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Title: Mannosylglucosylglycerate biosynthesis in the deep-branching phylum Planctomycetes: characterization of the uncommon enzymes from Rhodopirellula baltica
Authors: Cunha, Sofia 
Avó, Ana Filipa d’ 
Mingote, Ana 
Lamarosa, Pedro 
Costa, M. S. da 
Costa, J. 
Keywords: Water microbiology; Marine microbiology; Homeostasis; Multienzyme complexes
Issue Date: 2013
Publisher: Nature Publishing Group
Citation: CUNHA, Sofia; AVÓ, Ana Filipa d'; MINGOTE, Ana; LAMOSA, Pedro; COSTA, Costa, Milton S. da; COSTA, Joana - Mannosylglucosylglycerate biosynthesis in the deep-branching phylum Planctomycetes : characterization of the uncommon enzymes from Rhodopirellula baltica. "Scientific Reports"[em linha]. Macmillan Publishers, 2013. Vol. 3 , N.º 2378. [Consult. dia mês ano]. Disponível na WWW: URL:
Serial title, monograph or event: Scientific Reports
Volume: 3 : 2378
Abstract: 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.
DOI: 10.1038/srep02378
Rights: openAccess
Appears in Collections:FCTUC Ciências da Vida - Artigos em Revistas Internacionais

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