Xylulokinase

From Wikipedia, the free encyclopedia

In enzymology, a xylulokinase (EC 2.7.1.17) is an enzyme that catalyzes the chemical reaction

ATP + D-xylulose $\rightleftharpoons$ ADP + D-xylulose 5-phosphate

Thus, the two substrates of this enzyme are ATP and D-xylulose, whereas its two products are ADP and D-xylulose 5-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 ATP:D-xylulose 5-phosphotransferase. Other names in common use include xylulokinase (phosphorylating), and D-xylulokinase. This enzyme participates in pentose and glucuronate interconversions.

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

[edit] Structural studies

As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2ITM and 2NLX.

[edit] References

IUBMB entry for 2.7.1.17
BRENDA references for 2.7.1.17 (Recommended.)
PubMed references for 2.7.1.17
PubMed Central references for 2.7.1.17
Google Scholar references for 2.7.1.17
Hickman J and Ashwell G (1958). "Purification and properties of D-xylulokinase in liver". J. Biol. Chem. 232: 737–748.
Simpson FJ (1966). "D-Xylulokinase". Methods Enzymol. 9: 454–458.
Slein MW (1955). "Xylose isomerase from Pasteurella pestis, strain A-1122". J. Am. Chem. Soc. 77: 1663–1667.
Stumpf PK and Horecker BL (1956). "The roole of xylulose 5-phosphate in xylose metabolism of Lactobacillus pentosus". J. Biol. Chem. 218: 753–768.