Structural highlights
Publication Abstract from PubMed
Uridine-cytidine kinase (UCK), including human UCK2, are a family of enzymes that generally phosphorylate both uridine and cytidine. However, UCK of Thermus thermophilus HB8 (ttCK) phosphorylates only cytidine. This cytidine-restricted activity is thought to depend on Tyr93, although the precise mechanism remains unresolved. Exhaustive mutagenesis of Tyr93 in ttCK revealed that the uridine phosphorylation activity was restored only by replacement of Tyr93 with His or Gln. Replacement of His117 in human UCK2, corresponding to residue Tyr93 in ttCK, by Tyr resulted in a loss of uridine phosphorylation activity. These findings indicated that uridine phosphorylation activity commonly depends on a single residue in the UCK family.
Indispensable residue for uridine binding in the uridine-cytidine kinase family.,Tomoike F, Nakagawa N, Fukui K, Yano T, Kuramitsu S, Masui R Biochem Biophys Rep. 2017 Jul 8;11:93-98. doi: 10.1016/j.bbrep.2017.07.002., eCollection 2017 Sep. PMID:28955773[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tomoike F, Nakagawa N, Fukui K, Yano T, Kuramitsu S, Masui R. Indispensable residue for uridine binding in the uridine-cytidine kinase family. Biochem Biophys Rep. 2017 Jul 8;11:93-98. doi: 10.1016/j.bbrep.2017.07.002., eCollection 2017 Sep. PMID:28955773 doi:http://dx.doi.org/10.1016/j.bbrep.2017.07.002
