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Fhit proteins can also recognize substrates other than dinucleoside polyphosphates
Author(s) -
Guranowski Andrzej,
Wojdyła Anna M.,
Pietrowska-Borek Małgorzata,
Bieganowski Paweł,
Khurs Ele.,
Cliff Matthew J.,
Blackburn G. Michael,
Błaziak Damian,
Stec Wojciech J.
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.07.060
Subject(s) - nucleoside , nucleotide , phosphoramidate , adenosine , biochemistry , fhit , chemistry , adenosine triphosphate , polyphosphate , stereochemistry , phosphate , gene , carcinogenesis , tumor suppressor gene
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 ‐(γ‐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.