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Gene Review:

glmM - phosphoglucosamine mutase

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK3165, JW3143, mrsA, yhbF

De Reuse, H. et al., Mengin-Lecreulx, D. et al., Jolly, L. et al., Jolly, L. et al., Mio, T. et al., et al.

De Reuse, Labigne, Mengin-Lecreulx,

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Disease relevance of glmM

Chromosomal organization and transcription analysis of genes in the vicinity of Pseudomonas aeruginosa glmM gene encoding phosphoglucosamine mutase [1].
In vitro assays showed that the overexpression of this gene in E. coli cells led to a significant overproduction (from 15- to 50-fold) of phosphoglucosamine mutase activity [2].
The femR315 gene from Staphylococcus aureus, the interruption of which results in reduced methicillin resistance, encodes a phosphoglucosamine mutase [3].
The Helicobacter pylori ureC gene codes for a phosphoglucosamine mutase [4].

High impact information on glmM

The gene for this enzyme, which is essential for peptidoglycan and lipopolysaccharide biosyntheses, has been designated glmM [2].
Characterization of the essential gene glmM encoding phosphoglucosamine mutase in Escherichia coli [2].
Phosphoglucosamine mutase (GlmM) catalyzes the formation of glucosamine-1-phosphate from glucosamine-6-phosphate, an essential step in the pathway for UDP-N-acetylglucosamine biosynthesis in bacteria [5].
We showed that complete complementation of the glmM mutant can be obtained with a plasmid overproducing UreC [4].
Those authors showed that GlmM is a phosphoglucosamine mutase catalyzing interconversion of glucosamine-6-phosphate into glucosamine-1-phosphate, which is subsequently transformed into UDP-N-acetylglucosamine [4].

Chemical compound and disease context of glmM

The phosphoglucosamine mutase (GlmM) from Escherichia coli, specifically required for the interconversion of glucosamine-6-phosphate and glucosamine-1-phosphate (an essential step in the pathway for cell-wall peptidoglycan and lipopolysaccharide biosyntheses) was purified to homogeneity and its kinetic properties were investigated [6].
Because Ser(64) corresponds to the phosphorylating serine in the E. coli phosphoglucosamine mutase, it is likely that the activation of HsAgm1p also requires phosphorylation on Ser(64) [7].

Biological context of glmM

Significant conservation of the amino acid sequence of these proteins in such diverse organisms suggests a very ancient common ancestor for the genes and defines a consensus motif for the phosphoglucosamine mutase active site [4].

References

Chromosomal organization and transcription analysis of genes in the vicinity of Pseudomonas aeruginosa glmM gene encoding phosphoglucosamine mutase. Tavares, I.M., Leitão, J.H., Sá-Correia, I. Biochem. Biophys. Res. Commun. (2003) [Pubmed]
Characterization of the essential gene glmM encoding phosphoglucosamine mutase in Escherichia coli. Mengin-Lecreulx, D., van Heijenoort, J. J. Biol. Chem. (1996) [Pubmed]
The femR315 gene from Staphylococcus aureus, the interruption of which results in reduced methicillin resistance, encodes a phosphoglucosamine mutase. Jolly, L., Wu, S., van Heijenoort, J., de Lencastre, H., Mengin-Lecreulx, D., Tomasz, A. J. Bacteriol. (1997) [Pubmed]
The Helicobacter pylori ureC gene codes for a phosphoglucosamine mutase. De Reuse, H., Labigne, A., Mengin-Lecreulx, D. J. Bacteriol. (1997) [Pubmed]
Autophosphorylation of phosphoglucosamine mutase from Escherichia coli. Jolly, L., Pompeo, F., van Heijenoort, J., Fassy, F., Mengin-Lecreulx, D. J. Bacteriol. (2000) [Pubmed]
Reaction mechanism of phosphoglucosamine mutase from Escherichia coli. Jolly, L., Ferrari, P., Blanot, D., Van Heijenoort, J., Fassy, F., Mengin-Lecreulx, D. Eur. J. Biochem. (1999) [Pubmed]
Functional cloning and mutational analysis of the human cDNA for phosphoacetylglucosamine mutase: identification of the amino acid residues essential for the catalysis. Mio, T., Yamada-Okabe, T., Arisawa, M., Yamada-Okabe, H. Biochim. Biophys. Acta (2000) [Pubmed]

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