English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Global: Zendy Plus annual

Presents the access of premium content as premium feature

Premium Content

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Insights

Presents the pdf analysis as premium feature

PDF Analysis

Presents the zaia usage as premium feature

ZAIA

Global: Zendy Tools annual

Global: Zendy Free Plan

Global: Zendy Tools monthly

Global: Zendy Plus monthly

Flux into the glycolytic pathway of most cells is controlled via allosteric regulation of the irreversible, committing step catalyzed by ATP-dependent phosphofructokinase (PFK) (ATP-PFK; EC2.7.1.11 ), the key enzyme of glycolysis. In some organisms, the step is catalyzed by PPi -dependent PFK (PPi -PFK; EC2.7.1.90 ), which uses PPi instead of ATP as the phosphoryl donor, conserving ATP and rendering the reaction reversible under physiological conditions. We have determined the enzymic properties of PPi -PFK from the anaerobic, hyperthermophilic archaeonThermoproteus tenax , purified the enzyme to homogeneity, and sequenced the gene. The ∼100-kDa PPi -PFK fromT. tenax consists of 37-kDa subunits; is not regulated by classical effectors of ATP-PFKs such as ATP, ADP, fructose 2,6-bisphosphate, or metabolic intermediates; and shares 20 to 50% sequence identity with known PFK enzymes. Phylogenetic analyses of biochemically characterized PFKs grouped the enzymes into three monophyletic clusters: PFK group I represents only classical ATP-PFKs fromBacteria andEucarya ; PFK group II contains only PPi -PFKs from the genusPropionibacterium , plants, and amitochondriate protists; whereas group III consists of PFKs with either cosubstrate specificity, i.e., the PPi -dependent enzymes fromT. tenax andAmycolatopsis methanolica and the ATP-PFK fromStreptomyces coelicolor . Comparative analyses of the pattern of conserved active-site residues strongly suggest that the group III PFKs originally bound PPi as a cosubstrate.

journal of bacteriology

PP <sub>i</sub> -Dependent Phosphofructokinase from <i>Thermoproteus tenax</i> , an Archaeal Descendant of an Ancient Line in Phosphofructokinase Evolution

PP i -Dependent Phosphofructokinase from Thermoproteus tenax , an Archaeal Descendant of an Ancient Line in Phosphofructokinase Evolution

PP _i -Dependent Phosphofructokinase from Thermoproteus tenax , an Archaeal Descendant of an Ancient Line in Phosphofructokinase Evolution