Biosynthetic pathways in Oxalobacter formigenes

Cornick, Nancy A.

doi:10.31274/rtd-180813-11245

Cited by 3 publications

(3 citation statements)

References 80 publications

(75 reference statements)

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“…The lack of incorporation of 14C03 into alanine - (Table 3) and the apparent differences in the relative specific activities of alanine derived from [I-I%]-and [2-l4]-acetate suggest that Oxalobacter formigenes may incorporate acetate into pyruvate by a different mechanism. Subsequent data obtained by growing cells with [13C]acetate supports this and indicates that 40% of the acetate incorporated into amino acids enters as single carbons (Cornick 1995;Cornick et al 1996).…”

Section: Enzymatic Activitymentioning

confidence: 67%

Assimilation of oxalate, acetate, and CO₂byOxalobacter formigenes

Cornick¹,

Allison²

1996

Can. J. Microbiol.

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Oxalobacter formigenes is the only well-documented oxalate-degrading bacterium isolated from the gastrointestinal tract of animals. The production of ATP by Oxalobacter formigenes is centered around oxalate metabolism and oxalate is required for growth. A small amount of acetate (0.5 mM) is also required. Oxalate is decarboxylated to formate plus CO2 in nearly equimolar amounts. Experiments were conducted to determine which potential carbon sources (oxalate, acetate, formate, CO2) were assimilated by Oxalobacter formigenes and which metabolic pathways were operative in carbon assimilation. Measurements of the specific activities of total cell carbon after growth with different 14C-labeled precursors indicated that at least 54% of the total cell carbon was derived from oxalate and at least 7% was derived from acetate. Carbonate was also assimilated, but formate was not a significant source of cell carbon. Labeling patterns in amino acids from cells grown in [14C]oxalate or 14CO3 were different; however, in both cases 14C was widely distributed into most cellular amino acids. Carbon from [14C]acetate was less widely distributed and detected mainly in those amino acids known to be derived from alpha-ketoglutarate, oxaloacetate, and pyruvate. Cell-free extracts contained citrate synthase, isocitrate dehydrogenase, and malate dehydrogenase activities. The labeling observed in amino acids derived from acetate is in agreement with the function of these enzymes in biosynthesis and indicates that the majority of acetate carbon entered into amino acid biosynthesis via well-known pathways.

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Section: Enzymatic Activitymentioning

confidence: 67%

Assimilation of oxalate, acetate, and CO₂byOxalobacter formigenes

Cornick¹,

Allison²

1996

Can. J. Microbiol.

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“…This suggests some scrambling of label between intermediates that oxalate and acetate have in common. Preliminary data from cells grown in [14C]oxalate or [14C]acetate indicated that unidentified precursor metabolites are labeled by both oxalate and acetate but not by C 0 3 (Cornick 1995). Although the metabolism of other oxalate-degrading bacteria has not been examined using 13C-NMR, scrambling of carbons has been described in several other genera of bacteria.…”

Section: Discussionmentioning

confidence: 99%

Biosynthesis of amino acids byOxalobacter formigenes: analysis using¹³C-NMR

Cornick¹,

Yan²,

Bank³

et al. 1996

Can. J. Microbiol.

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The gram-negative anaerobe Oxalobacter formigenes, grows on oxalate as the principal carbon and energy source, but a small amount of acetate is also required for growth. Experiments were conducted to determine the distribution and the position of label in cellular amino acids from cells grown on [13C]oxalate, [13C]acetate (1-13C, 2-13C, and U-13C), and13CCO3. The labeling pattern (determined with NMR spectroscopy) of amino acids was consistent with their formation through common biosynthetic pathways. The majority of the carbons in the amino acids that are usually derived from pyruvate, oxaloacetate, α-ketoglutarate, 3-phosphoglycerate, and carbon in the aromatic amino acids were labeled by oxalate. Carbon from13CO3was assimilated primarily into amino acids expected to be derived from oxaloacetate and α-ketoglutarate. Approximately 60% of the acetate that was assimilated into amino acids was incorporated as a C2unit into proline, arginine, glutamate, and leucine. The pattern of labeling from acetate in glutamate, arginine, and proline was consistent with acetate incorporation via citrate (si)-synthase and subsequent formation of α-ketoglutarate via the first third of the tricarboxylic acid pathway. Acetate was also assimilated into amino acids derived from pyruvate and oxaloacetate, but results indicated that this incorporation was as single carbon atoms. Based on these findings, cell-free extracts were assayed for several key biosynthetic enzymes. Enzymatic activities found included glutamate dehydrogenase, phosphoenolpyruvate carboxylase, and pyruvate carboxylase. These findings are consistent with proposed biosynthetic mechanisms.Key words: oxalate, carbon flow, carbon assimilation.

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“…310 21, 1986. 311 Repair lime-based mortars are degraded by carbonation facilitated by CO 2 , dissolution by SO 2 , hydration of calcium silicates. Two key climatic elements are responsible: wind speed and rainfall intensity.…”

Section: Construction Materialsmentioning

confidence: 99%

Weathering of Compounded Products

Wypych¹

2013

Handbook of Material Weathering

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Biosynthetic pathways in Oxalobacter formigenes

Cited by 3 publications

References 80 publications

Assimilation of oxalate, acetate, and CO₂byOxalobacter formigenes

Assimilation of oxalate, acetate, and CO₂byOxalobacter formigenes

Biosynthesis of amino acids byOxalobacter formigenes: analysis using¹³C-NMR

Weathering of Compounded Products

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Biosynthetic pathways in Oxalobacter formigenes

Cited by 3 publications

References 80 publications

Assimilation of oxalate, acetate, and CO2byOxalobacter formigenes

Assimilation of oxalate, acetate, and CO2byOxalobacter formigenes

Biosynthesis of amino acids byOxalobacter formigenes: analysis using13C-NMR

Weathering of Compounded Products

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Assimilation of oxalate, acetate, and CO₂byOxalobacter formigenes

Assimilation of oxalate, acetate, and CO₂byOxalobacter formigenes

Biosynthesis of amino acids byOxalobacter formigenes: analysis using¹³C-NMR