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Saccharopine Dehydrogenase Activity in the High-Lysine Opaque and Floury Maize Mutants.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

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Saccharopine Dehydrogenase Activity in the High-Lysine Opaque and Floury Maize Mutants. / Pompeu, Georgia Bertoni; Vendemiatti, Ariane; Gratão, Priscila Lupino et al.
In: Food Biotechnology, Vol. 20, No. 1, 01.2006, p. 55-64.

Research output: Contribution to Journal/Magazine › Journal article › peer-review

Harvard

Pompeu, GB, Vendemiatti, A, Gratão, PL, Gaziola, SA, Lea, PJ & Azevedo, RA 2006, 'Saccharopine Dehydrogenase Activity in the High-Lysine Opaque and Floury Maize Mutants.', Food Biotechnology, vol. 20, no. 1, pp. 55-64. https://doi.org/10.1080/08905430500524101

APA

Pompeu, G. B., Vendemiatti, A., Gratão, P. L., Gaziola, S. A., Lea, P. J., & Azevedo, R. A. (2006). Saccharopine Dehydrogenase Activity in the High-Lysine Opaque and Floury Maize Mutants. Food Biotechnology, 20(1), 55-64. https://doi.org/10.1080/08905430500524101

Vancouver

Pompeu GB, Vendemiatti A, Gratão PL, Gaziola SA, Lea PJ, Azevedo RA. Saccharopine Dehydrogenase Activity in the High-Lysine Opaque and Floury Maize Mutants. Food Biotechnology. 2006 Jan;20(1):55-64. doi: 10.1080/08905430500524101

Author

Pompeu, Georgia Bertoni ; Vendemiatti, Ariane ; Gratão, Priscila Lupino et al. / Saccharopine Dehydrogenase Activity in the High-Lysine Opaque and Floury Maize Mutants. In: Food Biotechnology. 2006 ; Vol. 20, No. 1. pp. 55-64.

Bibtex

@article{12bee029d7864e81ab115a2e408a1dcb,
title = "Saccharopine Dehydrogenase Activity in the High-Lysine Opaque and Floury Maize Mutants.",
abstract = "Lysine is an essential amino acid normally present in very low concentration in cereal seeds. In previous reports we have studied the metabolism of lysine in several distinct high-lysine maize mutants and observed drastic variations in the activity of saccharopine dehydrogenase (SDH), a key enzyme involved in lysine degradation. We have now analyzed the activity of SDH using non-denaturing polyacrylamide gel electrophoresis (PAGE) to identify possible isoenzymes that could explain the patterns of activity previously observed. The results indicated the presence of at least two SDH isoenzymes, one contributing to approximately 90% of the total enzyme activity and a minor form only present in the wild type lines and the opaque-1 mutant. The results suggest that the differences in total SDH activity among the genotypes tested are due to alterations in the predominant SDH isoenzymic form, which is likely to be the bifunctional polypeptide containing lysine 2-oxoglutarate reductase.",
keywords = "Amino acids, Lysine, Mutants, Saccharopine dehydrogenase",
author = "Pompeu, {Georgia Bertoni} and Ariane Vendemiatti and Grat{\~a}o, {Priscila Lupino} and Gaziola, {Salete Aparecida} and Lea, {Peter John} and Azevedo, {Ricardo Antunes}",
year = "2006",
month = jan,
doi = "10.1080/08905430500524101",
language = "English",
volume = "20",
pages = "55--64",
journal = "Food Biotechnology",
issn = "0890-5436",
publisher = "Taylor and Francis Ltd.",
number = "1",

}

RIS

TY - JOUR

T1 - Saccharopine Dehydrogenase Activity in the High-Lysine Opaque and Floury Maize Mutants.

AU - Pompeu, Georgia Bertoni

AU - Vendemiatti, Ariane

AU - Gratão, Priscila Lupino

AU - Gaziola, Salete Aparecida

AU - Lea, Peter John

AU - Azevedo, Ricardo Antunes

PY - 2006/1

Y1 - 2006/1

N2 - Lysine is an essential amino acid normally present in very low concentration in cereal seeds. In previous reports we have studied the metabolism of lysine in several distinct high-lysine maize mutants and observed drastic variations in the activity of saccharopine dehydrogenase (SDH), a key enzyme involved in lysine degradation. We have now analyzed the activity of SDH using non-denaturing polyacrylamide gel electrophoresis (PAGE) to identify possible isoenzymes that could explain the patterns of activity previously observed. The results indicated the presence of at least two SDH isoenzymes, one contributing to approximately 90% of the total enzyme activity and a minor form only present in the wild type lines and the opaque-1 mutant. The results suggest that the differences in total SDH activity among the genotypes tested are due to alterations in the predominant SDH isoenzymic form, which is likely to be the bifunctional polypeptide containing lysine 2-oxoglutarate reductase.

AB - Lysine is an essential amino acid normally present in very low concentration in cereal seeds. In previous reports we have studied the metabolism of lysine in several distinct high-lysine maize mutants and observed drastic variations in the activity of saccharopine dehydrogenase (SDH), a key enzyme involved in lysine degradation. We have now analyzed the activity of SDH using non-denaturing polyacrylamide gel electrophoresis (PAGE) to identify possible isoenzymes that could explain the patterns of activity previously observed. The results indicated the presence of at least two SDH isoenzymes, one contributing to approximately 90% of the total enzyme activity and a minor form only present in the wild type lines and the opaque-1 mutant. The results suggest that the differences in total SDH activity among the genotypes tested are due to alterations in the predominant SDH isoenzymic form, which is likely to be the bifunctional polypeptide containing lysine 2-oxoglutarate reductase.

KW - Amino acids

KW - Lysine

KW - Mutants

KW - Saccharopine dehydrogenase

U2 - 10.1080/08905430500524101

DO - 10.1080/08905430500524101

M3 - Journal article

VL - 20

SP - 55

EP - 64

JO - Food Biotechnology

JF - Food Biotechnology

SN - 0890-5436

IS - 1

ER -