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Fhit proteins can also recognize substrates other than dinucleoside polyphosphates
Authors:Guranowski Andrzej  Wojdy?a Anna M  Pietrowska-Borek Ma?gorzata  Bieganowski Pawe?  Khurs Elena N  Cliff Matthew J  Blackburn G Michael  B?aziak Damian  Stec Wojciech J
Institution:Department of Biochemistry and Biotechnology, The University of Life Sciences, 60-637 Poznań, Poland. guranowski@au.poznan.pl
Abstract:We show here that Fhit proteins, in addition to their function as dinucleoside triphosphate hydrolases, act similarly to adenylylsulfatases and nucleoside phosphoramidases, liberating nucleoside 5'-monophosphates from such natural metabolites as adenosine 5'-phosphosulfate and adenosine 5'-phosphoramidate. Moreover, Fhits recognize synthetic nucleotides, such as adenosine 5'-O-phosphorofluoridate and adenosine 5'-O-(gamma-fluorotriphosphate), and release AMP from them. With respect to the former, Fhits behave like a phosphodiesterase I concomitant with cleavage of the P-F bond. Some kinetic parameters and implications of the novel reactions catalyzed by the human and plant (Arabidopsis thaliana) Fhit proteins are presented.
Keywords:APS or S-pA  adenosine 5′-phosphosulfate  NH2-pA  adenosine 5′-phosphoramidate  ATP-F or F-pppA  adenosine 5′-O-(γ-fluorotriphosphate)  HPLC  high performance liquid chromatography  TLC  thin layer chromatography
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