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Polyphosphatase PPN1 of Saccharomyces cerevisiae: Switching of Exopolyphosphatase and Endopolyphosphatase Activities

The polyphosphatase PPN1 of Saccharomyces cerevisiae shows an exopolyphosphatase activity splitting phosphate from chain end and an endopolyphosphatase activity fragmenting high molecular inorganic polyphosphates into shorter polymers. We revealed the compounds switching these activities of PPN1. Ph...

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Detalles Bibliográficos
Autores principales: Andreeva, Nadezhda, Trilisenko, Ludmila, Eldarov, Mikhail, Kulakovskaya, Tatiana
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Public Library of Science 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4350845/
https://www.ncbi.nlm.nih.gov/pubmed/25742176
http://dx.doi.org/10.1371/journal.pone.0119594
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author Andreeva, Nadezhda
Trilisenko, Ludmila
Eldarov, Mikhail
Kulakovskaya, Tatiana
author_facet Andreeva, Nadezhda
Trilisenko, Ludmila
Eldarov, Mikhail
Kulakovskaya, Tatiana
author_sort Andreeva, Nadezhda
collection PubMed
description The polyphosphatase PPN1 of Saccharomyces cerevisiae shows an exopolyphosphatase activity splitting phosphate from chain end and an endopolyphosphatase activity fragmenting high molecular inorganic polyphosphates into shorter polymers. We revealed the compounds switching these activities of PPN1. Phosphate release and fragmentation of high molecular polyphosphate prevailed in the presence of Co(2+) and Mg(2+), respectively. Phosphate release and polyphosphate chain shortening in the presence of Co(2+) were inhibited by ADP but not affected by ATP and argininе. The polyphosphate chain shortening in the presence of Mg(2+) was activated by ADP and arginine but inhibited by ATP.
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spelling pubmed-43508452015-03-17 Polyphosphatase PPN1 of Saccharomyces cerevisiae: Switching of Exopolyphosphatase and Endopolyphosphatase Activities Andreeva, Nadezhda Trilisenko, Ludmila Eldarov, Mikhail Kulakovskaya, Tatiana PLoS One Research Article The polyphosphatase PPN1 of Saccharomyces cerevisiae shows an exopolyphosphatase activity splitting phosphate from chain end and an endopolyphosphatase activity fragmenting high molecular inorganic polyphosphates into shorter polymers. We revealed the compounds switching these activities of PPN1. Phosphate release and fragmentation of high molecular polyphosphate prevailed in the presence of Co(2+) and Mg(2+), respectively. Phosphate release and polyphosphate chain shortening in the presence of Co(2+) were inhibited by ADP but not affected by ATP and argininе. The polyphosphate chain shortening in the presence of Mg(2+) was activated by ADP and arginine but inhibited by ATP. Public Library of Science 2015-03-05 /pmc/articles/PMC4350845/ /pubmed/25742176 http://dx.doi.org/10.1371/journal.pone.0119594 Text en © 2015 Andreeva et al http://creativecommons.org/licenses/by/4.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly credited.
spellingShingle Research Article
Andreeva, Nadezhda
Trilisenko, Ludmila
Eldarov, Mikhail
Kulakovskaya, Tatiana
Polyphosphatase PPN1 of Saccharomyces cerevisiae: Switching of Exopolyphosphatase and Endopolyphosphatase Activities
title Polyphosphatase PPN1 of Saccharomyces cerevisiae: Switching of Exopolyphosphatase and Endopolyphosphatase Activities
title_full Polyphosphatase PPN1 of Saccharomyces cerevisiae: Switching of Exopolyphosphatase and Endopolyphosphatase Activities
title_fullStr Polyphosphatase PPN1 of Saccharomyces cerevisiae: Switching of Exopolyphosphatase and Endopolyphosphatase Activities
title_full_unstemmed Polyphosphatase PPN1 of Saccharomyces cerevisiae: Switching of Exopolyphosphatase and Endopolyphosphatase Activities
title_short Polyphosphatase PPN1 of Saccharomyces cerevisiae: Switching of Exopolyphosphatase and Endopolyphosphatase Activities
title_sort polyphosphatase ppn1 of saccharomyces cerevisiae: switching of exopolyphosphatase and endopolyphosphatase activities
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4350845/
https://www.ncbi.nlm.nih.gov/pubmed/25742176
http://dx.doi.org/10.1371/journal.pone.0119594
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