Abstract
Transamination represents a class of reaction wherein the amino nitrogen of an amino acid (donor) is transferred to aminate the carbonyl group of a keto acid (acceptor). The acceptor now becomes an amino acid whereas the donor becomes a keto acid. Transamidation involves the transfer of −NH2 from a carboxamide group to a suitable acceptor. Transamination is far better understood than transamidation, but both types of transfer reaction appear to be of general importance in the metabolism of plants and other organisms. The role of transamination in amino acid synthesis is discussed in the chapter “The synthesis of amino acids in plants”, p. 224.
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Literature
Adler, E., G. Günther u. J. E. Everett: Über den enzymatischen Abbau und Aufbau der Glutaminsäure. IV. In Hefe. Hoppe-Seylers Z. 255, 27–35 (1938).
Albaum, H. G., and P. P. Cohen: Transamination and protein synthesis in germinating oat seedlings. J. of Biol. Chem. 149, 19–27 (1943).
Bessman, S. P., J. Rossen and E. C. Layne: γ-Aminobutyric acid-glutamic acid transamination in brain. J. of Biol. Chem. 201, 385–391 (1953).
Bonner, J.: Plant Biochemistry. New York: Academic Press, Inc. 1950.
Braunstein, A. E.: Transamination and the integrative functions of the dicarboxylic acids in nitrogen metabolism. Adv. Protein Chem. 3, 1–52b (1947).
Braunstein, A. E., u. M. G. Kritzmann: Über den Ab- und Aufbau von Aminosäuren durch Umaminierung. Enzymologia (Den Haag) 2, 129–146 (1937).
Burris, R. H.: Organic acids in plant metabolism. Annual Rev. Plant Physiol. 4, 91–114 (1953).
Cammarata, P. S., and P. P. Cohen: The scope of the transamination reaction in animal tissues. J. of Biol. Chem. 187, 439–452 (1950).
Cedrangolo, F., e G. Carandante: Aspartico- and glutamico-aminopherase in higher plant. Arch. di Sci. biol. 26, 369–383 (1940). Cited from Chem. Abstr. 35, 7988 (1941).
Cohen, P. P.: [1] Transaminases. In: The Enzymes, vol. 1, part 2, pp. 1040–1067. J. B. Sumner and K. Myrbäck, editors. New York: Academic Press, Inc. 1951.
Nitrogen metabolism of amino acids. In: Chemical Pathways of Metabolism, vol. 2, pp. 1–46. D. M. Greenberg, editor. New York: Academic Press, Inc. 1954.
Delwiche, C. C., W. D. Loomis and P. K. Stumpf: Amide metabolism in higher plants. II. The exchange of isotopic ammonia by glutamyl transphorase. Arch. of Biochem. a. Biophysics 33, 333–338 (1951).
Dowmont, Y. P., and J. S. Fruton: Chromatography of peptides as applied to transamidation reactions. J. of Biol. Chem. 197, 271–283 (1952).
Durell, J., and J. S. Fruton: Proteinase-catalyzed transamidation and its efficiency. J. of Biol. Chem. 207, 487–500 (1954).
Eberts jr., F. S., R. H. Burris and A. J. Riker: The metabolism of nitrogenous compounds by sunflower crown gall tissue cultures. Plant Physiol. 29, 1–10 (1954).
Elliott, W. H.: Isolation of glutamine synthetase and glutamotransferase from green peas. J. of Biol. Chem. 201, 661–372 (1953).
Feldman, L. I., and I. C. Gunsalus: The occurrence of a wide variety of transaminases in bacteria. J. of Biol. Chem. 187, 821–830 (1950).
Fincham, J. R. S.: [1] Transaminases in Neurospora crassa. Nature (Lond.) 168, 957–958 (1951).
Ornithine transaminase in Neurospora and its relation to the biosynthesis of proline. Biochemic. J. 53, 313–320 (1953).
Fowden, L., and J. Done: A new transamination reaction. Nature (Lond.) 171, 1068–1069 (1953).
Fruton, J. S.: The role of proteolytic enzymes in the biosynthesis of peptide bonds. Yale J. Biol. a. Med. 22, 263–271 (1950).
Fruton, J. S., R. B. Johnston and M. Fried: Elongation of peptide chains in enzyme-catalyzed transamidation reactions. J. of Biol. Chem. 190, 39–53 (1951).
Gnu, K. V., A. N. Radhakrishnan and C. S. Vaidyanathan: Transaminase activity in plants. J. Indian Inst. Sci., Sect. A 34, 305–313 (1952).
Green, D. E., L. F. Leloir and V. Nocito: Transaminases. J. of Biol. Chem. 161, 559–582 (1945).
Grisolia, S., and R. H. Bttrris: Preparation of glutamate and carbamyl glutamate selectively labeled with deuterium. J. of Biol. Chem. 210, 109–117 (1954).
Gunsalus, C. F., and J. Tonzetich: Transaminases for pyridoxamine and purines. Nature (Lond.) 170, 162 (1952).
Hilton, M. A., F. W. Barnes jr., S. S. Henry and T. Enns: Mechanisms in enzymic transamination. Rate of exchange of the hydrogen of aspartate. J. of Biol. Chem. 209, 743–754 (1954).
Johnston, R. B., M. J. Mycek and J. S. Fruton: Catalysis of transamidation reactions by proteolytic enzymes. J. of Biol. Chem. 185, 629–641 (1950).
Krebs, H. A.: Equilibria in transamination systems. Biochemic. J. 54, 82–86 (1953).
Kritzmann, M. G.: The enzyme system transferring the amino-group of aspartic acid. Nature (Lond.) 143, 603–604 (1939).
Leonard, M. J. K., and R. H. Burris: A survey of transaminases in plants. J. of Biol. Chem. 170, 701–709 (1947).
Levintow, L., A. Meister, G. H. Hogeboom and E. L. Kuff: Studies on the relationship between the enzymatic synthesis of glutamine and the glutamyl transfer reaction. J. Amer. Chem. Soc. 77, 5304–5308 (1955).
Looms, W. D.: Glutamyl transferase in higher plants. Dissertation. University of California, Berkeley 1953.
Loomis, W. D., and P. K. Stumpf: Activation of plant glutamyl transphorase by ADP, IDP, and ATP. Federat. Proc. 12, 240–241 (1953).
Meister, A.: [1] Preparation and enzymatic reactions of the keto analogues of asparagine and glutamine. J. of Biol. Chem. 200, 571–589 (1953).
Enzymatic transamination reactions involving arginine and ornithine. J. of Biol. Chem. 206, 587–596 (1954).
Studies on the mechanism and specificity of the glutamine-α-keto acid transamination-deamidation reaction. J. of Biol. Chem. 210, 17–35 (1954).
Enzymatic transfer of alpha-amino groups. Science (Lancaster, Pa.) 120, 43–50 (1954).
Transamination. Adv. Enzymol. 16, 185–246 (1955).
Meister, A., and P. E. Fraser: Enzymatic formation of l-asparagine by transamination. J. of Biol. Chem. 210, 37–43 (1954).
Meister, A., L. Levintow, R. E. Greenfield and P. A. Abendschein: Hydrolysis and transfer reactions catalyzed by ω-amidase preparations. J. of Biol. Chem. 215, 441–460 (1955).
Meister, A., H. A. Sober and E. A. Peterson: [1] Activation of purified glutamic-aspartic apotransaminase by crystalline pyridoxamine phosphate. J. Amer. Chem. Soc. 74, 2385–2386 (1952).
[2] Studies on the coenzyme activation of glutamic-aspartic apotransaminase. J. of Biol. Chem. 206, 89–100 (1954).
Metzler, D. E., M. Ikawa and E. E. Snell: A general mechanism for vitamin B6-catalyzed reactions. J. Amer. Chem. Soc. 76, 648–652 (1954).
Metzler, D. E., J. Olivard and E. E. Snell: Transamination of pyridoxamine and amino acids with glyoxylic acid. J. Amer. Chem. Soc. 76, 644–648 (1954).
Metzler, D. E., and E. E. Snell: Some transamination reactions involving vitamin B6. J. Amer. Chem. Soc. 74, 979–983 (1952).
Miettinen, J. K., and A. I. Virtanen: Nitrogen metabolism of pea and alder. Transamination of γ-aminobutyric acid and l(+)-citrulline with α-ketoglutaric acid. Acta chem. scand. (Copenh.) 7, 1243–1246 (1953).
Millbank, J. W.: Demonstration of transaminase systems in the alga Chlorella. Nature (Lond.) 171, 476–477 (1953).
Peterson, E. A., and H. A. Sober: Preparation of crystalline phosphorylated derivatives of vitamin B6. J. Amer. Chem. Soc. 76, 169–175 (1954).
Peyser, P.: Some aspects of the mechanism of transamination. Dissertation. Columbia University 1954. Diss. Abstr. 14, 1301–1302 (1954).
Rabinowitz, J. C., and E. E. Snell: The vitamin B6 group. XII. Microbiological activity and natural occurrence of pyridoxamine phosphate. J. of Biol. Chem. 169, 643–650 (1947).
Rautanen, N.: [1] Transamination in green plants. J. of Biol. Chem. 163, 687–688 (1946).
[2] On the synthesis of the first amino acids in green plants. Ann. Acad. Sci. fenn., Ser. A, II 1948, No. 33, 1–66.
Roberts, E.: Studies of transamination. Arch. of Biochem. a. Biophysics 48, 395–401 (1954).
Roberts, E., P. Ayengar and I. Posner: Transamination of γ-aminobutyric acid and β-alanine in microorganisms. J. of Biol. Chem. 203, 195–204 (1953).
Roberts, E., and H. M. Bregoff: Transamination of γ-aminobutyric acid and β-alanine in brain and liver. J. of Biol. Chem. 201, 393–398 (1953).
Rudman, D., and A. Meister: Transamination in Escherichia coli. J. of Biol. Chem. 200, 591–604 (1953).
Rudnick, D., P. Mela and H. Waelsch: Enzymes of glutamine metabolism in the developing chick embryo. J. of Exper. Zool. 126, 297–321 (1954).
Ruggieri, G.: Certain transamination systems in plants. Ricerca Sci. 23, 1208–1213 (1953). Cited from Chem. Abstr. 48, 821i (1954).
Snell, E. E.: [1] The vitamin B6 group. V. The reversible interconversions of pyridoxal and pyridoxamine by transamination reactions. J. Amer. Chem. Soc. 67, 194–197 (1945).
Summary of known metabolic functions of nicotinic acid, riboflavin, and vitamin B6. Physiologic. Rev. 33, 509–524 (1953).
Stumpf, P. K.: Transaminases in higher plants. Federat. Proc. 10, 256 (1951).
Stumpf, P. K., and W. D. Loomis: Observations on a plant amide enzyme system requiring manganese and phosphate. Arch. of Biochem. 25, 451–453 (1950).
Stumpf, P. K., W. D. Loomis and C. Michelson: Amide metabolism in higher plants. I. Preparation and properties of a glutamyl transphorase from pumpkin seedüng. Arch. of Biochem. 30, 126–137 (1951).
Umbreit, W. W.: Pyridoxine and related compounds. In: The Vitamins, vol. 3, pp. 234 to 242. W. H. Sebrell jr. and R. S. Harris, editors. New York: Academic Press, Inc. 1954.
Varner, J. E., and G. C. Webster: Studies on the enzymatic synthesis of glutamine. Plant Physiol. 30, 393–402 (1955).
Virtanen, A. I., and T. Laine: [1] Biological synthesis of amino acids from atmospheric nitrogen. Nature (Lond.) 141, 748–749 (1938).
[2] Über die Umaminierung in grünen Pflanzen. Biochem. Z. 308, 213–215 (1941).
Waelsch, H.: [1] Certain aspects of intermediary metabolism of glutamine, asparagine, and glutathione. Adv. Enzymol. 13, 237–319 (1952).
The biological significance of the γ-glutamyl radical. In: Phosphorus Metabolism, vol. 2, pp. 109–125. W. D. Mc Elroy and B. Glass, editors. Baltimore: Johns Hopkins Press 1952.
Wealsch, H., P. Owades, E. Borek, N. Grossowicz and M. Schou: The enzyme-catalyzed exchange of ammonia with the amide group of glutamine and asparagine. Arch. of Biochem. 27, 237–239, 482 (1950).
Webster, G. C.: Enzymatic synthesis of glutamine in higher plants. Plant Physiol. 28, 724–727 (1953).
Williams, V. R., and J. B. Neilands: Apparent ionization constants, spectral properties and metal chelation of the cotransaminases and related compounds. Arch. of Biochem. a. Biophysics 53, 56–70 (1954).
Wilson, D. G., K. W. King and R. H. Burris: Transamination in plants. J. of Biol. Chem. 208, 863–874 (1954).
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Loomis, W.D., Stumpf, P.K. (1958). Transamination and transamidation. In: Allen, E.K., et al. Der Stickstoffumsatz / Nitrogen Metabolism. Handbuch der Pflanzenphysiologie / Encyclopedia of Plant Physiology, vol 8. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-94733-9_12
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DOI: https://doi.org/10.1007/978-3-642-94733-9_12
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