Fhit proteins can also recognize substrates other than dinucleoside polyphosphates

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• 作者：Andrzej Guranowski ; Anna M. Wojdył ; a ; Mał ; gorzata Pietrowska-Borek ; Paweł ; Bieganowski ; Elena N. Khurs ; Matthew J. Cliff ; G. Michael Blackburn ; Damian Bł ; aziak ; Wojciech J. Stec
• 关键词：Fhit protein ; Dinucleoside triphosphatase activity ; Nucleoside phosphoramidase activity ; Adenylylsulfatase activity ; Phosphodiesterase I activity ; P– ; F bond cleavage
• 刊名：FEBS Letters
• 出版年：2008
• 出版时间：3 September 2008
• 年：2008
• 卷：582
• 期：20
• 页码：3152-3158
• 全文大小：360 K

文摘

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.