Purification and characterization of oxalyl-coenzyme A decarboxylase from Oxalobacter formigenes

Baetz, A L; Allison, Milton J.

doi:10.1128/jb.171.5.2605-2608.1989

Cited by 103 publications

(92 citation statements)

References 17 publications

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“…OOR is the first protein shown to catalyze anaerobic oxalate oxidation, unlike previously described anaerobic enzymes that produce CO 2 and formyl-CoA (6,9). Although several features (e.g.…”

Section: Discussionmentioning

confidence: 99%

“…Formyl-CoA transferase then exchanges the formyl group for an oxalyl-group on CoA, thus producing formate and regenerating oxalyl-CoA. Energy for growth on oxalate in O. formigenes results from a formate-oxalate antiporter, which generates an electrochemical transmembrane gradient for ATP synthesis (5,6), so most formate produced is excreted rather than oxidized (7). Other organisms, such as Cupriavidus oxalaticus, also use oxalyl-CoA decarboxylase to metabolize oxalate but use formate dehydrogenase to generate NADH with the electrons derived from oxalate (8,9).…”

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confidence: 99%

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Identification and Characterization of Oxalate Oxidoreductase, a Novel Thiamine Pyrophosphate-dependent 2-Oxoacid Oxidoreductase That Enables Anaerobic Growth on Oxalate

Pierce

Becker

Ragsdale

2010

Journal of Biological Chemistry

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Moorella thermoacetica is an anaerobic acetogen, a class of bacteria that is found in the soil, the animal gastrointestinal tract, and the rumen. This organism engages the Wood-Ljungdahl pathway of anaerobic CO 2 fixation for heterotrophic or autotrophic growth. This paper describes a novel enzyme, oxalate oxidoreductase (OOR), that enables M. thermoacetica to grow on oxalate, which is produced in soil and is a common component of kidney stones. Exposure to oxalate leads to the induction of three proteins that are subunits of OOR, which oxidizes oxalate coupled to the production of two electrons and CO 2 or bicarbonate. Like other members of the 2-oxoacid: ferredoxin oxidoreductase family, OOR contains thiamine pyrophosphate and three [Fe 4 S 4 ] clusters. However, unlike previously characterized members of this family, OOR does not use coenzyme A as a substrate. Oxalate is oxidized with a k cat of 0.09 s ؊1 and a K m of 58 M at pH 8. OOR also oxidizes a few other 2-oxoacids (which do not induce OOR) also without any requirement for CoA. The enzyme transfers its reducing equivalents to a broad range of electron acceptors, including ferredoxin and the nickel-dependent carbon monoxide dehydrogenase. In conjunction with the well characterized WoodLjungdahl pathway, OOR should be sufficient for oxalate metabolism by M. thermoacetica, and it constitutes a novel pathway for oxalate metabolism.Moorella thermoacetica is a strictly anaerobic Gram-positive acetogenic bacterium. Acetogens are commonly found in the soil, animal gastrointestinal tract, and the rumen and grow heterotrophically or autotrophically on many different electron donors. Electrons from these substrates are used to reduce CO 2 to acetate by the Wood-Ljungdahl pathway. During growth by this pathway, acetate and cell mass are the only growth products, and electron-rich growth substrates like glucose are converted stoichiometrically to acetate; therefore, M. thermoacetica is called a homoacetogen. M. thermoacetica can use other electron acceptors (e.g. nitrate, nitrite, thiosulfate, and dimethyl sulfoxide). Under most conditions, nitrate reduction occurs preferentially to CO 2 reduction, and nitrate has been shown to repress autotrophic growth (1, 2). However, oxalate is unique in its properties as an electron donor by M. thermoacetica for acetogenic growth. When both nitrate and CO 2 are provided to cells growing on oxalate, CO 2 is reduced to acetate during exponential growth phase, and nitrate is only used as the electron acceptor during stationary phase (3). Oxalate is the only substrate with which M. thermoacetica has been shown to reduce CO 2 instead of nitrate when both are present.Oxalate (C 2 O 4 2Ϫ ) is the most oxidized two-carbon compound. It is made in high concentrations by some plants and fungi and can reach high micromolar concentrations in soil (4). Oxalate is toxic to mammals but is metabolized by many bacteria and plants by various pathways. In Oxalobacter formigenes, oxalate is first activated to oxalylCoA and then decarboxylated, giv...

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Identification and Characterization of Oxalate Oxidoreductase, a Novel Thiamine Pyrophosphate-dependent 2-Oxoacid Oxidoreductase That Enables Anaerobic Growth on Oxalate

Pierce

Becker

Ragsdale

2010

Journal of Biological Chemistry

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“…Thus, the frequency of oxalate-degrading strains is likely low in this species. is a well studied organism which metabolizes oxalate using oxalyl-CoA decarboxylase and formyl-CoA transferase and produces CO, and formate as the end products at a 1:1 ratio (4,5,23). Although the oxalate-degrading mechanisms of E. faecalis remain to be clarified, oxalate-degrading E. faecalis had 3 proteins (40, 48 and 65 kDa) that were absent in non-oxalate-degrading strain.…”

Section: Discussionmentioning

confidence: 99%

Oxalate‐Degrading Enterococcus faecalis

Hokama

Honma

Toma

et al. 2000

Microbiology and Immunology

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An oxalate-degrading Enterococcus faecalis was isolated from human stools under anaerobic conditions. The bacteria required a poor nutritional environment and repeated subculturing to maintain their oxalate-degrading ability. The E. faecalis produced 3 proteins (65, 48, and 40 kDa) that were not produced by non-oxalate-degrading E. faecalis as examined by SDS-PAGE. Antibodies against oxalyl-coenzyme A decarboxylase (65 kDa) and formyl-coenzyme A transferase (48 kDa) obtained from Oxalobacter formigenes (an oxalate-degrading anaerobic bacterium in the human intestine) reacted with 2 of the proteins (65 and 48 kDa) from the E. faecalis as examined by Western blottings. This is the first report on the isolation of oxalate-degrading facultative anaerobic bacteria from humans.

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“…This organism takes up oxalate from the intestinal lumen via an oxalate/formate exchanger encoded by gene oxlT (8). Oxalate is then metabolized by oxalyl-CoA decarboxylase, encoded by gene oxc (9). The lactic acid bacteria preparation that we studied was shown not to possess oxlT, oxc, or frc (3).…”

Section: Discussionmentioning

confidence: 99%

A Randomized, Controlled Trial of Lactic Acid Bacteria for Idiopathic Hyperoxaluria

Goldfarb

Modersitzki²,

Asplin³

2007

Clinical Journal of the American Society of Nephrology

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Background: Urinary oxalate excretion is an important contributor to calcium oxalate stone formation. Methods of reducing oxalate excretion are not wholly satisfactory, and no controlled trials using them have been performed to prevent stone recurrence. Some lactic acid bacteria can degrade oxalate in vitro. This study sought to reduce urinary oxalate excretion in calcium stone formers with idiopathic hyperoxaluria.Design, setting, participants, and measurements: A randomized, double-blind, placebo-controlled trial was performed of Oxadrop, a mix of four lactic acid bacterium species. This preparation previously reduced oxalate excretion in stone formers with idiopathic and enteric hyperoxaluria. Patients were selected from two stone prevention clinics. Twenty people with calcium stones and idiopathic hyperoxaluria (>40 mg/d) were enrolled and randomly assigned 1:1 in placebo and active preparation arms. Both groups took 3.6 g of granulate each day: Either placebo or the experimental preparation. Participants performed two consecutive 24-h urine collections at baseline, at 28 d of therapy, and at 56 d, after being off the preparation for 4 wk. Diet was replicated at each point.Results: There was no effect of the study preparation: Mean 24-h urinary oxalate excretion in placebo-treated patients was 73.9 mg at baseline and 72.7 mg after treatment, whereas the Oxadrop-treated patients had 59.1 mg at baseline and 55.4 mg after treatment. The preparation was well tolerated; three participants on active treatment experienced mild constipation.Conclusions: In this randomized, placebo-controlled trial, Oxadrop did not reduce urinary oxalate excretion in participants with idiopathic hyperoxaluria.

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Purification and characterization of oxalyl-coenzyme A decarboxylase from Oxalobacter formigenes

Cited by 103 publications

References 17 publications

Identification and Characterization of Oxalate Oxidoreductase, a Novel Thiamine Pyrophosphate-dependent 2-Oxoacid Oxidoreductase That Enables Anaerobic Growth on Oxalate

Identification and Characterization of Oxalate Oxidoreductase, a Novel Thiamine Pyrophosphate-dependent 2-Oxoacid Oxidoreductase That Enables Anaerobic Growth on Oxalate

Oxalate‐Degrading Enterococcus faecalis

A Randomized, Controlled Trial of Lactic Acid Bacteria for Idiopathic Hyperoxaluria

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