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Journal of Bacteriology, August 2000, p. 4453-4457, Vol. 182, No. 16
Centro de Engenharia Biológica e
Química, Instituto Superior Técnico, 1049-001 Lisbon,
Portugal,1 and Laboratoire des
Enveloppes Bactériennes et des Antibiotiques, Biochimie
Structurale et Cellulaire, EP1088 CNRS, Université Paris-Sud,
91405 Orsay, France2
Received 20 March 2000/Accepted 10 May 2000
A search for a potential algC homologue within the
Pseudomonas aeruginosa PAO1 genome database has revealed an
open reading frame (ORF) of unknown function, ORF540 in contig 54 (July
1999 Pseudomonas genome release), that theoretically coded
for a 445-amino-acid-residue polypeptide (I. M. Tavares, J. H. Leitão, A. M. Fialho, and I. Sá-Correia, Res.
Microbiol. 150:105-116, 1999). The product of this gene is here
identified as the phosphoglucosamine mutase (GlmM) which catalyzes the
conversion of glucosamine-6-phosphate to glucosamine-1-phosphate, an
essential step in the formation of the cell wall precursor
UDP-N-acetylglucosamine. The P. aeruginosa gene
has been cloned into expression vectors and shown to restore normal
peptidoglycan biosynthesis and cell growth of a glmM Escherichia coli mutant strain. The GlmM enzyme from P. aeruginosa has been overproduced to high levels and purified to
homogeneity in a six-histidine-tagged form. Beside its
phosphoglucosamine mutase activity, the P. aeruginosa enzyme is shown to exhibit phosphomannomutase and phosphoglucomutase activities, which represent about 20 and 2% of its GlmM activity, respectively.
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.
Identification of the Pseudomonas aeruginosa
glmM Gene, Encoding Phosphoglucosamine Mutase
*
Corresponding author. Mailing address: Centro de
Engenharia Biológica e Química, Instituto Superior
Técnico, Av. Rovisco Pais, 1049-001 Lisboa, Portugal.
Phone: 351-218417682. Fax: 351-218480072. E-mail:
pcisc{at}alfa.ist.utl.pt.
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