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

Azevedo, Ricardo A. and Smith, Richard J. and Lea, Peter J. (1992) Aspartate kinase regulation in maize: Evidence for co-purification of threonine-sensitive aspartate kinase and homoserine dehydrogenase. Phytochemistry, 31 (11). pp. 3731-3734.

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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.

Item Type:
Journal Article
Journal or Publication Title:
Phytochemistry
Uncontrolled Keywords:
/dk/atira/pure/researchoutput/libraryofcongress/ge
Subjects:
ID Code:
22735
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Deposited On:
14 Jan 2009 13:21
Refereed?:
No
Published?:
Published
Last Modified:
01 Jan 2020 06:32