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Adenylylsulfate–ammonia adenylyltransferase activity is another inherent property of Fhit proteins

Fhits (fragile histidine triad proteins) occur in eukaryotes but their function is largely unknown, although human Fhit is believed to act as a tumour suppressor. Fhits also exhibit dinucleoside triphosphatase, adenylylsulfatase and nucleoside phosphoramidase activities that in each case yield nucle...

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Autores principales: Wojdyła-Mamoń, Anna M., Guranowski, Andrzej
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4613722/
https://www.ncbi.nlm.nih.gov/pubmed/26181368
http://dx.doi.org/10.1042/BSR20150135
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author Wojdyła-Mamoń, Anna M.
Guranowski, Andrzej
author_facet Wojdyła-Mamoń, Anna M.
Guranowski, Andrzej
author_sort Wojdyła-Mamoń, Anna M.
collection PubMed
description Fhits (fragile histidine triad proteins) occur in eukaryotes but their function is largely unknown, although human Fhit is believed to act as a tumour suppressor. Fhits also exhibit dinucleoside triphosphatase, adenylylsulfatase and nucleoside phosphoramidase activities that in each case yield nucleoside 5′-monophosphate as a product. Due to the dinucleoside triphosphatase activity, Fhits may also be involved in mRNA decapping. In the present study, we demonstrate Fhit-catalysed ammonolysis of adenosine 5′-phosphosulfate, which results in the formation of adenosine 5′-phosphoramidate. This reaction has previously been associated with adenylylsulfate–ammonia adenylyltransferase (EC 2.7.7.51). Our finding shows that the capacity to catalyse ammonolysis is another inherent property of Fhits. Basic kinetic parameters and substrate specificity of this reaction catalysed by human Fhit are presented.
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spelling pubmed-46137222015-11-02 Adenylylsulfate–ammonia adenylyltransferase activity is another inherent property of Fhit proteins Wojdyła-Mamoń, Anna M. Guranowski, Andrzej Biosci Rep Original Papers Fhits (fragile histidine triad proteins) occur in eukaryotes but their function is largely unknown, although human Fhit is believed to act as a tumour suppressor. Fhits also exhibit dinucleoside triphosphatase, adenylylsulfatase and nucleoside phosphoramidase activities that in each case yield nucleoside 5′-monophosphate as a product. Due to the dinucleoside triphosphatase activity, Fhits may also be involved in mRNA decapping. In the present study, we demonstrate Fhit-catalysed ammonolysis of adenosine 5′-phosphosulfate, which results in the formation of adenosine 5′-phosphoramidate. This reaction has previously been associated with adenylylsulfate–ammonia adenylyltransferase (EC 2.7.7.51). Our finding shows that the capacity to catalyse ammonolysis is another inherent property of Fhits. Basic kinetic parameters and substrate specificity of this reaction catalysed by human Fhit are presented. Portland Press Ltd. 2015-08-07 /pmc/articles/PMC4613722/ /pubmed/26181368 http://dx.doi.org/10.1042/BSR20150135 Text en © 2015 Authors http://creativecommons.org/licenses/by/3.0/ This is an open access article published by Portland Press Limited and distributed under the Creative Commons Attribution Licence 3.0 (http://creativecommons.org/licenses/by/3.0/) .
spellingShingle Original Papers
Wojdyła-Mamoń, Anna M.
Guranowski, Andrzej
Adenylylsulfate–ammonia adenylyltransferase activity is another inherent property of Fhit proteins
title Adenylylsulfate–ammonia adenylyltransferase activity is another inherent property of Fhit proteins
title_full Adenylylsulfate–ammonia adenylyltransferase activity is another inherent property of Fhit proteins
title_fullStr Adenylylsulfate–ammonia adenylyltransferase activity is another inherent property of Fhit proteins
title_full_unstemmed Adenylylsulfate–ammonia adenylyltransferase activity is another inherent property of Fhit proteins
title_short Adenylylsulfate–ammonia adenylyltransferase activity is another inherent property of Fhit proteins
title_sort adenylylsulfate–ammonia adenylyltransferase activity is another inherent property of fhit proteins
topic Original Papers
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4613722/
https://www.ncbi.nlm.nih.gov/pubmed/26181368
http://dx.doi.org/10.1042/BSR20150135
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