S.R. Pekovich, B.A. McCool, P.R. Martin, 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
  • 150
    • 0029770049 scopus 로고    scopus 로고
    • Conserved residues are functionally distinct within transketolases of different species
    • C.K. Singleton, J.J.L. Wang, L. Shan, P.R. Martin, 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
  • 151
    • 0015086056 scopus 로고
    • A NADH-dependent transketolase assay in erythrocyte hemolysates
    • E.H.J. Smeets, H. Muller, J. de Wael, 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
  • 152
    • 0345470658 scopus 로고    scopus 로고
    • In vitro phosphorylation of purified transketolase by protein kinase C
    • Y. Soh, K.S. Jeong, In vitro phosphorylation of purified transketolase by protein kinase C, Mol. Cells 6 (1996) 692-696.
    • (1996) Mol. Cells , vol.6 , pp. 692-696
    • Soh, Y.1    Jeong, K.S.2
  • 153
    • 0027420528 scopus 로고
    • Nucleotide sequence of the Escherichia coll K-12 transketolase (tkt) gene
    • G.A. Sprenger, Nucleotide sequence of the Escherichia coll K-12 transketolase (tkt) gene, Biochim. Biophys. Acta 1216 (1993) 307-310.
    • (1993) Biochim. Biophys. Acta , vol.1216 , pp. 307-310
    • Sprenger, G.A.1
  • 154
    • 0029067816 scopus 로고
    • Transketolase a of Escherichia coli K12. Purification and properties of the enzyme from recombinant strains
    • G.A. Sprenger, U. Schörken, G. Sprenger, H. Sahm, 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
  • 155
    • 0001331116 scopus 로고
    • The oxidative pentose-phosphate cycle. I. Preparation of substrates and enzymes
    • P. Srere, J.R. Cooper, M. Tabachnick, E. Racker, The oxidative pentose-phosphate cycle. I. Preparation of substrates and enzymes, Arch. Biochem. Biophys. 74 (1958) 295-305.
    • (1958) Arch. Biochem. Biophys. , vol.74 , pp. 295-305
    • Srere, P.1    Cooper, J.R.2    Tabachnick, M.3    Racker, E.4
  • 156
    • 0027515306 scopus 로고
    • Yeast TKL1 gene encodes a trans-ketolase that is required for efficient glycolysis and biosynthesis of aromatic amino acids
    • M. Sundström, Y. Lindqvist, G. Schneider, U. Hellman, H. Rönne, Yeast TKL1 gene encodes a trans-ketolase 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    Rönne, H.5
  • 157
    • 0019328954 scopus 로고
    • Glycolate formation catalysed by spinach leaf transketolase utilizing the superoxide radical
    • T. Takabe, S. Asami, T. Akazawa, Glycolate formation catalysed by spinach leaf transketolase utilizing the superoxide radical, Biochemistry 19 (1980) 3985-3989.
    • (1980) Biochemistry , vol.19 , pp. 3985-3989
    • Takabe, T.1    Asami, S.2    Akazawa, T.3
  • 158
    • 0021431738 scopus 로고
    • Improved determination of transketolase activity in erythrocytes
    • T. Takeuchi, K. Nishino, Y. Itokawa, Improved determination of transketolase activity in erythrocytes, Clin. Chem. 30 (1984) 658-661.
    • (1984) Clin. Chem. , vol.30 , pp. 658-661
    • Takeuchi, T.1    Nishino, K.2    Itokawa, Y.3
  • 159
    • 0022535340 scopus 로고
    • Purification and characterisation of, and preparation of an antibody to, transketolase from human red blood cells
    • T. Takeuchi, K. Nishino, Y. Itokawa, Purification and characterisation of, and preparation of an antibody to, transketolase from human red blood cells, Biochem. Biophys. Acta 872 (1986) 24-32.
    • (1986) Biochem. Biophys. Acta , vol.872 , pp. 24-32
    • Takeuchi, T.1    Nishino, K.2    Itokawa, Y.3
  • 160
    • 0026603664 scopus 로고
    • Blood and serum thiamin and thiamin phosphate ester concentrations in patients with alcohol dependence syndrome before and after thiamin treatment
    • C.M.E. Tallaksen, T. Bohmer, H. Bell, Blood and serum thiamin and thiamin phosphate ester concentrations in patients with alcohol dependence syndrome before and after thiamin treatment, Alcohol. Clin. Exp. Res. 16 (1992) 320-325.
    • (1992) Alcohol. Clin. Exp. Res. , vol.16 , pp. 320-325
    • Tallaksen, C.M.E.1    Bohmer, T.2    Bell, H.3
  • 161
    • 0027314595 scopus 로고
    • Thiamin and thiamin phosphate ester deficiency assessed by high performance liquid chromatography in four clinical cases of Wernicke's encephalopathy
    • C.M.E. Tallaksen, H. Bell, T. Bohmer, Thiamin and thiamin phosphate ester deficiency assessed by high performance liquid chromatography in four clinical cases of Wernicke's encephalopathy, Alcohol. Clin. Exp. Res. 17 (1993) 712-716.
    • (1993) Alcohol. Clin. Exp. Res. , vol.17 , pp. 712-716
    • Tallaksen, C.M.E.1    Bell, H.2    Bohmer, T.3
  • 162
    • 0023114283 scopus 로고
    • Measurement of Michaelis constant for human erythrocyte transketolase and thiamin diphosphate
    • J.R. Tate, P.F. Nixon, 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
  • 163
    • 0020755112 scopus 로고
    • Function of the arginine residue of the active site of baker's yeast transketolase
    • R.A. Usmanov, G.A. Kochetov, Function of the arginine residue of the active site of baker's yeast transketolase, Biokhimiya 48 (1983) 772-781.
    • (1983) Biokhimiya , vol.48 , pp. 772-781
    • Usmanov, R.A.1    Kochetov, G.A.2
  • 164
    • 0029736891 scopus 로고    scopus 로고
    • Interaction of dihydroxyethylthiamine pyrophosphate with transketolase
    • R.A. Usmanov, N.N. Sidorova, G.A. Kochetov, Interaction of dihydroxyethylthiamine pyrophosphate with transketolase, Biochem. Mol. Biol. Int. 38 (1996) 307-314.
    • (1996) Biochem. Mol. Biol. Int. , vol.38 , pp. 307-314
    • Usmanov, R.A.1    Sidorova, N.N.2    Kochetov, G.A.3
  • 166
    • 0015239544 scopus 로고
    • Heptulose synthesis from nonphosphorylated aldoses and ketoses by spinach transketolase
    • J.J. Villafranca, B. Axelrod, Heptulose synthesis from nonphosphorylated aldoses and ketoses by spinach transketolase, J. Biol. Chem. 246 (1971) 3126-3131.
    • (1971) J. Biol. Chem. , vol.246 , pp. 3126-3131
    • Villafranca, J.J.1    Axelrod, B.2
  • 167
    • 0019977617 scopus 로고
    • A superior synthesis of aspartame
    • F.J. Vinick, S. Jung, A superior synthesis of aspartame, Tetrahedron Lett. 23 (1982) 1315-1318.
    • (1982) Tetrahedron Lett. , vol.23 , pp. 1315-1318
    • Vinick, F.J.1    Jung, S.2
  • 168
    • 0019385190 scopus 로고
    • The interrelation between transketolase and dihydroxy acetone synthase activities in the methylotrophic yeast Candida boidinii
    • M.J. Waites, J.R. Quayle, The interrelation between transketolase and dihydroxy acetone synthase activities in the methylotrophic yeast Candida boidinii, J. Gen. Microbiol. 124 (1981) 309-316.
    • (1981) J. Gen. Microbiol. , vol.124 , pp. 309-316
    • Waites, M.J.1    Quayle, J.R.2
  • 169
    • 0028829654 scopus 로고
    • Xylose-metabolizing Saccharomyces cerevisiae strains overexpressing the TKL1 and TAL1 genes encoding the pentose phosphate pathway enzymes transketolase and transaldolase
    • M. Walfridsson, J. Hallborn, M. Penttilä, S. Keränen, B. Hahn-Hägerdahl, Xylose-metabolizing Saccharomyces cerevisiae strains overexpressing the TKL1 and TAL1 genes encoding the pentose phosphate pathway enzymes transketolase and transaldolase, Appl. Environ. Microbiol. 61 (1995) 4184-4190.
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 4184-4190
    • Walfridsson, M.1    Hallborn, J.2    Penttilä, M.3    Keränen, S.4    Hahn-Hägerdahl, B.5
  • 170
    • 0004135644 scopus 로고
    • WH Freeman and Company, San Francisco
    • C. T. Walsh, Enzymatic reaction mechanisms. WH Freeman and Company, San Francisco, 1979, pp. 682-702.
    • (1979) Enzymatic Reaction Mechanisms , pp. 682-702
    • Walsh, C.T.1
  • 172
    • 0030853640 scopus 로고    scopus 로고
    • Aspartate 155 of human transketolase is essential for thiamine diphosphate-magnesium binding, and cofactor binding is required for dimer formation
    • J.L. Wang, P.R. Martin, C.K. Singleton, Aspartate 155 of human transketolase is essential for thiamine diphosphate-magnesium binding, and cofactor binding is required for dimer formation, Biochim. Biophys. Acta 1341 (1997) 165-172.
    • (1997) Biochim. Biophys. Acta , vol.1341 , pp. 165-172
    • Wang, J.L.1    Martin, P.R.2    Singleton, C.K.3
  • 173
    • 0020483448 scopus 로고
    • The isolation and preliminary characterisation of apotransketolase from human erythrocytes
    • L.G. Warnock, C.R. Prudehomme, The isolation and preliminary characterisation of apotransketolase from human erythrocytes, Biochem. Biophys. Res. Commun. 106 (1982) 719-723.
    • (1982) Biochem. Biophys. Res. Commun. , vol.106 , pp. 719-723
    • Warnock, L.G.1    Prudehomme, C.R.2
  • 174
    • 0008355413 scopus 로고
    • Thiazolium C(2)-proton exchange: General-base catalysis, direct proton transfer, and acid inhibition
    • M.W. Washabaugh, W.P. Jencks, Thiazolium C(2)-proton exchange: general-base catalysis, direct proton transfer, and acid inhibition, J. Am. Chem. Soc. 111 (1989) 674-683.
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 674-683
    • Washabaugh, M.W.1    Jencks, W.P.2
  • 176
    • 0028575439 scopus 로고
    • Analysis of an invariant cofactor-protein interaction in thiamin diphosphate dependent enzymes by site-directed mutagenesis
    • C. Wikner, L. Meshalkina, U. Nilsson, M. Nikkola, Y. Lindqvist, G. Schneider, 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
  • 179
    • 0018069860 scopus 로고
    • New reaction sequences for the non-oxidative pentose phosphate pathway
    • J.F. Williams, P.P. Blackmore, M.G. Clark, New reaction sequences for the non-oxidative pentose phosphate pathway, Biochem. J. 176 (1978) 257-282.
    • (1978) Biochem. J. , vol.176 , pp. 257-282
    • Williams, J.F.1    Blackmore, P.P.2    Clark, M.G.3
  • 182
    • 0015538687 scopus 로고
    • Biochemical assessment of thiamine status in adult Australians
    • B. Wood, D.G. Pennington, Biochemical assessment of thiamine status in adult Australians, Int. J. Vit. Nutr. Res. 43 (1973) 12-19.
    • (1973) Int. J. Vit. Nutr. Res. , vol.43 , pp. 12-19
    • Wood, B.1    Pennington, D.G.2
  • 183
    • 49049151037 scopus 로고
    • The electrophoresis and detection of transketolase
    • T. Wood, C.C. Muzariri, The electrophoresis and detection of transketolase, Anal. Biochem. 118 (1981) 221-226.
    • (1981) Anal. Biochem. , vol.118 , pp. 221-226
    • Wood, T.1    Muzariri, C.C.2
  • 185
    • 0014239305 scopus 로고
    • Regulation of glycolysis in human red cells
    • H. Yoshikawa, S. Minakami, Regulation of glycolysis in human red cells, Folia Haemat. 89 (1968) 357-373.
    • (1968) Folia Haemat , vol.89 , pp. 357-373
    • Yoshikawa, H.1    Minakami, S.2
  • 186
    • 33646313204 scopus 로고
    • Decarboxylation of pyruvate by thiamine analogues
    • R.G. Yount, D.E. Metzler, Decarboxylation of pyruvate by thiamine analogues, J. Biol. Chem. 234 (1959) 738-741.
    • (1959) J. Biol. Chem. , vol.234 , pp. 738-741
    • Yount, R.G.1    Metzler, D.E.2
  • 187
    • 0028953195 scopus 로고
    • Metabolic engineering of a pentose metabolism pathway in ethanologenic Zymomonas mobilis
    • M. Zhang, C. Eddy, K. Deanda, M. Finkelstein, S. Picataggio, Metabolic engineering of a pentose metabolism pathway in ethanologenic Zymomonas mobilis, Science 267 (1995) 240-243.
    • (1995) Science , vol.267 , pp. 240-243
    • Zhang, M.1    Eddy, C.2    Deanda, K.3    Finkelstein, M.4    Picataggio, S.5


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