| ADP-specific phosphofructokinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.1.146 | ||||||||
| CAS no. | 237739-62-7 | ||||||||
| 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, an ADP-specific phosphofructokinase (EC 2.7.1.146) is an enzyme that catalyzes the chemical reaction
- ADP + D-fructose 6-phosphate AMP + D-fructose 1,6-bisphosphate
Thus, the two substrates of this enzyme are ADP and D-fructose 6-phosphate, whereas its two products are AMP and D-fructose 1,6-bisphosphate.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ADP:D-fructose-6-phosphate 1-phosphotransferase. This enzyme is also called ADP-6-phosphofructokinase, ADP-dependent phosphofructokinase.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1U2X.
References
- Tuininga JE, Verhees CH, van der Oost J, Kengen SW, Stams AJ, de Vos WM (July 1999). "Molecular and biochemical characterization of the ADP-dependent phosphofructokinase from the hyperthermophilic archaeon Pyrococcus furiosus". The Journal of Biological Chemistry. 274 (30): 21023–8. doi:10.1074/jbc.274.30.21023. PMID 10409652.
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