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Volumn 20, Issue 2, 1997, Pages 127-134

Kinetics of overexpressed transketolase from Escherichia coli JM 107/pQR 700

Author keywords

Biotransformation; Direct enzyme assay; Enzyme kinetics; Escherichia coli JM 107 pQR 700; Overexpressed transketolase; Ping pong Bi Bi mechanism; Rate equation

Indexed keywords

BINDING ENERGY; BIOASSAY; BIOCONVERSION; CARBON DIOXIDE; CHEMICAL BONDS; ENZYME INHIBITION; MATHEMATICAL TRANSFORMATIONS; NUMERICAL METHODS; ORGANIC COMPOUNDS; PH; PLANTS (BOTANY);

EID: 0031081566     PISSN: 01410229     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0141-0229(96)00106-8     Document Type: Article
Times cited : (27)

References (14)
  • 1
    • 0003631337 scopus 로고
    • Transferase-catalyzed synthesis: Applications in series of amino-acids and monosaccharides
    • Servi, S., Ed.. Kluwer Academic Publishers, Dordrecht
    • 1. Bolte, J., Demuynck, C., Constant, O., and Hecquet, L. Transferase-catalyzed synthesis: Applications in series of amino-acids and monosaccharides. In: Microbial Reagents in Organic Synthesis (Servi, S., Ed.). Kluwer Academic Publishers, Dordrecht, 1992, 57-66
    • (1992) Microbial Reagents in Organic Synthesis , pp. 57-66
    • Bolte, J.1    Demuynck, C.2    Constant, O.3    Hecquet, L.4
  • 2
    • 0001619883 scopus 로고
    • Transketolase
    • Boyer, P. D., Lardy, H., and Myrback, K., Eds.. Academic Press, New York
    • 2. Racker, E. Transketolase. In: The Enzymes Vol. 5 (Boyer, P. D., Lardy, H., and Myrback, K., Eds.). Academic Press, New York, 1961, 397-406
    • (1961) The Enzymes , vol.5 , pp. 397-406
    • Racker, E.1
  • 3
    • 0015239544 scopus 로고
    • Heptulose synthesis from non-phosphorylated aldoses and ketoses by spinach transketolase
    • 3. Villafranca, J. J. and Axelrod, B. Heptulose synthesis from non-phosphorylated aldoses and ketoses by spinach transketolase. J. Biol. Chem. 1971, 246, 3126-3131
    • (1971) J. Biol. Chem. , vol.246 , pp. 3126-3131
    • Villafranca, J.J.1    Axelrod, B.2
  • 4
    • 70349629097 scopus 로고
    • Mechanism of action of transketolase. I. Properties of the crystalline enzyme
    • 4. Datta, A. G. and Racker, E. Mechanism of action of transketolase. I. Properties of the crystalline enzyme. J. Biol. Chem. 1961, 236, 617-623
    • (1961) J. Biol. Chem. , vol.236 , pp. 617-623
    • Datta, A.G.1    Racker, E.2
  • 5
    • 0028922711 scopus 로고
    • Improved production and stability of E. Coli recombinants expressing transketolase for large scale biotransformation
    • 5. French, C. and Ward, J. M. Improved production and stability of E. coli recombinants expressing transketolase for large scale biotransformation. Biotechnol. Lett. 1995, 17, 247-252
    • (1995) Biotechnol. Lett. , vol.17 , pp. 247-252
    • French, C.1    Ward, J.M.2
  • 6
    • 0011485425 scopus 로고
    • Enzyme catalysed carbon-carbon bond formation: Large-scale production of Escherichia coli transketolase
    • in press
    • 6. Hobbs, G. R., Mitra, R. K., Shauhan, R., Woodley, J. M., and Lilly, M. D. Enzyme catalysed carbon-carbon bond formation: Large-scale production of Escherichia coli transketolase. Biotechnol. Bioeng. 1995, in press
    • (1995) Biotechnol. Bioeng.
    • Hobbs, G.R.1    Mitra, R.K.2    Shauhan, R.3    Woodley, J.M.4    Lilly, M.D.5
  • 7
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • 7. Bradford, M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72, 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 8
    • 50549159930 scopus 로고
    • Kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations
    • 8. Cleland, W. W. Kinetics of enzyme-catalyzed reactions with two or more substrates or products. I. Nomenclature and rate equations. Biochim. Biophys. Acta 1963, 67, 104-137
    • (1963) Biochim. Biophys. Acta , vol.67 , pp. 104-137
    • Cleland, W.W.1
  • 9
    • 0001738080 scopus 로고
    • Kinetic studies of glutamic oxaloacetic transaminase isozymes
    • 9. Henson, C. P. and Cleland, W. W. Kinetic studies of glutamic oxaloacetic transaminase isozymes. Biochemistry 1964, 3, 338-345
    • (1964) Biochemistry , vol.3 , pp. 338-345
    • Henson, C.P.1    Cleland, W.W.2
  • 13
    • 0029067816 scopus 로고
    • Transketolase A of Escherichia coli K-12. Purification and properties of the enzyme from recombinant strains
    • 13. Springer, G. A., Schorken, U., Sprenger, G., and Sahm, H. Transketolase A of Escherichia coli K-12. Purification and properties of the enzyme from recombinant strains. Eur. J. Biochem. 1995, 230, 525-532
    • (1995) Eur. J. Biochem. , vol.230 , pp. 525-532
    • Springer, G.A.1    Schorken, U.2    Sprenger, G.3    Sahm, H.4
  • 14
    • 0000922007 scopus 로고
    • Utilization of enzymes in organic chemistry: Transketolase catalysed synthesis of ketoses
    • 14. Bolte, J., Demuynck, C., and Samaki, H. Utilization of enzymes in organic chemistry: Transketolase catalysed synthesis of ketoses. Tetrahedron Lett. 1987, 28, 5525-5528
    • (1987) Tetrahedron Lett. , vol.28 , pp. 5525-5528
    • Bolte, J.1    Demuynck, C.2    Samaki, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.