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1998 | 20 | 2 |
Tytuł artykułu

Metabolism of amino acids in germinating yellow lupin seeds. II. Pathway of conversion of aspartate to alanine during the imbibition

Warianty tytułu
Języki publikacji
EN
Abstrakty
EN
The incorporation of ¹⁴C-aspartate during the imbibition of yellow lupin seeds resulted in the production of ¹⁴C-alanine and ¹⁴CO₂. On the basis of tracer and enzymatic assays, conducted in vitro on the extract obtained from lupin seeds, it is postulated that aspartate can be converted to oxaloacetate, then, by phosphoenolopyruvate and pyruvate to alanine. This pathway can be catalyzed by the following enzymes: aspartate aminotransferase, phosphoenolpyruvate carboxykinase, pyruvate kinase and alanine aminotransferase.
Wydawca
-
Rocznik
Tom
20
Numer
2
Opis fizyczny
p.123-127,fig.
Twórcy
autor
  • A.Mickiewicz University, Al.Niepodleglosci 14, 61-713 Poznan, Poland
autor
autor
autor
Bibliografia
  • Andreo C. S., Gonzalez D., Iglesias A. 1987. Higher plant phosphoenolpyruvate carboxylase. Structure and regulation. FEBS Letters 213/1: 1–8.
  • Bradford M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein, utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248–254.
  • Bergmeyer H.U., Bernt E. 1974. 2-oxoglutarate. UV-Spectrophotometric determination. In: Methods of Enzymatic Analysis (H.U. Bergmeyer ed. 2nd ed., vol. 3. Academic Press, New York pp 1577–1580.
  • Collins D.M., Wilson A.T. 1972. Metabolism of the axis and cotyledons of Phaseolus vulgaris seeds during early germination. Phytochemistry, 11: 1931–1936.
  • Collins D.M., Wilson A.T. 1975. Embryo and endosperm metabolism of barley seeds during early germination. J. Exp. Bot. 26: 737–740.
  • Holdsworth E., Bruck K. 1977. Enzymes concerned with β-carboxylation in marine phytoplankter. Purification and properties of phosphoenolpyruvate carboxykinase. Arch. Biochem. Biophys. 182: 87–94.
  • Jetten M.S.M., Sinskey A.J. 1993. Characterization of phospoenolpyruvate carboxykinase from Corynebacterium glutamicum. FEMS Microbiology Letters 111: 183–188.
  • Latzko E., Kelly G.J. 1983. The many faced function of phosphoenolpyruvate carboxylase in C3 plants. Physiol. Veg. 31: 805–815.
  • Perl M. 1986. ATP synthesis and utilization in the early stage of seeds germination in relation to seed dormancy and quality. Physiol. Plant., 66: 177–182.
  • Perl M. 1978. Phosphoenol-pyruvate-carboxylase activity in cotton and sorghum seeds and its relation to seedling development. Planta 139: 239–243.
  • Reeves H., Rabin R., Wogner W.S., Aji S.J. 1971. Malate dehydrogenase. In: Methods in Microbiology. Norris J.R., Ribbons D.W., Academic Press New York, vol. 6A: 451–452.
  • Ratajczak W., Gierczak C. and Ratajczak L. 1990. Changes in free amino acids levels at early stages of germination of yellow lupine seeds. Acta Physiol. Plant. 12: 253–258.
  • Ratajczak W., Lehmann T., Polcyn W. and Ratajczak L. 1996. Metabolism of amino acids in germinating yellow lupine seeds. I. The decomposition of 14C-aspartate and 14C-glutamate during the imbibition. Acta Physiol. Plant. 18: 13–18.
  • Ratajczak W., Polcyn W., Lehmann T. and Ratajczak L. 1997. Changes in the activity of phosphoenolpyruvate carboxylating enzymes in germinating yellow lupin seeds. Acta Physiol. Plant. 20: 119–122.
  • Spedding D.J., Wilson A.T. 1968. Studies of the early reactions in the germination of Sinapsis alba seeds. Phytochemistry 7: 897–901.
  • Worthington Enzyme Manual 1993. Ed. Von Worthington, Worthington Biochemical Corporation, Freehold, New Jersey, USA, pp 342–346.
Typ dokumentu
Bibliografia
Identyfikatory
Identyfikator YADDA
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