The enzyme has been isolated from the bacterium Bacillus selenitireducens. In the absence of glycerol the enzyme produces α-D-glucopyranose and phosphate from β-D-glucopyranose 1-phosphate. In this reaction the glucosyl residue is transferred to a water molecule with an inversion of the anomeric conformation.
Nihira, T., Saito, Y., Ohtsubo, K., Nakai, H. and Kitaoka, M. 2-O-α-D-glucosylglycerol phosphorylase from Bacillus selenitireducens MLS10 possessing hydrolytic activity on β-D-glucose 1-phosphate. PLoS One9:e86548 (2014). [DOI] [PMID: 24466148]
Touhara, K.K., Nihira, T., Kitaoka, M., Nakai, H. and Fushinobu, S. Structural basis for reversible phosphorolysis and hydrolysis reactions of 2-O-α-glucosylglycerol phosphorylase. J. Biol. Chem.289 (2014) 18067–18075. [DOI] [PMID: 24828502]