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L-xylulokinase

From Wikipedia, the free encyclopedia
L-xylulokinase
Identifiers
EC no.2.7.1.53
CAS no.37278-01-6
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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PMCarticles
PubMedarticles
NCBIproteins

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.