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Aspartate kinase regulation in maize: Evidence for co-purification of threonine-sensitive aspartate kinase and homoserine dehydrogenase.

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Aspartate kinase regulation in maize: Evidence for co-purification of threonine-sensitive aspartate kinase and homoserine dehydrogenase. / Azevedo, Ricardo A.; Smith, Richard J.; Lea, Peter J.
In: Phytochemistry, Vol. 31, No. 11, 1992, p. 3731-3734.

Research output: Contribution to Journal/Magazine › Journal article

Harvard

Azevedo, RA, Smith, RJ & Lea, PJ 1992, 'Aspartate kinase regulation in maize: Evidence for co-purification of threonine-sensitive aspartate kinase and homoserine dehydrogenase.', Phytochemistry, vol. 31, no. 11, pp. 3731-3734. https://doi.org/10.1016/S0031-9422(00)97517-4

APA

Azevedo, R. A., Smith, R. J., & Lea, P. J. (1992). Aspartate kinase regulation in maize: Evidence for co-purification of threonine-sensitive aspartate kinase and homoserine dehydrogenase. Phytochemistry, 31(11), 3731-3734. https://doi.org/10.1016/S0031-9422(00)97517-4

Vancouver

Azevedo RA, Smith RJ, Lea PJ. Aspartate kinase regulation in maize: Evidence for co-purification of threonine-sensitive aspartate kinase and homoserine dehydrogenase. Phytochemistry. 1992;31(11):3731-3734. doi: 10.1016/S0031-9422(00)97517-4

Author

Azevedo, Ricardo A. ; Smith, Richard J. ; Lea, Peter J. / Aspartate kinase regulation in maize: Evidence for co-purification of threonine-sensitive aspartate kinase and homoserine dehydrogenase. In: Phytochemistry. 1992 ; Vol. 31, No. 11. pp. 3731-3734.

Bibtex

@article{b0276c3361e24a619b2fd73bdf6c60fb,
title = "Aspartate kinase regulation in maize: Evidence for co-purification of threonine-sensitive aspartate kinase and homoserine dehydrogenase.",
abstract = "The threonine-sensitive and resistant forms of homoserine dehydrogenase activities were assayed in all fractions obtained during the purification of three aspartate kinase isoenzymes (threonine, lysine and lysine plus S-adenosylmethionine-sensitive) from maize cultures. The homoserine dehydrogenase isoenzyme resistant to inhibition by threonine, has a molecular weight of 70 000 and could be easily separated from the three aspartate kinase isoenzymes by ion-exchange chromatography and gel filtration; similarly the two lysine-sensitive forms of aspartate kinase could be separated from both forms of homoserine dehydrogenase. The homoserine dehydrogenase sensitive to threonine inhibition has a molecular weight of 180 000 and co-purified with the threonine-sensitive aspartate kinase isoenzyme. The hypothesis of the presence of a bifunctional protein containing activities of aspartate kinase-homoserine dehydrogenase is discussed.",
keywords = "Zea mays, Gramineae, aspartate kinase, aspartic acid pathway, homoserine dehydrogenase, threonine.",
author = "Azevedo, {Ricardo A.} and Smith, {Richard J.} and Lea, {Peter J.}",
year = "1992",
doi = "10.1016/S0031-9422(00)97517-4",
language = "English",
volume = "31",
pages = "3731--3734",
journal = "Phytochemistry",
publisher = "Elsevier Limited",
number = "11",

}

RIS

TY - JOUR

T1 - Aspartate kinase regulation in maize: Evidence for co-purification of threonine-sensitive aspartate kinase and homoserine dehydrogenase.

AU - Azevedo, Ricardo A.

AU - Smith, Richard J.

AU - Lea, Peter J.

PY - 1992

Y1 - 1992

N2 - The threonine-sensitive and resistant forms of homoserine dehydrogenase activities were assayed in all fractions obtained during the purification of three aspartate kinase isoenzymes (threonine, lysine and lysine plus S-adenosylmethionine-sensitive) from maize cultures. The homoserine dehydrogenase isoenzyme resistant to inhibition by threonine, has a molecular weight of 70 000 and could be easily separated from the three aspartate kinase isoenzymes by ion-exchange chromatography and gel filtration; similarly the two lysine-sensitive forms of aspartate kinase could be separated from both forms of homoserine dehydrogenase. The homoserine dehydrogenase sensitive to threonine inhibition has a molecular weight of 180 000 and co-purified with the threonine-sensitive aspartate kinase isoenzyme. The hypothesis of the presence of a bifunctional protein containing activities of aspartate kinase-homoserine dehydrogenase is discussed.

AB - The threonine-sensitive and resistant forms of homoserine dehydrogenase activities were assayed in all fractions obtained during the purification of three aspartate kinase isoenzymes (threonine, lysine and lysine plus S-adenosylmethionine-sensitive) from maize cultures. The homoserine dehydrogenase isoenzyme resistant to inhibition by threonine, has a molecular weight of 70 000 and could be easily separated from the three aspartate kinase isoenzymes by ion-exchange chromatography and gel filtration; similarly the two lysine-sensitive forms of aspartate kinase could be separated from both forms of homoserine dehydrogenase. The homoserine dehydrogenase sensitive to threonine inhibition has a molecular weight of 180 000 and co-purified with the threonine-sensitive aspartate kinase isoenzyme. The hypothesis of the presence of a bifunctional protein containing activities of aspartate kinase-homoserine dehydrogenase is discussed.

KW - Zea mays

KW - Gramineae

KW - aspartate kinase

KW - aspartic acid pathway

KW - homoserine dehydrogenase

KW - threonine.

U2 - 10.1016/S0031-9422(00)97517-4

DO - 10.1016/S0031-9422(00)97517-4

M3 - Journal article

VL - 31

SP - 3731

EP - 3734

JO - Phytochemistry

JF - Phytochemistry

IS - 11

ER -