Polyphosphate—glucose phosphotransferase
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 and 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.
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