| Literature DB >> 200838 |
Abstract
The combined phosphorylation of uridine and cytidine by a partially purified preparation of uridine-cytidine kinase has been studied with dual-substrate kinetics. The kinetic patterns obtained are consistent with the theoretical analysis for two competing, alternate substrates interacting with a single enzyme. Thus, despite feedback regulation of the kinase by both UTP and CTP, the results allow a clear conclusion that both nucleosides are phosphorylated by the same enzyme, and probably at a single site, rather than by two closely related isozymes, each specific for one pyrimidine.Entities:
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Year: 1977 PMID: 200838 DOI: 10.1007/bf01730833
Source DB: PubMed Journal: Mol Cell Biochem ISSN: 0300-8177 Impact factor: 3.396