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

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An Erratum to this article was published on 01 September 1998

Abstract

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.

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Abbreviations

GOT:

L-aspartate:2-oxoglutarate aminotransferase

GPT:

L-alanine:2-oxoglutarate aminotransferase

MA:

malate

OAA:

oxaloacetate

PA:

pyruvate

PEP:

phosphoenolpyruvate

PEPC:

phosphoenolpyruvate carboxylase

PEPCK:

phosphoenolpyruvate carboxykinase

References

  • Andreo C. S., Gonzalez D., Iglesias A. 1987. Higher plant phosphoenolpyruvate carboxylase. Structure and regulation. FEBS Letters 213/1: 1–8.

    Article  CAS  Google Scholar 

  • 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.

    Article  CAS  PubMed  Google Scholar 

  • 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.

    Google Scholar 

  • Collins D.M., Wilson A.T. 1972. Metabolism of the axis and cotyledons of Phaseolus vulgaris seeds during early germination. Phytochemistry, 11: 1931–1936.

    Article  CAS  Google Scholar 

  • Collins D.M., Wilson A.T. 1975. Embryo and endosperm metabolism of barley seeds during early germination. J. Exp. Bot. 26: 737–740.

    Article  CAS  Google Scholar 

  • 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.

    Article  CAS  PubMed  Google Scholar 

  • Jetten M.S.M., Sinskey A.J. 1993. Characterization of phospoenolpyruvate carboxykinase from Corynebacterium glutamicum. FEMS Microbiology Letters 111: 183–188.

    Article  CAS  Google Scholar 

  • Latzko E., Kelly G.J. 1983. The many faced function of phosphoenolpyruvate carboxylase in C3 plants. Physiol. Veg. 31: 805–815.

    Google Scholar 

  • 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.

    Article  CAS  Google Scholar 

  • Perl M. 1978. Phosphoenol-pyruvate-carboxylase activity in cotton and sorghum seeds and its relation to seedling development. Planta 139: 239–243.

    Article  CAS  PubMed  Google Scholar 

  • 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.

    Google Scholar 

  • 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.

    CAS  Google Scholar 

  • 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.

    CAS  Google Scholar 

  • 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.

    Article  Google Scholar 

  • Spedding D.J., Wilson A.T. 1968. Studies of the early reactions in the germination of Sinapsis alba seeds. Phytochemistry 7: 897–901.

    Article  CAS  Google Scholar 

  • Worthington Enzyme Manual 1993. Ed. Von Worthington, Worthington Biochemical Corporation, Freehold, New Jersey, USA, pp 342–346.

    Google Scholar 

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Ratajczak, W., Polcyn, W., Lehmann, T. et al. Metabolism of amino acids in germinating yellow lupin seeds. II. Pathway of conversion of aspartate to alanine during the imbibition. Acta Physiol Plant 20, 123–127 (1998). https://doi.org/10.1007/s11738-998-0002-8

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  • DOI: https://doi.org/10.1007/s11738-998-0002-8

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