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Family II pyrophosphatases from photosynthetic bacteria can hydrolyze free pyrophosphate

Authors Sarmina A, Peña-Segura C, Celis H

Received 5 August 2016

Accepted for publication 16 September 2016

Published 1 February 2017 Volume 2017:1 Pages 1—5

DOI https://doi.org/10.2147/CHEM.S119049

Checked for plagiarism Yes

Review by Single-blind

Peer reviewers approved by Dr Akshita Wason

Peer reviewer comments 3

Editor who approved publication: Professor A.M Kannan


Alejandra Sarmina, Claudia Peña-Segura, Heliodoro Celis

Department of Molecular Genetics, Instituto de Fisiología Celular, Universidad Nacional Autónoma de México, Ciudad de México, México

Abstract: The hydrolytic activity from three partially purified family II pyrophosphatases from the photosynthetic bacteria Rhodobacter sphaeroides, Rhodobacter capsulatus, and Rhodovulum sulfidophilum, as well as the recombinant cytoplasmic pyrophosphatase from Rba. sphaeroides, was tested with Mg2+–PPi, Mn2+–PPi, and PPi4−. Unlike family I pyrophosphatases that hydrolyze only the Mg2+–PPi complex like those from Rhodospirillum rubrum, all family II enzymes tested showed hydrolytic activity with Mg2+–PPi, Mn2+–PPi, and PPi4− without cation. The activity without added cation remained the same, even under exhaustive dialysis or after desalting the enzyme through a Sephadex G-25 column. However, this activity disappeared upon the addition of ethylenediaminetetraacetic acid and could not be restored by adding Mg2+. Moreover, the enzyme inactivation was not related to dissociation into lower molecular subunits as in other family II enzymes. This is the first report on pyrophosphatases that can hydrolyze pyrophosphate without a divalent cation added and that presumably contain a tightly bound divalent cation in their structure.

Keywords: cytoplasmic pyrophosphatases, metal cofactors, inorganic pyrophosphate, Rhodobacter sphaeroides, Rhodospirillum rubrum

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