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Aspartate kinase regulation in maize: Regulation by calcium and calmodulin.

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Aspartate kinase regulation in maize: Regulation by calcium and calmodulin. / Azevedo, R. A.; Smith, R. J.; Lea, P. J.
In: Phytochemistry, Vol. 31, No. 11, 1992, p. 3735-3738.

Research output: Contribution to Journal/MagazineJournal article

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Azevedo RA, Smith RJ, Lea PJ. Aspartate kinase regulation in maize: Regulation by calcium and calmodulin. Phytochemistry. 1992;31(11):3735-3738. doi: 10.1016/S0031-9422(00)97518-6

Author

Azevedo, R. A. ; Smith, R. J. ; Lea, P. J. / Aspartate kinase regulation in maize: Regulation by calcium and calmodulin. In: Phytochemistry. 1992 ; Vol. 31, No. 11. pp. 3735-3738.

Bibtex

@article{34f18f2eab6642f3bb45bff7202a3eee,
title = "Aspartate kinase regulation in maize: Regulation by calcium and calmodulin.",
abstract = "Three aspartate kinase isoenzymes (EC 2.7.2.4) sensitive to lysine, threonine and S-adenosylmethionine isolated from maize cultures, have been studied in the presence of calcium and spinach calmodulin. Neither was able to produce any change in aspartate kinase activity. Apart from the normal inhibition caused by the addition of lysine or threonine, none of the calcium antagonists tested showed a significant inhibition of activity. These results confirm those previously described for carrot in which no evidence was obtained for a regulatory role of calcium or calmodulin on aspartate kinase activity.",
keywords = "Zea mays, Gramineae, aspartate kinase, calcium, calmodulin, aspartic acid pathway.",
author = "Azevedo, {R. A.} and Smith, {R. J.} and Lea, {P. J.}",
year = "1992",
doi = "10.1016/S0031-9422(00)97518-6",
language = "English",
volume = "31",
pages = "3735--3738",
journal = "Phytochemistry",
publisher = "Elsevier Limited",
number = "11",

}

RIS

TY - JOUR

T1 - Aspartate kinase regulation in maize: Regulation by calcium and calmodulin.

AU - Azevedo, R. A.

AU - Smith, R. J.

AU - Lea, P. J.

PY - 1992

Y1 - 1992

N2 - Three aspartate kinase isoenzymes (EC 2.7.2.4) sensitive to lysine, threonine and S-adenosylmethionine isolated from maize cultures, have been studied in the presence of calcium and spinach calmodulin. Neither was able to produce any change in aspartate kinase activity. Apart from the normal inhibition caused by the addition of lysine or threonine, none of the calcium antagonists tested showed a significant inhibition of activity. These results confirm those previously described for carrot in which no evidence was obtained for a regulatory role of calcium or calmodulin on aspartate kinase activity.

AB - Three aspartate kinase isoenzymes (EC 2.7.2.4) sensitive to lysine, threonine and S-adenosylmethionine isolated from maize cultures, have been studied in the presence of calcium and spinach calmodulin. Neither was able to produce any change in aspartate kinase activity. Apart from the normal inhibition caused by the addition of lysine or threonine, none of the calcium antagonists tested showed a significant inhibition of activity. These results confirm those previously described for carrot in which no evidence was obtained for a regulatory role of calcium or calmodulin on aspartate kinase activity.

KW - Zea mays

KW - Gramineae

KW - aspartate kinase

KW - calcium

KW - calmodulin

KW - aspartic acid pathway.

U2 - 10.1016/S0031-9422(00)97518-6

DO - 10.1016/S0031-9422(00)97518-6

M3 - Journal article

VL - 31

SP - 3735

EP - 3738

JO - Phytochemistry

JF - Phytochemistry

IS - 11

ER -