L-xylulokinase
| L-xylulokinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.1.53 | ||||||||
| CAS no. | 37278-01-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
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.
References
[edit]- ANDERSON RL, WOOD WA (1962). "Purification and properties of L-xylulokinase". J. Biol. Chem. 237: 1029–33. PMID 13861293.
