Reduction of Oxalate Content of Foods by the Oxalate Degrading Bacterium, <i>Eubacterium Lentum</i> WYH‐1

Itô, Haruo; Miura, Naoto; Masai, Motoyuki; Yamamoto, Kazuhiro; Hara, T.

doi:10.1111/j.1442-2042.1996.tb00626.x

Cited by 32 publications

(25 citation statements)

References 18 publications

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“…The oxalate-degrading human bacteria described to date were only anaerobes including Oxalobacter formigenes, Eubacterium lentum, Bifidobacterium adolescentis, and Propionibacterium acnes (2,17,19). There has been no previous report of facultatively anaerobic oxalate-degrading E. faecalis.…”

Section: Discussionmentioning

confidence: 89%

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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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Section: Discussionmentioning

confidence: 89%

“…Therefore, oxalate-degrading bacteria has only been studied by a few investigators. In 1994, Ito and associates found another oxalate-degrading organism, Eubacterium lentum, and they purified two enzymes (oxalyl-CoA decarboxylase and formylCoA transferase) that are involved in oxalate degradation (17,19).…”

mentioning

confidence: 99%

Oxalate‐Degrading Enterococcus faecalis

Hokama

Honma

Toma

et al. 2000

Microbiology and Immunology

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“…Other oxalate-degrading bacteria isolated from the human GIT include Eubacterium lentum (22) and Enterococcus faecalis (20 . They observed a reduction in the excreted oxalate in the patients and showed that L. acidophilus and S. thermophilus could reduce oxalate concentrations in vitro, even when their growth was partially inhibited by this compound.…”

Section: Discussionmentioning

confidence: 99%

Transcriptional and Functional Analysis of Oxalyl-Coenzyme A (CoA) Decarboxylase and Formyl-CoA Transferase Genes from Lactobacillus acidophilus

Azcarate‐Peril

Bruno-Bárcena²,

Hassan³

et al. 2006

Appl Environ Microbiol

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Oxalic acid is found in dietary sources (such as coffee, tea, and chocolate) or is produced by the intestinal microflora from metabolic precursors, like ascorbic acid. In the human intestine, oxalate may combine with calcium, sodium, magnesium, or potassium to form less soluble salts, which can cause pathological disorders such as hyperoxaluria, urolithiasis, and renal failure in humans. In this study, an operon containing genes homologous to a formyl coenzyme A transferase gene (frc) and an oxalyl coenzyme A decarboxylase gene (oxc) was identified in the genome of the probiotic bacterium Lactobacillus acidophilus. Physiological analysis of a mutant harboring a deleted version of the frc gene confirmed that frc expression specifically improves survival in the presence of oxalic acid at pH 3.5 compared with the survival of the wild-type strain. Moreover, the frc mutant was unable to degrade oxalate. These genes, which have not previously been described in lactobacilli, appear to be responsible for oxalate degradation in this organism. Transcriptional analysis using cDNA microarrays and reverse transcription-quantitative PCR revealed that mildly acidic conditions were a prerequisite for frc and oxc transcription. As a consequence, oxalate-dependent induction of these genes occurred only in cells first adapted to subinhibitory concentrations of oxalate and then exposed to pH 5.5. Where genome information was available, other lactic acid bacteria were screened for frc and oxc genes. With the exception of Lactobacillus gasseri and Bifidobacterium lactis, none of the other strains harbored genes for oxalate utilization.

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“…In a related study (230) As an alternative to treatment of patients with these conditions, it is possible to reduce the oxalate content of food prior to its being eaten (176; R. Yoshida, T. Tanaka, and Y. Hotta, 5 March 1994, European patent application 0639329 A1). In one such method, it was shown (132) that the oxalate-degrading bacterium Eubacterium lentum WYH-1, isolated from human feces (133), could completely degrade 1 mg of oxalate per ml in artificial intestinal juice or the oxalate in an infusion of black tea-one of the major sources of oxalate in the human diet (321). Similarly, barley roots in a stirred-tank reactor have been used to reduce the level of oxalate in ginger juice (313).…”

Section: Medical Diagnosis and Treatmentmentioning

confidence: 99%

Microbial Relatives of the Seed Storage Proteins of Higher Plants: Conservation of Structure and Diversification of Function during Evolution of the Cupin Superfamily

Dunwell

Khuri

Gane

2000

Microbiol Mol Biol Rev

313

297

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SUMMARY This review summarizes the recent discovery of the cupin superfamily (from the Latin term “cupa,” a small barrel) of functionally diverse proteins that initially were limited to several higher plant proteins such as seed storage proteins, germin (an oxalate oxidase), germin-like proteins, and auxin-binding protein. Knowledge of the three-dimensional structure of two vicilins, seed proteins with a characteristic β-barrel core, led to the identification of a small number of conserved residues and thence to the discovery of several microbial proteins which share these key amino acids. In particular, there is a highly conserved pattern of two histidine-containing motifs with a varied intermotif spacing. This cupin signature is found as a central component of many microbial proteins including certain types of phosphomannose isomerase, polyketide synthase, epimerase, and dioxygenase. In addition, the signature has been identified within the N-terminal effector domain in a subgroup of bacterial AraC transcription factors. As well as these single-domain cupins, this survey has identified other classes of two-domain bicupins including bacterial gentisate 1,2-dioxygenases and 1-hydroxy-2-naphthoate dioxygenases, fungal oxalate decarboxylases, and legume sucrose-binding proteins. Cupin evolution is discussed from the perspective of the structure-function relationships, using data from the genomes of several prokaryotes, especially Bacillus subtilis. Many of these functions involve aspects of sugar metabolism and cell wall synthesis and are concerned with responses to abiotic stress such as heat, desiccation, or starvation. Particular emphasis is also given to the oxalate-degrading enzymes from microbes, their biological significance, and their value in a range of medical and other applications.

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Reduction of Oxalate Content of Foods by the Oxalate Degrading Bacterium, Eubacterium Lentum WYH‐1

Abstract: Eubacterium lentum WYH-1 was able to efficiently decompose the oxalate in foods.

Cited by 32 publications

References 18 publications

Oxalate‐Degrading Enterococcus faecalis

Oxalate‐Degrading Enterococcus faecalis

Transcriptional and Functional Analysis of Oxalyl-Coenzyme A (CoA) Decarboxylase and Formyl-CoA Transferase Genes from Lactobacillus acidophilus

Microbial Relatives of the Seed Storage Proteins of Higher Plants: Conservation of Structure and Diversification of Function during Evolution of the Cupin Superfamily

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