Polyphosphate kinase

From Wikipedia, the free encyclopedia

In enzymology, a polyphosphate kinase (EC 2.7.4.1) is an enzyme that catalyzes the chemical reaction

ATP + (phosphate)n $\rightleftharpoons$ ADP + (phosphate)n⁺1

Thus, the two substrates of this enzyme are ATP and (phosphate)n, whereas its two products are ADP and (phosphate)n+1.

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:polyphosphate phosphotransferase. This enzyme is also called polyphosphoric acid kinase. This enzyme participates in oxidative phosphorylation.

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

[edit] Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes 1XDO, 1XDP, and 2O8R.

[edit] References

IUBMB entry for 2.7.4.1
BRENDA references for 2.7.4.1 (Recommended.)
PubMed references for 2.7.4.1
PubMed Central references for 2.7.4.1
Google Scholar references for 2.7.4.1
HOFFMANN-OSTENHOF O, KENEDY J, KECK K, GABRIEL O, SCHONFELLINGER HW (1954). "[A new transphosphorylase from yeast.]". Biochim. Biophys. Acta. 14: 285. PMID 13172250.
KORNBERG A, KORNBERG SR, SIMMS ES (1956). "Metaphosphate synthesis by an enzyme from Escherichia coli". Biochim. Biophys. Acta. 20: 215–27. doi:10.1016/0006-3002(56)90280-3. PMID 13315368.
Muhammed A (1961). "Studies on biosynthesis of polymetaphosphate by an enzyme from Corynebacterium xerosis". Biochim. Biophys. Acta 54: 121–132. doi:10.1016/0006-3002(61)90945-3.