1-phosphofructokinase

Not to be confused with Phosphofructokinase 1.

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

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
Search PMC articles PubMed articles NCBI proteins

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 2JG5 and 2ABQ, both from structural genomics efforts. The protein is a homodimer.