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Gene Review:

pgmB - beta-phosphoglucomutase

Enterococcus faecalis V583

Andersson, U. et al., Andersson, U. et al.

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Disease relevance of pgmB

Furthermore, both TrePP and beta-phosphoglucomutase activity were detected in Enterococcus faecalis cell extract, indicating that this bacterium exhibits the same trehalose assimilation route as L. lactis [1].
Maltose and trehalose catabolic pathways are linked through their common enzyme, beta-phosphoglucomutase, and metabolite, beta-glucose 1-phosphate, in Lactococcus lactis [2].

High impact information on pgmB

This operon includes the gene encoding beta-phosphoglucomutase in addition to three open reading frames believed to encode a transcriptional regulator and two trehalose-specific phosphotransferase system components [1].
Maltose is degraded by the concerted action of maltose phosphorylase and beta-phosphoglucomutase, whereas trehalose is assimilated by a novel pathway, including the recently discovered enzyme, trehalose 6-phosphate phosphorylase, and beta-phosphoglucomutase [2].

References

Trehalose-6-phosphate phosphorylase is part of a novel metabolic pathway for trehalose utilization in Lactococcus lactis. Andersson, U., Levander, F., Rådström, P. J. Biol. Chem. (2001) [Pubmed]
Beta-glucose 1-phosphate-interconverting enzymes in maltose- and trehalose-fermenting lactic acid bacteria. Andersson, U., Rådström, P. Environ. Microbiol. (2002) [Pubmed]

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