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PFK belongs to the phosphofructokinase B (PfkB) family of sugar kinases. [7] Other members of this family (also known as the Ribokinase family) include ribokinase (RK), adenosine kinase (AK), inosine kinase, and 1-phosphofructokinase. [7] [8] [9] The members of the PfkB/RK family are identified by the presence of three conserved sequence motifs.
Phosphofructokinase-1 (PFK-1) is one of the most important regulatory enzymes (EC 2.7.1.11) of glycolysis. It is an allosteric enzyme made of 4 subunits and controlled by many activators and inhibitors .
The lack of PFK blocks the completion of the glycolytic pathway. Therefore, all products past the block would be deficient, including Adenosine triphosphate (ATP). It may affect humans as well as other mammals (especially dogs). [4] It was named after the Japanese physician Seiichiro Tarui (b. 1927), who first observed the condition in 1965. [5]
PFK-2 is known as the "bifunctional enzyme" because of its notable structure: though both are located on one protein homodimer, its two domains act as independently functioning enzymes. [5] One terminus serves as a kinase domain (for PFK-2) while the other terminus acts as a phosphatase domain (FBPase-2). [6]
Phosphofructokinase, or PFK, catalyzes the conversion of fructose-6-phosphate to fructose-1,6-bisphosphate and is an important point in the regulation of glycolysis. High levels of ATP, H +, and citrate inhibit PFK. If citrate levels are high, it means that glycolysis is functioning at an optimal rate. High levels of AMP stimulate PFK.
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