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Structure function analysis of ADP-dependent cyanobacterial phosphofructokinase reveals new phylogenetic grouping in the PFK-A family. | LitMetric

Structure function analysis of ADP-dependent cyanobacterial phosphofructokinase reveals new phylogenetic grouping in the PFK-A family.

J Biol Chem

Molecular Enzyme Technology and Biochemistry (MEB), Environmental Microbiology and Biotechnology (EMB), Centre for Water and Environmental Research (CWE), Faculty of Chemistry, University of Duisburg-Essen, Essen, Germany. Electronic address:

Published: November 2024

AI Article Synopsis

  • Photosynthetic organisms like cyanobacteria adjust their carbohydrate metabolism based on light conditions, switching between making and breaking down carbohydrates.
  • A study on the cyanobacterium Synechocystis sp. PCC 6803 revealed two iso-enzymes of phosphofructokinase (PFK) that uniquely use ADP instead of ATP and have different regulatory mechanisms affecting their activity in light and darkness.
  • This finding is significant as it shows a previously undocumented ADP dependence in the PFK-A enzyme family, suggesting a unique evolutionary adaptation in some cyanobacteria and a few related bacteria.

Article Abstract

Depending on the light conditions, photosynthetic organisms switch between carbohydrate synthesis or breakdown, for which the reversibility of carbohydrate metabolism, including glycolysis, is essential. Kinetic regulation of phosphofructokinase (PFK), a key-control point in glycolysis, was studied in the cyanobacterium Synechocystis sp. PCC 6803. The two PFK iso-enzymes (PFK- A1, PFK-A2), were found to use ADP instead of ATP, and have similar kinetic characteristics, but differ in their allosteric regulation. PFK-A1 is inhibited by 3-phosphoglycerate, a product of the Calvin-Benson-Bassham cycle, while PFK-A2 is inhibited by ATP, which is provided by photosynthesis. This regulation enables cyanobacteria to switch PFK off in light, and on in darkness. ADP dependence has not been reported before for the PFK-A enzyme family and was thought to be restricted to the PFK-B ribokinase superfamily. Phosphate donor specificity within the PFK-A family could be related to specific binding motifs in ATP-, ADP-, and PPi-dependent PFK-As. Phylogenetic analysis revealed a distribution of ADP-PFK-As in cyanobacteria and in a few alphaproteobacteria, which was confirmed in enzymatic studies.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11609450PMC
http://dx.doi.org/10.1016/j.jbc.2024.107868DOI Listing

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