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J Bacteriol, February 1998, p. 473-477, Vol. 180, No. 3
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Mutational Analysis of UMP Kinase from Escherichia coli

Nadia Bucurenci,1 Lidia Serina,2 Cristina Zaharia,1 Stéphanie Landais,3 Antoine Danchin,4 and Octavian Bârzu2,*

Institute Cantacuzino, 70100 Bucharest, Romania,1 and Laboratoire de Chimie Structurale des Macromolécules,2 Laboratoire de l'Hybridolab,3 and Unité de Régulation de l'Expression Génétique,4 Institut Pasteur, 75724 Paris Cedex 15, France

Received 13 October 1997/Accepted 20 November 1997

UMP kinase from Escherichia coli is one of the four regulatory enzymes involved in the de novo biosynthetic pathway of pyrimidine nucleotides. This homohexamer, with no counterpart in eukarya, might serve as a target for new antibacterial drugs. Although the bacterial enzyme does not show sequence similarity with any other known nucleoside monophosphate kinase, two segments between amino acids 35 to 78 and 145 to 194 exhibit 28% identity with phosphoglycerate kinase and 30% identity with aspartokinase, respectively. Based on these similarities, a number of residues of E. coli UMP kinase were selected for site-directed mutagenesis experiments. Biochemical, kinetic, and spectroscopic analysis of the modified proteins identified residues essential for catalysis (Asp146), binding of UMP (Asp174), and interaction with the allosteric effectors, GTP and UTP (Arg62 and Asp77).

* Corresponding author. Mailing address: Laboratoire de Chimie Structurale des Macromolécules, 28, rue du Docteur Roux, 75724 Paris Cedex 15, France. Phone and fax: 33 (1) 45 68 84 05. E-mail: obarzu{at}pasteur.fr.




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