Zusammenfassung
Transaldolase katalysiert die Übertragung der Dihydroxyacetongruppe eines Ketozuckers auf einen Acceptor-Aldehyd, meist eine Aldose. Als Donatoren des „aktiven Dihydroxyacetons“1 kommen in erster Linie in Betracht Sedoheptulose-7-P und Fructose-6-P, als Acceptor-Aldosen können D-Glycerinaldehyd-3-P oder D-Erythrose-4-P wirken1–4.
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Abbreviations
- TA:
-
Transaldolase
- TK:
-
Transketolase
- PGI:
-
Phosphoglucose-Isomerase
- G-6-P-DH:
-
Glucose-6-phosphat-Dehydrogenase
- TIM:
-
Triosephosphat-Isomerase
- GDH:
-
α-Glycerophosphat-Dehydrogenase
- F-6-P:
-
Fructose-6-phosphat
- F-1,6-DP:
-
Fructose-1,6-diphosphat
- S-7-P:
-
Sedoheptulose-7-phosphat
- DHA:
-
Dihydroxyaceton
- D-Ga-3-P:
-
D-Glycerinaldehyd-3-phosphat
- D-E-4-P:
-
D-Erythrose-4-phosphat
- R-5-P:
-
Ribose-5-phosphat
- Ru-5-P:
-
Ribulose-5-phosphat
- ÄDTA:
-
Äthylendiamintetraacetat
- TPP:
-
Thiaminpyrophosphat
Referenzen
Dische, Z.: J. biol. Ch. 204, 983 (1953).
Dische, Z., L. B. Shettles and M. Osnos: Arch. Biochem. 22, 169 (1949).
Bruns, F. H., E. Dünwald u. E. Noltmann: B. Z. 330, 497 (1958).
Horecker, B. L., and P. Z. Smyrniotis: Am. Soc. 75, 2021 (1953).
Horecker, B. L., and P. Z. Smyrniotis: J. biol. Ch. 212, 811 (1955).
Bonsignore, A., S. Pontremoli, E. Grazi and M. Mangiarotti: Biochem. biophys. Res. Comm. 1, 79 (1959).
Bonsignore, A., S. Pontremoli, E. Grazi and B. L. Horecker: J. biol. Ch. 235, 1888 (1960).
Racker, E., in: Boyer-Lardy-Myrbäck, Enzymes, Bd. V, S. 407.
Kornberg, H. L., and E. Racker: Biochem. J. 61, III (1955).
Srere, P. A., H. L. Kornberg and E. Racker: Fed. Proc. 14, 285 (1955).
Horecker, B. L., and A. H. Mehler: Ann. Rev. 24, 233 (1955).
Venkataraman, R., A. G. Datta and E. Racker: Fed. Proc. 19, 82 (1960).
Dische, Z.: Naturwiss. 26, 252 (1938).
Glock, G. E.: Biochem. J. 52, 575 (1952).
Axelrod, B., R. S. Bandurski, C. M. Greiner and R. Jang: J. biol. Ch. 202, 619 (1953).
Horecker, B. L., M. Gibbs, H. Klenow and P. Z. Smyrniotis: J. biol. Ch. 207, 393 (1954).
Haba, G. de la, and E. Racker: Fed. Proe. 11, 201 (1952).
Waldvogel, M. J. u. F. Schlenk: Arch. Biochem. 14, 484 (1947).
Horecker, B. L., and P. Z. Smyrniotis: Fed. Proc. 13, 232 (1954).
Gibbs, M., and B. L. Horecker: J. biol. Ch. 208, 813 (1954).
Horecker, B. L., in: McElroy, W. D., and B. Glass (Hrsgb.): Mechanism of Enzyme Action S. 544. Baltimore 1954.
Schroeder, E., and E. Racker: Fed. Proc. 18, 318 (1959).
Couri, D., and E. Racker: Arch. Biochem. 83, 195 (1959).
Srere, P., J. R. Cooper, M. Tabachnick and E. Racker: Arch. Biochem. 74, 295 (1958).
Dische, Z., and E. Pollaczek: 2. Int. Congr. Biochem., Paris, 1952, S. 289.
Bergmann, E. D., U. Z. Littauer and B. E. Volcani: Biochim. biophys. Acta 13, 288 (1954).
Gromet, Z., M. Schramm and S. Hestrin: Biochem. J. 67, 679 (1957).
Gunsalus, I. C., B. L. Horecker and W. A. Wood: Bact. Rev. 19, 79 (1955).
Dische, Z., H. T. Shigeura and E. Landsberg: Arch. Biochem. 89, 123 (1960).
Glock, G. E., and P. McLean: Biochem. J. 56, 171 (1954).
Bernstein, I. A.: J. biol. Ch. 205, 317 (1953).
Marks, P. A., and P. Feigelson: J. biol. Ch. 226, 1001 (1957).
Shuster, L., and A. Goldin: J. biol. Ch. 230, 883 (1958).
Axelrod, B., E. S. Bandurski, C. M. Greiner and E. Jang: J. biol. Ch. 202, 619 (1953).
Horecker, B. L., M. Gibbs, H. Klenow and P. Z. Smyrniotis: J. biol. Ch. 207, 393 (1954).
Dische, Z., and E. Pollaczek: 2. Int. Congr. Biochem., Paris, 1952, S. 289.
Glock, G. E., and P. McLean: Biochem. J. 56, 171 (1954).
Horecker, B. L., P. Z. Smyrniotis and H. Klenow: J. biol. Ch. 205, 661 (1953).
Horecker, B. L., and P. Z. Smyrniotis: Am. Soc. 74, 2123 (1952).
Wood, W. A., and E. F. Schwerdt: J. biol. Ch. 206, 625 (1954).
Racker, E., G. de la Haba and I. G. Leder: Arch. Biochem. 48, 238 (1954).
Horecker, B. L., and P. Z. Smyrniotis: J. biol. Ch. 212, 811 (1955).
Keilin, D., and E. F. Hartree: Proc. E. Soc. London (B) 124, 397 (1938).
Horecker, B. L., and P. Z. Smyrniotis: J. biol. Ch. 212, 811 (1955).
Venkataraman, R., and E. Eacker: J. biol. Ch. 236, 1876 (1961).
Black, S.: Arch. Biocnem. 34, 86 (1951).
Keilin, D., and E. F. Hartree: Proc. K. Soc. London (B) 124, 397 (1938).
Horecker, B. L., and P. Z. Smyrniotis: J. biol. Ch. 212, 811 (1955).
Venkataraman, E., and E. Eacker: J. biol. Ch. 236, 1883 (1961).
Horecker, B. L., and P. Z. Smyrniotis: J. biol. Ch. 212, 811 (1955).
Backer, E., in: Boyer -Lardy -Myrbäck, Enzymes, Bd. V, S. 407.
Srere, P., J. E. Cooper, M. Tabachnick and E. Backer: Arch. Biochem. 74, 295 (1958).
Dische, Z., H. T. Shigeura and E. Landsberg: Arch. Biochem. 89, 123 (1960).
Venkataraman, B., and E. Backer: J. biol. Ch. 236, 1876 (1961).
Pontremoli, S., A. Bonsignore, E. Grazi and B.L. Horecker: J. biol. Ch. 235, 1881 (1960).
Horecker, B. L., and P. Z. Smyrniotis: Am. Soc. 75, 2021 (1953).
Backer, E., and E. Schroeder: Arch. Biochem. 66, 241 (1957).
Venkataraman, B., A. G. Datta and E. Backer: Fed. Proc. 19, 82 (1960).
Bonsignore, A., S. Pontremoli, E. Grazi and M. Mangiarotti: Biochem. biophys. Bes. Comm. 1, 79 (1959).
Horecker, B. L., P. Z. Smyrniotis, H. H. Hiatt and P. A. Marks: J. biol. Ch. 212, 827 (1955).
Lineweaver, H., and D. Burk: Am. Soc. 56, 658 (1934).
Venkataraman, E., and E. Backer: J. biol. Ch. 236, 1876 (1961).
Horecker, B. L., and P. Z. Smyrniotis: J. biol. Ch. 212, 811 (1955).
Horecker, B. L., and P. Z. Smyrniotis: Am. Soc. 75, 2021 (1953).
Venkataraman, E., A. G. Datta and E. Eacker: Fed. Proc. 19, 82 (1960).
Gibbs, M., and B. L. Horecker: J. biol. Ch. 208, 813 (1954).
Ljungdahl, L., H. G. Wood, E. Eacker and D. Couri: J. biol. Ch. 236, 1622 (1961).
Eacker, E.; in: Boyer-Lardy-Myrbäck, Enzymes, Bd. V, S. 407.
Venkataraman, E., and E. Eacker: J. biol. Ch. 236, 1883 (1961).
Pontremoli, S., A. Bonsignore, E. Grazi and B. L. Horecker: J. biol. Ch. 235, 1881 (1960).
Dische, Z., and M. E. Dische: Biochim. biophys. Acta 27, 184 (1958).
Kornberg, H. L., and E. Eacker: Biochem. J. 61, III (1955).
Srere, P. A., H. L. Kornberg and E. Eacker: Fed. Proc. 14, 285 (1955).
Bruns, F. H., E. Dünwald und E. Noltmann: B. Z. 330, 497 (1958).
Grazi, E., A. de Flora and S. Pontremoli: Biochem. biophys. Ees. Comm. 2, 121 (1960).
Venkataraman, K., and E. Racker: J. biol. Ch. 236, 1876 (1961).
Backer, E., in: Boyer-Lardy-Myrbäck, Enzymes, Bd. V, S. 407.
Venkataraman, E., A. G. Datta and E. Backer: Fed. Proc. 19, 82 (1960).
Cooper, J., B. A. Srere, M. Tabachnick and E. Backer: Arch. Biochem. 74, 306 (1958).
Wood, H. Gr., L. Ljungdahl, D. Couri and E. Backer: Fed. Proc. 18, 354 (1959).
Ljungdahl, L., H. G. Wood, E. Backer and D. Couri: J. biol. Ch. 236, 1622 (1961).
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Bruns, F.H., Reinauer, H. (1966). Transaldolase. In: Bruns, F.H., et al. Enzyme. Handbuch der Physiologisch- und Pathologisch-Chemischen Analyse, vol 6 / b. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-662-30541-6_5
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