Abstract
The exopolyphosphatase of Escherichia coli processively and completely hydrolyses long polyphosphate chains to ortho-phosphate. Genetic surveys, based on the analysis of single ppx− or ppk− mutants and on the double mutant, demonstrate a relationship between these genes and the survival capacity. The exopolyphosphatase belongs to the ASKHA protein superfamily, hence, its active site is well known; however, the knowledge of the way in which this enzyme binds polyP remains incomplete. Here we present different computational approaches, site-direct mutagenesis and kinetic data to understand the relationship between structure and function of exopolyphosphatase. We propose H378 as a fundamental gatekeeper for the recognition of long chain polyphosphate.
Original language | English |
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Pages (from-to) | 64-72 |
Number of pages | 9 |
Journal | Archives of Biochemistry and Biophysics |
Volume | 606 |
DOIs | |
Publication status | Published - 15 Sept 2016 |
Keywords
- Binding
- Exopolyphosphatase
- Molecular dynamics
- Polyphosphate
- Processivity
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology