PMID:10100629

Citation	Mora, P, Rubio, V, Fresquet, V and Cervera, J (1999) Localization of the site for the nucleotide effectors of Escherichia coli carbamoyl phosphate synthetase using site-directed mutagenesis. FEBS Lett. 446:133-6
Abstract	Replacement by alanine of Ser-948, Thr-974 and Lys-954 of Escherichia coli carbamoyl phosphate synthetase (CPS) shows that these residues are involved in binding the allosteric inhibitor UMP and the activator IMP. The mutant CPSs are active in vivo and in vitro and exhibit normal activation by ornithine, but the modulation by both UMP and IMP is either lost or diminished. The results demonstrate that the sites for UMP and IMP overlap and that the activator ornithine binds elsewhere. Since the mutated residues were found in the crystal structure of CPS near a bound phosphate, Ser-948, Thr-974 and Lys-954 bind the phosphate moiety of UMP and IMP.
Links	PubMed
Keywords	Allosteric Regulation; Binding Sites/genetics; Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing)/chemistry; Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing)/genetics; Carbamoyl-Phosphate Synthase (Glutamine-Hydrolyzing)/metabolism; Escherichia coli/enzymology; Escherichia coli/genetics; Mutagenesis, Site-Directed; Nucleotides/metabolism
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