This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Similar articles in this journal Similar articles in Web of Science Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Web of Science (46) Citing Articles via Google Scholar Google Scholar Articles by Meyer, A. O. Articles by Latzko, E. Search for Related Content PubMed PubMed Citation Articles by Meyer, A. O. Articles by Latzko, E. Agricola Articles by Meyer, A. O. Articles by Latzko, E.

Articles

Pyruvate Orthophosphate Dikinase from the Immature Grains of Cereal Grasses ¹

Botanisches Institut der Universität, Schlossgarten 3, D-4400 Münster, Federal Republic of Germany

Pyruvate orthophosphate dikinase has been identified in the green grains of eight cereal grasses, most of which are classified as C₃ plants. The wheat (Triticum aestivum L. cv. Lerma Rojo) grain enzyme was further investigated: activity was low in very young grains, increased to a maximum at about 25 days after anthesis, then returned to a low level as the grain matured. It appeared to be located in the aleurone layer. A procedure was developed for obtaining partially purified preparations of pyruvate orthophosphate dikinase from the ears of wheat, oat (Avena sativa L.), barley (Hordeum distichum L.), and rye (Secale cereale L.). These preparations were suitable for measuring activities in both the forward and reverse reaction directions. The affinities of these enzymes for the six substrates (pyruvate, orthophosphate, and ATP in the forward reaction; phosphoenolpyruvate, pyrophosphate, and AMP in the reverse reaction) were determined and found to be similar to the reported affinities of the enzyme from the leaves of the C₄ plant Zea mays. A possible role for pyruvate orthophosphate dikinase in cereal grains is considered briefly.

¹ Support by the Deutsche Forschungsgemeinschaft is gratefully acknowledged.

This article has been cited by other articles:

				T. A. Hennen-Bierwagen, Q. Lin, F. Grimaud, V. Planchot, P. L. Keeling, M. G. James, and A. M. Myers Proteins from Multiple Metabolic Pathways Associate with Starch Biosynthetic Enzymes in High Molecular Weight Complexes: A Model for Regulation of Carbon Allocation in Maize Amyloplasts Plant Physiology, March 1, 2009; 149(3): 1541 - 1559. [Abstract] [Full Text] [PDF]

				E. Grafahrend-Belau, F. Schreiber, D. Koschutzki, and B. H. Junker Flux Balance Analysis of Barley Seeds: A Computational Approach to Study Systemic Properties of Central Metabolism Plant Physiology, January 1, 2009; 149(1): 585 - 598. [Abstract] [Full Text] [PDF]

				V. Mechin, C. Thevenot, M. Le Guilloux, J.-L. Prioul, and C. Damerval Developmental Analysis of Maize Endosperm Proteome Suggests a Pivotal Role for Pyruvate Orthophosphate Dikinase Plant Physiology, March 1, 2007; 143(3): 1203 - 1219. [Abstract] [Full Text] [PDF]

				E. Rosche, J. Chitty, P. Westhoff, and W. C. Taylor Analysis of Promoter Activity for the Gene Encoding Pyruvate Orthophosphate Dikinase in Stably Transformed C4 Flaveria Species Plant Physiology, July 1, 1998; 117(3): 821 - 829. [Abstract] [Full Text]