High inorganic triphosphatase activities in bacteria and mammalian cells: identification of the enzymes involved.

ABSTRACT:

Background

We recently characterized a specific inorganic triphosphatase (PPPase) from Nitrosomonas europaea. This enzyme belongs to the CYTH superfamily of proteins. Many bacterial members of this family are annotated as predicted adenylate cyclases, because one of the founding members is CyaB adenylate cyclase from A. hydrophila. The aim of the present study is to determine whether other members of the CYTH protein family also have a PPPase activity, if there are PPPase activities in animal tissues and what enzymes are responsible for these activities.

Methodology/principal findings

Recombinant enzymes were expressed and purified as GST- or His-tagged fusion proteins and the enzyme activities were determined by measuring the release of inorganic phosphate. We show that the

SUBMITTER: Kohn G 

PROVIDER: S-EPMC3440374 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature