1-phosphofructokinase
| 1-phosphofructokinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Fructose 1-phosphate kinase homodimer, Bacillus halodurans | |||||||||
| Identifiers | |||||||||
| EC no. | 2.7.1.56 | ||||||||
| CAS no. | 37278-03-8 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / 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]
- ^ Reeves RE, Warren LG, Hsu DS (1966). "1-Phosphofructokinase from an anaerobe". J. Biol. Chem. 241 (6): 1257–61. PMID 4222878.
- ^ 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.
- ^ a b Park J, Gupta RS: Adenosine kinase and ribokinase--the RK family of proteins. Cell Mol Life Sci 2008, 65: 2875-2896.
- ^ 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.
- ^ 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.
