Characterization of the ugpG gene encoding a UDP-glucose pyrophosphorylase from the gellan gum producer Sphingomonas paucimobilis ATCC 31461

Marques, Ana Rita; Ferreira, P. B.; Sá‐Correia, Isabel; Fialho, Arsénio M.

doi:10.1007/s00438-003-0805-7

Cited by 22 publications

(6 citation statements)

References 48 publications

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“…The ugpG gene, encoding a UDP-glucose pyrophosphorylase (EC 2.7.7.9), which catalyses the reversible conversion of glucose-1-phosphate and UTP into precursor UDP-D-glucose and diphosphate48, is NX02_05810 . The ugdG gene, encoding a UDP-glucose dehydrogenase (EC 1.1.1.22), which converts UDP-glucose into the activated precursor UDP-D-glucuronic acid, is NX02_04625 49.…”

Section: Resultsmentioning

confidence: 99%

The evolutionary life cycle of the polysaccharide biosynthetic gene cluster based on the Sphingomonadaceae

Huang

et al. 2017

Sci Rep

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Although clustering of genes from the same metabolic pathway is a widespread phenomenon, the evolution of the polysaccharide biosynthetic gene cluster remains poorly understood. To determine the evolution of this pathway, we identified a scattered production pathway of the polysaccharide sanxan by Sphingomonas sanxanigenens NX02, and compared the distribution of genes between sphingan-producing and other Sphingomonadaceae strains. This allowed us to determine how the scattered sanxan pathway developed, and how the polysaccharide gene cluster evolved. Our findings suggested that the evolution of microbial polysaccharide biosynthesis gene clusters is a lengthy cyclic process comprising cluster 1 → scatter → cluster 2. The sanxan biosynthetic pathway proved the existence of a dispersive process. We also report the complete genome sequence of NX02, in which we identified many unstable genetic elements and powerful secretion systems. Furthermore, nine enzymes for the formation of activated precursors, four glycosyltransferases, four acyltransferases, and four polymerization and export proteins were identified. These genes were scattered in the NX02 genome, and the positive regulator SpnA of sphingans synthesis could not regulate sanxan production. Finally, we concluded that the evolution of the sanxan pathway was independent. NX02 evolved naturally as a polysaccharide producing strain over a long-time evolution involving gene acquisitions and adaptive mutations.

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Section: Resultsmentioning

confidence: 99%

The evolutionary life cycle of the polysaccharide biosynthetic gene cluster based on the Sphingomonadaceae

Huang

et al. 2017

Sci Rep

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“…Clearly, these two sites are important to substrate recognition and enzymatic activity, but the location and full nature of the GFPP active site remain a mystery. The enzyme does not contain the T(V/L)RD motif that was identified as a base recognition motif in human guanylate binding protein (27), the GXGTRXLPXTK motif (29), nor does it contain recognition motifs that have been identified in other nucleotide-sugar metabolizing proteins (30).…”

Section: Discussionmentioning

confidence: 97%

Identification of Catalytic Amino Acids in the Human GTP Fucose Pyrophosphorylase Active Site

Quirk

Seley

2005

Biochemistry

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GTP-l-fucose pyrophosphorylase(GFPP) catalyzes the reversible formation of the nucleotide-sugar GDP-beta-l-fucose from guanosine triphosphate and beta-l-fucose-1-phosphate. The enzyme functions primarily in the mammalian liver and kidney to salvage free fucose during the breakdown of glycoproteins and glycolipids. GFPP shares little primary sequence identity with other nucleotide-sugar metabolizing enzymes, and the three-dimensional structure of the protein is unknown. The enzyme does contain several sequences that could be nucleotide binding sites, but none of them are an exact match to consensus sequences. Using a combination of site-directed mutagenesis and UV photoaffinity cross-linking, we have identified five amino acid residues that are critical for catalysis. Some of these amino acids are found within the poorly conserved nucleotide binding consensus structures, while others represent new motifs. Two active site lysines can be cross-linked to photoaffinity probes. The site of cross-linking depends on the probe used. The identification of these critical residues highlights how distinct GFPP is from other nucleotide-sugar pyrophosphorylases.

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“…The approximate molecular weight of the rmlA protein was 50 kDa while the molecular weight of the pgmG protein was 31 kDa. The enzyme glucose-1phosphate uridylyltransferase, encoded by ugpG, catalyzes the production of UDP-glucose and pyrophosphate from its substrates glucose-1-phosphate and UTP in S. elodea ATCC 31461 [57]. The X-ray crystal structure of the glucose-1-phosphate uridylyltransferase from ATCC 31461 has been elucidated [58].…”

Section: Genetics Of Gellan Biosynthesismentioning

confidence: 99%

Synthesis of the Microbial Polysaccharide Gellan from Dairy and Plant-Based Processing Coproducts

West

2021

Polysaccharides

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This review examines the production of the microbial polysaccharide gellan, synthesized by Sphingomonas elodea, on dairy and plant-based processing coproducts. Gellan is a water-soluble gum that structurally exists as a tetrasaccharide comprised of 20% glucuronic acid, 60% glucose and 20% rhamnose, for which various food, non-food and biomedical applications have been reported. A number of carbon and nitrogen sources have been tested to determine whether they can support bacterial gellan production, with several studies attempting to optimize gellan production by varying the culture conditions. The genetics of the biosynthesis of gellan has been explored in a number of investigations and specific genes have been identified that encode the enzymes responsible for the synthesis of this polysaccharide. Genetic mutants exhibiting overproduction of gellan have also been identified and characterized. Several dairy and plant-based processing coproducts have been screened to learn whether they can support the production of gellan in an attempt to lower the cost of synthesizing the microbial polysaccharide. Of the processing coproducts explored, soluble starch as a carbon source supported the highest gellan production by S. elodea grown at 30 °C. The corn processing coproducts corn steep liquor or condensed distillers solubles appear to be effective nitrogen sources for gellan production. It was concluded that further research on producing gellan using a combination of processing coproducts could be an effective solution in lowering its overall production costs.

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Characterization of the ugpG gene encoding a UDP-glucose pyrophosphorylase from the gellan gum producer Sphingomonas paucimobilis ATCC 31461

Cited by 22 publications

References 48 publications

The evolutionary life cycle of the polysaccharide biosynthetic gene cluster based on the Sphingomonadaceae

The evolutionary life cycle of the polysaccharide biosynthetic gene cluster based on the Sphingomonadaceae

Identification of Catalytic Amino Acids in the Human GTP Fucose Pyrophosphorylase Active Site

Synthesis of the Microbial Polysaccharide Gellan from Dairy and Plant-Based Processing Coproducts

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