tailieunhanh - Báo cáo khoa học: Novel diadenosine polyphosphate analogs with oxymethylene bridges replacing oxygen in the polyphosphate chain

Tham khảo luận văn - đề án 'báo cáo khoa học: novel diadenosine polyphosphate analogs with oxymethylene bridges replacing oxygen in the polyphosphate chain', luận văn - báo cáo, báo cáo khoa học phục vụ nhu cầu học tập, nghiên cứu và làm việc hiệu quả | Novel diadenosine polyphosphate analogs with oxymethylene bridges replacing oxygen in the polyphosphate chain Potential substrates and or inhibitors of Ap4A hydrolases Andrzej Guranowski1 Elzbieta Starzynska1 Matgorzata Pietrowska-Borek2 Dominik Rejman3 and George M Blackburn3 1 Department of Biochemistry and Biotechnology University of Life Sciences Poznan Poland 2 Department of Plant Physiology University of Life Sciences Poznan Poland 3 Department of Molecular Biology and Biotechnology University of Sheffield UK Keywords adenine nucleotide analogs Ap4A hydrolases dinucleoside polyphosphates modified pyrophosphate substrates stable pyrophosphate analogs Correspondence A. Guranowski Department of Biochemistry and Biotechnology University of Life Sciences 35 Wotyiiska Street 60 637 Poznan Poland Fax 48 61 8487146 Tel 48 61 8487201 E-mail guranow@ G. M. Blackburn Department of Molecular Biology and Biotechnology Sheffield University Sheffield S10 2TN UK Fax 44 1142222800 Tel 44 1142229462 E-mail Present address Institute of Organic Chemistry and Biochemistry AS CR . Prague Czech Republic Received 24 June 2008 revised 3 December 2008 accepted 30 December 2008 Dinucleoside polyphosphates NpnN s where N and N are nucleosides and n 3-6 phosphate residues are naturally occurring compounds that may act as signaling molecules. One of the most successful approaches to understand their biological functions has been through the use of NpnN analogs. Here we present the results of studies using novel diadenosine polyphosphate analogs with an oxymethylene group replacing one or two bridging oxygen s in the polyphosphate chain. These have been tested as potential substrates and or inhibitors of the symmetrically acting Ap4A hydrolase bis 5 -nucleosyl -tetraphosphatase symmetrical EC from E. coli and of two asymmetrically acting Ap4A hydrolases bis 5 -nu-cleosyl -tetraphosphatase asymmetrical EC from humans and .

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