L-xylulokinase

L-xylulokinase
Identifiers
EC no.2.7.1.53
CAS no.37278-01-6
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

L-xylulokinase (EC 2.7.1.53) is an enzyme that catalyzes the chemical reaction

ATP +
 
 
 
 
Reversible left-right reaction arrow
 
 
 
ADP +
 

The enzyme characterised from Aerobacter aerogenes converts L-xylulose to L-xylulose-5-phosphate by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP).[1]

This enzyme is a transferase, specifically one 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).[2]

References

  1. ↑ Anderson, R.L.; Wood, W.A. (1962). "Purification and Properties of l-Xylulokinase". Journal of Biological Chemistry. 237 (4): 1029–1033. doi:10.1016/S0021-9258(18)60278-9. PMID 13861293.
  2. ↑ Enzyme 2.7.1.53 at KEGG Pathway Database.