1-phosphofructokinase

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1-phosphofructokinase
2abq.jpg
Fructose 1-phosphate kinase homodimer, Bacillus halodurans
Identifiers
EC no.2.7.1.56
CAS no.37278-03-8
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO

In enzymology, 1-phosphofructokinase (EC 2.7.1.56) 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[edit]

As of 2021, two structures have been solved for this class of enzymes, with the PDB accession codes 2JG5 and 2ABQ, both from structural genomics efforts. The protein is a homodimer.

References[edit]

  1. ^ Reeves RE, Warren LG, Hsu DS (1966). "1-Phosphofructokinase from an anaerobe". J. Biol. Chem. 241 (6): 1257–61. PMID 4222878.
  2. ^ Sapico V, Anderson RL (1969). "D-fructose 1-phosphate kinase and D-fructose 6-phosphate kinase from Aerobacter aerogenes. A comparative study of regulatory properties". J. Biol. Chem. 244 (22): 6280–8. PMID 4242639.
  3. ^ a b Park J, Gupta RS: Adenosine kinase and ribokinase--the RK family of proteins. Cell Mol Life Sci 2008, 65: 2875-2896.
  4. ^ a b 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.