Phosphofructokinase 2


January 18, 2022

Phosphofructokinase 2 (phosphofructokinase 2, 6-phosphofructo-2-kinase, abbreviation: PFK-2) or fructose bisphosphatase 2, fructose-2,6-bisphosphatase (Fructose 2,6-bisphosphatase) Abbreviation: FBPase-2) is an enzyme that indirectly regulates the intracellular glycolytic system and the rate of glycosylation. This enzyme catalyzes the formation and degradation of fructose-2,6-bisphosphate (Fru-2,6-P2) from fructose-6-phosphate. Fru-2,6-P2 activates glycolytic pathway phosphofructokinase 1 (PFK-1) to contribute to the rate-determining step of glycolysis, and fructose-1,6-bisphosphatase in the gluconeogenic pathway. Inhibit 1. Since Fru-2,6-P2 regulates glycolysis and gluconeogenesis differently, it acts as an important signal in switching these reverse pathways. Since PFK-2 produces Fru-2,6-P2 in response to hormonal signals, metabolism becomes more sensitive and efficient in coordination with the demands of the body's glycolytic system. This enzyme is involved in the metabolism of fructose and mannose. This enzyme is important in the regulation of carbohydrate metabolism in the liver and is most abundant in the liver, kidneys and heart. In mammals, several genes encode different isozymes, each with different tissue distribution and enzyme characteristics. The enzyme families described here have similarities to ATP-driven phosphofructokinases, both of which have little sequence similarity but are important for their interaction with fructose-6-phosphate. Some residues appear to be common. PKF-2 is known as a bifunctional enzyme, both of which are catalyzed by the same polypeptide, but at one end, where the two domains act as enzymes that function independently. The N-terminus) acts as the kinase domain (PFK-2) and the other endpoint (C-terminus) acts as the phosphatase domain (FBPase-2). In mammals, various isozymes of PFK-2 are encoded to meet tissue-specific demands. Although they have the same general function, there are slight differences in the properties of the enzyme and they are controlled by different regulation.


The monomer of this bifunctional enzyme is clearly divided into two functional domains. The kinase domain is located on the N-terminal side, and has a structure in which a β-sheet consisting of five parallel strands and one antiparallel edge strand at the terminal is surrounded by seven α-helices. A nucleotide binding fold is located on the C-terminal side of the first β-strand. The kinase domain appears to be closely related to the mononucleotide-binding protein superfamily, such as adenylate cyclase. On the other hand, the phosphatase domain is located on the C-terminal side. This domain is similar to protein families such as phosphoglycerate mutase and acid phosphatase. This domain is an α / β mixed structure with a β sheet consisting of 6 strands in the center, and an α helical subdomain covers the active site. Finally, the N-terminal region regulates kinase activity and phosphatase activity, stabilizing the enzyme dimer. The central catalytic core is conserved in all PFK-2s, but there is slight structural diversity between isoforms due to amino acid sequence differences and alternative splicing. With some exceptions.

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