Pseudouridine kinase

Pseudouridine kinase
Identifiers
EC no.2.7.1.83
CAS no.62213-40-5
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

Pseudouridine kinase (EC 2.7.1.83) is an enzyme that catalyzes the chemical reaction

ATP +
 
 
 
 
Reversible left-right reaction arrow
 
 
 
ADP +
 
2D representation of the chemical structure of Q27102833.
pseudouridine 5'-phosphate

The enzyme characterised from Escherichia coli converts pseudouridine to pseudouridine 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:pseudouridine 5'-phosphotransferase. This enzyme is also called pseudouridine kinase (phosphorylating).[2]

References

  1. ↑ Solomon LR, Breitman TR (1971). "Pseudouridine kinase of Escherichia coli: a new enzyme". Biochem. Biophys. Res. Commun. 44 (2): 299–304. Bibcode:1971BBRC...44..299S. doi:10.1016/0006-291X(71)90599-7. PMID 4334133.
  2. ↑ Enzyme 2.7.1.83 at KEGG Pathway Database.