EC 2.7.1.48 - Uridine/cytidine kinase

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IntEnz Enzyme Nomenclature
EC 2.7.1.48

Names

Accepted name:
uridine/cytidine kinase
Other names:
pyrimidine ribonucleoside kinase
uridine kinase (phosphorylating)
uridine phosphokinase
uridine-cytidine kinase
uridine monophosphokinase
Systematic name:
ATP:uridine/cytidine 5'-phosphotransferase

Reactions

Comments:

The enzyme, found in prokaryotes and eukaryotes, phosphorylates both uridine and cytidine to their monophosphate forms. The enzyme from Escherichia coli prefers GTP to ATP. The human enzyme also catalyses the phosphorylation of several cytotoxic ribonucleoside analogs. Cf. EC 2.7.1.213.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0004849
CAS Registry Number: 9026-39-5
UniProtKB/Swiss-Prot: (243) [show] [UniProt]

References

  1. Orengo, A.
    Regulation of enzymic activity by metabolites. I. Uridine-cytidine kinase of Novikoff ascites rat tumor.
    J. Biol. Chem. 244 : 2204-2209 (1969). [PMID: 5782006]
  2. Sköld, O.
    Uridine kinase from Erlich ascites tumor: purification and properties.
    J. Biol. Chem. 235 : 3273-3279 (1960).
  3. Valentin-Hansen, P.
    Uridine-cytidine kinase from Escherichia coli.
    Meth. Enzymol. 51 : 308-314 (1978). [PMID: 211379]
  4. Van Rompay, A. R., Norda, A., Linden, K., Johansson, M., Karlsson, A.
    Phosphorylation of uridine and cytidine nucleoside analogs by two human uridine-cytidine kinases.
    Mol. Pharmacol. 59 : 1181-1186 (2001). [PMID: 11306702]
  5. Ohler, L., Niopek-Witz, S., Mainguet, S. E., Mohlmann, T.
    Pyrimidine Salvage: Physiological Functions and Interaction with Chloroplast Biogenesis.
    Plant Physiol. 180 : 1816-1828 (2019). [PMID: 31101721]

[EC 2.7.1.48 created 1965, modified 2020]