Xylulokinase
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In enzymology, a xylulokinase (EC 2.7.1.17) is an enzyme that catalyzes the chemical reaction
- ATP + D-xylulose ⇌ ADP + D-xylulose 5-phosphate
| xylulokinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
D-xylulokinase monomer, Human | |||||||||
| Identifiers | |||||||||
| EC no. | 2.7.1.17 | ||||||||
| CAS no. | 9030-58-4 | ||||||||
| 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 | ||||||||
| |||||||||
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.
Structural studies
As of late 2007, two structures have been solved for this class of enzymes, with PDB accession codes 2ITM and 2NLX.
Applications
Hydrogen production
In 2014 a low-temperature 50 °C (122 °F), atmospheric-pressure enzyme-driven process to convert xylose into hydrogen with nearly 100% of the theoretical yield was announced. The process employs 13 enzymes, including xylulokinase.[1][2]
References
Further reading
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