Abstract
Bacterial L-asparaginases catalyzing hydrolysis of L-asparagine to L-aspartate and ammonia, are used in medical practice for treatment of acute lymphoblastic leukemia. The long-term therapy with these preparations is accompanied by a number of side effects, which are attributed to glutaminase activity of L-asparaginase. Substrate specificity and activity of L-asparaginases are directly associated with the oligomerization process of this enzyme, which is active only as the tetramer because its active sites are located in the contact areas between monomers. The present work is devoted to homology modeling of spatial structure of L-asparaginase from Erwinia carotovora, the comparative molecular-graphic analysis of subunit interfaces, and the development of a new experimental approach for studies of enzyme oligomerization. L-Asparaginase was immobilized on a surface of CM5 optical chip of biosensor Biacore 3000, which is based on the surface plasmon resonance technology. The dissociation process of enzyme tetrameric complexes up to monomers and subsequent oligomerization process have been registered.
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Original Russian Text © Yu.V. Mezentsev, A.A. Molnar, O.V. Gnedenko, Yu.V. Krasotkina, N.N. Sokolov, A.S. Ivanov, 2007, published in Biomeditsinskaya Khimiya.
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Mezentsev, Y.V., Molnar, A.A., Gnedenko, O.V. et al. Oligomerization of L-asparaginase from Erwinia carotovora . Biochem. Moscow Suppl. Ser. B 1, 58–67 (2007). https://doi.org/10.1134/S199075080701009X
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DOI: https://doi.org/10.1134/S199075080701009X