Commenced in January 2007
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New Malate Dehydrogenase-Glutamate Oxaolacetate Aminotransferase Glutamate Oxaloacetate Aminotransferase Enzyme System from Cereals and its Bioengineering Application
Abstract:Malate dehydrogenase-glutamate oxaloacetate aminotransferase (MDh-GOAT) enzyme complex (the EC) was isolated and purified from wheat and rise, their some main physicchemical properties were studied. Michael-s constants of the EC MDh-GOAT to malate, glutamate and NAD were investigated. This kinetic results show a high relationship to glutamate. Taking into account important role of the the EC in catabolism of glutamate – the central amino acid of a nitric exchange, there is a sharp necessity of deeper studying of this enzyme complex. Therefore the basic purpose of the work is studying the basic physical and chemical properties of this enzyme complex discovered by us, which would be very important for understanding the mechanisms of reaction catalyzed by the EC.
Digital Object Identifier (DOI): doi.org/10.5281/zenodo.1061661Procedia APA BibTeX Chicago EndNote Harvard JSON MLA RIS XML ISO 690 PDF Downloads 1086
 B.G. Forde, P. J. Lea, "Glutamate in plants: metabolism, regulation, and signaling", Journal of Experimental Botany, vol. 58, issue 9, pp. 2339- 2358, 2007.
 J. L Bailey, Techniques in protein chemistry, Elsevier Scientific Publishing Co., Inc., New York, N.Y. p. 294-295, 1962.
 M.K. Gilmanov, O.V. Fursov, A.P. Frantsev, Methods of clearing and studying of enzymes of plants, Alma-ata, 1981, pp. 91-92. (In russian).
 A. Almeida, S.J. Heales, J.P. Bola├▒os, J.M. Medina, "Glutamate neurotoxicity is associated with nitric oxide-mediated mitochondrial d", Brain Res, vol. 790, pp. 209-216, 1998.