Английская Википедия:1-phosphofructokinase

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Шаблон:Short description Шаблон:Distinguish

Шаблон:Infobox enzyme In enzymology, 1-phosphofructokinase (Шаблон:EC number) is an enzyme that catalyzes the chemical reaction

ATP + D-fructose 1-phosphate → ADP + D-fructose 1,6-bisphosphate

Thus, the two substrates of this enzyme are ATP and D-fructose 1-phosphate, whereas its two products are ADP and D-fructose 1,6-bisphosphate. The enzyme was first described and characterized in the 1960s.[1][2]

This enzyme belongs to the phosphofructokinase B (PfkB) or Ribokinase family of sugar kinases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor.[3][4] The systematic name of this enzyme class is ATP:D-fructose-phosphate 6-phosphotransferase. Other names in common use include fructose-1-phosphate kinase, 1-phosphofructokinase (phosphorylating), D-fructose-1-phosphate kinase, fructose 1-phosphate kinase, and 1-phosphofructokinase. This enzyme participates in fructose and mannose metabolism. The members of the PfkB/RK family are identified by the presence of three conserved sequence motifs and their enzymatic activity generally shows a dependence on the presence of pentavalent ions.[3][4][5]

Structure

As of 2021, two structures have been solved for this class of enzymes, with the PDB accession codes Шаблон:PDB link and Шаблон:PDB link, both from structural genomics efforts. The protein is a homodimer.

References

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Шаблон:Kinases Шаблон:Enzymes Шаблон:Portal bar

  1. Шаблон:Cite journal
  2. Шаблон:Cite journal
  3. 3,0 3,1 Park J, Gupta RS: Adenosine kinase and ribokinase--the RK family of proteins. Cell Mol Life Sci 2008, 65: 2875-2896.
  4. 4,0 4,1 Bork P, Sander C, Valencia A: Convergent evolution of similar enzymatic function on different protein folds: the hexokinase, ribokinase, and galactokinase families of sugar kinases. Protein Sci 1993, 2: 31-40.
  5. Maj MC, Singh B, Gupta RS: Pentavalent ions dependency is a conserved property of adenosine kinase from diverse sources: identification of a novel motif implicated in phosphate and magnesium ion binding and substrate inhibition. Biochemistry 2002, 41: 4059-4069.