Polyphosphate-glucose phosphotransferase

From Wikipedia, the free encyclopedia

In enzymology, a polyphosphate-glucose phosphotransferase (EC 2.7.1.63) 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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1WOQ.

[edit] References

IUBMB entry for 2.7.1.63
BRENDA references for 2.7.1.63 (Recommended.)
PubMed references for 2.7.1.63
PubMed Central references for 2.7.1.63
Google Scholar references for 2.7.1.63
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.