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New Malate Dehydrogenase-Glutamate Oxaolacetate Aminotransferase Glutamate Oxaloacetate Aminotransferase Enzyme System from Cereals and its Bioengineering Application

Authors: Zhanar S. Kudiyarova, Zhanar K. Rakhmetova, L. K. Bekbayeva, N. Z. Omirbekova, M. K. Gilmanov

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.

Keywords: Malate dehydrogenase-glutamate oxaloacetate aminotransferase, enzyme complex, glutamate.

Digital Object Identifier (DOI): doi.org/10.5281/zenodo.1061661

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References:


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