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The biosynthetic pathway for the rare compatible solute mannosylglucosylglycerate (MGG) accumulated byRhodopirellula baltica, a marine member of the phylumPlanctomycetes, has been elucidated. Like one of thepathways used in the thermophilic bacterium Petrotoga mobilis, it has genes coding forglucosyl-3-phosphoglycerate synthase (GpgS) and mannosylglucosyl-3-phosphoglycerate (MGPG)synthase (MggA). However, unlike Ptg. mobilis, the mesophilic R. baltica uses a novel and very specificMGPG phosphatase (MggB). It also lacks a key enzyme of the alternative pathway in Ptg. mobilis – themannosylglucosylglycerate synthase (MggS) that catalyses the condensation of glucosylglycerate withGDP-mannose to produce MGG. The R. baltica enzymes GpgS, MggA, and MggB were expressed in E. coliand characterized in terms of kinetic parameters, substrate specificity, temperature and pH dependence.This is the first characterization of genes and enzymes for the synthesis of compatible solutes in the phylumPlanctomycetes and for the synthesis of MGG in a mesophile.This work was supported by Fundação para a Ciência e Tecnologia (FCT) Project PTDC/BIA-MIC/105247/2008 and PEst-C/SAU/LA0001/2011. S. Cunha acknowledgescholarship from FCT (SFRH/BD/46212/2008). The NationalNMRNetwork (REDE/1517/RMN/2005) was supported by POCI 2010 and FCT

scientific reports

Mannosylglucosylglycerate biosynthesis in the deep-branching phylum Planctomycetes: characterization of the uncommon enzymes from Rhodopirellula baltica