Bacterial conversion of D-glucarate to glycerate and pyruvate

Blumenthal, Harold J.; Fish, Donald C.

doi:10.1016/0006-291x(63)90341-3

Cited by 35 publications

(28 citation statements)

References 9 publications

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“…The enzyme glycerate kinase (GarK) is central to both of these pathways; in E. coli, it catalyzes the synthesis of 2-phosphoglycerate by utilizing glyoxylate when the latter is available as the main carbon substrate (21,27). When D-glucarate, D-glycerate, or D-galactarate is available as the carbon source, GarK utilizes the substrate through a catabolic pathway (3). The gene garK is 3.4-fold upregulated by H 2 ( Table 2) .…”

Section: Resultsmentioning

confidence: 99%

Hydrogen-Stimulated Carbon Acquisition and Conservation in Salmonella enterica Serovar Typhimurium

et al. 2011

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Salmonella enterica serovar Typhimurium can utilize molecular hydrogen for growth and amino acid transport during anaerobic growth. Via microarray we identified H 2 gas-affected gene expression changes in Salmonella. The addition of H 2 caused altered expression of 597 genes, of which 176 genes were upregulated and 421 were downregulated. The significantly H 2 -upregulated genes include those that encode proteins involved in the transport of iron, manganese, amino acids, nucleosides, and sugars. Genes encoding isocitrate lyase (aceA) and malate synthase (aceB), both involved in the carbon conserving glyoxylate pathway, and genes encoding the enzymes of the D-glucarate and D-glycerate pathways (gudT, gudD, garR, garL, garK) are significantly upregulated by H 2 . Cells grown with H 2 showed markedly increased AceA enzyme activity compared to cells without H 2 . Mutant strains with deletion of either aceA or aceB had reduced H 2 -dependent growth rates. Genes encoding the glutamine-specific transporters (glnH, glnP, glnQ) were upregulated by H 2 , and cells grown with H 2 showed increased [ 14 C]glutamine uptake. Similarly, the mannose uptake system genes (manX, manY) were upregulated by H 2, and cells grown with H 2 showed about 2.0-fold-increased [ 14 C]D-mannose uptake compared to the cells grown without H 2 . Hydrogen stimulates the expression of genes involved in nutrient and carbon acquisition and carbon-conserving pathways, linking carbon and energy metabolism to sustain H 2 -dependent growth.

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Section: Resultsmentioning

confidence: 99%

Hydrogen-Stimulated Carbon Acquisition and Conservation in Salmonella enterica Serovar Typhimurium

et al. 2011

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“…It might be that the UAO represents a catabolic enzyme and the oxidation of galacturonic acid and glucuronic acid generated by hydrolysis of polysaccharides is, as in bacteria (2,4,6), the first step in the utilization of uronic acids as a source of carbon. Bacteria convert uronic acids to various organic acids, including a-ketoglutaric acid (6) and pyruvic acid (4). Since the enzyme was found to oxidize polygalacturonic acid, it might also be that the natural substrate is a polysaccharide containing terminal uronic acid residues.…”

Section: Resultsmentioning

confidence: 99%

“…Bacteria contain an enzyme, hexuronic acid dehydrogenase, which catalyzes the NAD-linked oxidation of hexuronic acids to hexaric acids. This reaction is the first step in the catabolism of uronic acids in bacteria (2,4,6).…”

mentioning

confidence: 99%

Metabolism of Uronic Acids in Plant Tissues

Riov¹

1975

Plant Physiol.

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A new enzyme, named uronic acid oxidase, was extracted and Free uronic acids generated within the plant by hydrolysis of uronic acid-rich polysaccharides or by hydrolysis of nucleotides are quickly metabolized; they are reduced, oxidized, decarboxylated, or converted to cell wall polysaccharides (10). Tracer studies have demonstrated that plants are capable of oxidizing D-galacturonic acid and D-glucuronic acid to the corresponding hexaric acids, galactaric acid, and D-glucaric acid (9. 11), but the enzymes involved have not yet been investigated. The enzymic conversion of hexuronic acids to hexaric acids has been studied in animals (13, 18) and especially in bacteria (3, 5, 23). Bacteria contain an enzyme, hexuronic acid dehydrogenase, which catalyzes the NAD-linked oxidation of hexuronic acids to hexaric acids. This reaction is the first step in the catabolism of uronic acids in bacteria (2, 4, 6).Recently, in studying the role of polygalacturonase in abscission of citrus leaf explants (17), we observed that the enzymic preparations used contained an enzyme which oxidized the free galacturonic acid released by the polygalacturonase, as well as the free reducing groups of the substrate, sodium polypectate. Based on preliminary studies, the enzyme was named uronic acid oxidase (17). The present work was designed to isolate and characterize the enzyme which catalyzes the oxidation of uronic acids in citrus leaves.

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“…Enzymatic reactions were stopped by trifluoroacetic acid and neutralized by 5 M K 2 CO 3 . ␣-Ketoglutarate was assayed with glutamate dehydrogenase in the presence of 50 mM NH 4 Cl in 100 mM Tris, pH 7.5.…”

Section: Methodsmentioning

confidence: 99%

“…D-Glucaric acid is a natural product that can serve as a growth substrate for a number of bacteria (3)(4)(5) (4). The genes of E. coli responsible for the different enzymatic activities of the pathway have been identified (6,7).…”

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confidence: 99%

New Insights into the Alternative d-Glucarate Degradation Pathway

Aghaie¹,

Lechaplais

Sirven

et al. 2008

Journal of Biological Chemistry

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Although the D-glucarate degradation pathway is well characterized in Escherichia coli, genetic and biochemical information concerning the alternative pathway proposed in Pseudomonas species and Bacillus subtilis remains incomplete. Acinetobacter baylyi ADP1 is a Gram-negative soil bacterium possessing the alternative pathway and able to grow using D-glucarate as the only carbon source. Based on the annotation of its sequenced genome (1), we have constructed a complete collection of singlegene deletion mutants (2). High throughput profiling for growth on a minimal medium containing D-glucarate as the only carbon source for ϳ2450 mutants led to the identification of the genes involved in D-glucarate degradation. Protein purification after recombinant production in E. coli allowed us to reconstitute the enzymatic pathway in vitro. We describe here the kinetic characterization of D-glucarate dehydratase, D-5-keto-4-deoxyglucarate dehydratase, and of cooperative ␣-ketoglutarate semialdehyde dehydrogenase. Transcription and expression analyses of the genes involved in D-glucarate metabolism within a single organism made it possible to access information regarding the regulation of this pathway for the first time.

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Bacterial conversion of D-glucarate to glycerate and pyruvate

Cited by 35 publications

References 9 publications

Hydrogen-Stimulated Carbon Acquisition and Conservation in Salmonella enterica Serovar Typhimurium

Hydrogen-Stimulated Carbon Acquisition and Conservation in Salmonella enterica Serovar Typhimurium

Metabolism of Uronic Acids in Plant Tissues

New Insights into the Alternative d-Glucarate Degradation Pathway

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