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Information × Registration Number 0220U104577, 0120U103863 , R & D reports Title Salicylic acid binding proteins in plants: study by biochemical methods and by molecular dynamics popup.stage_title Head Kravets Volodymyr S., Доктор біологічних наук Registration Date 23-12-2020 Organization V.P. Kukhar Institute of Bioorganic Chemistry and Petrochemistry of the National Academy of Sciences of Ukraine popup.description2  Recombinant glyceraldehyde 3-phosphate dehydrogenase GAPA1 from Arabidopsis thaliana binds a functional analogue of salicylic acid - 3-aminoylsalicylic acid (3-AESC). At the same time, native salicylic acid (SA) has been shown to compete with glyceraldehyde 3-phosphate dehydrogenase GAPA1 binding in the presence of 3-AESC. The data obtained indicate that 3-AESC and SA compete for the same binding sites on the protein surface. The identification of these sites was performed by molecular dynamics methods (GROMACS) with subsequent verification of the results by the production of recombinant proteins with point mutations at the position of Asn35 and Arg81. The binding capacity of 3-AESC in the recombinant proteins Asn35Gly and Arg81Leu was significantly reduced. The data thus obtained indicate that the interaction of glyceraldehyde 3-phosphate dehydrogenase GAPA1 with SA occurs with the participation of these amino acid residues on the protein surface. SA has also been shown to inhibit the enzymatic activity of GAPA1 in vitro. By comparing the spatial structures of GAPA1 in the complex with the NADP cofactor and in the binding complex with the SA, it was found that these interactions are spatially superimposed - the SA interacts with GAPA1 at the site of binding of the adenine part of the NADP cofactor. Thus, the effect of SA on the activity of glyceraldehyde 3-phosphate dehydrogenase GAPA1 from Arabidopsis thaliana is realized by binding to protein at the level of amino acid residues Asn35 and Arg81, which prevents the association with NADP cofactor. Product Description popup.authors Pokotylo Igor V. popup.nrat_date 2020-12-23 Close