Polyphosphate-glucose phosphotransferase

In enzymology, a polyphosphate-glucose phosphotransferase is an enzyme that catalyzes the chemical reaction


 * (phosphate)n + D-glucose $$\rightleftharpoons$$ (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.