Structural highlights
Function
GGP_BACIE Catalyzes both the (1) reversible phosphorolysis of 2-O-alpha-D-glucopyranosyl-sn-glycerol (GG) from beta-D-glucose 1-phosphate (betaGlc1P) and glycerol and (2) the hydrolysis of betaGlc1P. the betaGlc1P hydrolysis is a glucosyl-transfer reaction to an acceptor water molecule that produces an anomer-inverted alpha-glucose, not a phosphatase-type reaction. In the absence of glycerol produces alpha-D-glucopyranose and phosphate from beta-D-glucopyranose 1-phosphate.[1] [2]
References
- ↑ Nihira T, Saito Y, Ohtsubo K, Nakai H, Kitaoka M. 2-O-alpha-D-glucosylglycerol phosphorylase from Bacillus selenitireducens MLS10 possessing hydrolytic activity on beta-D-glucose 1-phosphate. PLoS One. 2014 Jan 22;9(1):e86548. doi: 10.1371/journal.pone.0086548. eCollection , 2014. PMID:24466148 doi:http://dx.doi.org/10.1371/journal.pone.0086548
- ↑ Touhara KK, Nihira T, Kitaoka M, Nakai H, Fushinobu S. Structural basis for reversible phosphorolysis and hydrolysis reactions of 2-O-alpha-Glucosylglycerol phosphorylase. J Biol Chem. 2014 May 14. pii: jbc.M114.573212. PMID:24828502 doi:http://dx.doi.org/10.1074/jbc.M114.573212
