In enzymology, a polyphosphate-glucose phosphotransferase (EC 2.7.1.63) is an enzyme that catalyzes the chemical reaction.
(phosphate)n + D-glucose ⇌ {\displaystyle \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.
References
Szymona M (1962). "Purification and properties of a new hexokinase utilizing inorganic pyrophosphate". Acta Biochim. Pol. 9: 165–181. Szymona M, Ostrowski W (May 1964). "Inorganic polyphosphate glucokinase of Mycobacterium phlei". Biochimica et Biophysica Acta (BBA) - Specialized Section on Enzymological Subjects. 85 (2): 283–95. doi:10.1016/0926-6569(64)90249-4. PMID 14212975.
