Polyphosphate—glucose phosphotransferase
polyphosphate-glucose phosphotransferase | |||||||||
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Identifiers | |||||||||
EC number | 2.7.1.63 | ||||||||
CAS number | 9033-50-5 | ||||||||
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 / EGO | ||||||||
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In enzymology, a polyphosphate-glucose phosphotransferase (EC 2.7.1.63) is an enzyme that catalyzes the chemical reaction
- (phosphate)n + D-glucose (phosphate)n-1 + D-glucose 6-phosphate
Thus, the two substrates of this enzyme are (phosphate)n and D-glucose, whereas its two products are (phosphate)n-1 and D-glucose 6-phosphate.
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 polyphosphate:D-glucose 6-phosphotransferase. Other names in common use include polyphosphate glucokinase, polyphosphate-D-(+)-glucose-6-phosphotransferase, and polyphosphate-glucose 6-phosphotransferase. This enzyme participates in glycolysis / gluconeogenesis. It employs one cofactor, neutral salt.
Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1WOQ.
References
- Szymona M (1962). "Purification and properties of a new hexokinase utilizing inorganic pyrophosphate". Acta Biochim. Pol. 9: 165–181.
- Szymona M; Ostrowski W (1964). "Inorganic polyphosphate glucokinase of Mycobacterium phlei". Biochim. Biophys. Acta. 85: 283–295. doi:10.1016/0926-6569(64)90249-4. PMID 14212975.