L-xylulokinase

From Wikipedia, the free encyclopedia

In enzymology, a L-xylulokinase (EC 2.7.1.53) is an enzyme that catalyzes the chemical reaction

ATP + L-xylulose ADP + L-xylulose 5-phosphate

Thus, the two substrates of this enzyme are ATP and L-xylulose, whereas its two products are ADP and L-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:L-xylulose 5-phosphotransferase. This enzyme is also called L-xylulokinase (phosphorylating). This enzyme participates in pentose and glucuronate interconversions and ascorbate and aldarate metabolism.

[edit] References

• IUBMB entry for 2.7.1.53
• BRENDA references for 2.7.1.53 (Recommended.)
• PubMed references for 2.7.1.53
• PubMed Central references for 2.7.1.53
• Google Scholar references for 2.7.1.53
• ANDERSON RL, WOOD WA (1962). "Purification and properties of L-xylulokinase". J. Biol. Chem. 237: 1029–33. PMID 13861293. 

[edit] External links

The CAS registry number for this enzyme class is 37278-01-6.

• IUBMB entry for 2.7.1.53

• KEGG entry for 2.7.1.53

• BRENDA entry for 2.7.1.53

• NiceZyme view of 2.7.1.53

• EC2PDB: PDB structures for 2.7.1.53

• PRIAM entry for 2.7.1.53

• PUMA2 entry for 2.7.1.53

• IntEnz: Integrated Enzyme entry for 2.7.1.53

• MetaCyc entry for 2.7.1.53

• Atomic-resolution structures of enzymes belonging to this class

[edit] Gene Ontology (GO) codes

• EGO entry for GO code 0008744: L-xylulokinase

• AMIGO entry for GO code 0008744: L-xylulokinase