Cloning and Expression of the Oxalyl-CoA Decarboxylase Gene From the Bacterium, Oxalobacter formigenes: Prospects for Gene Therapy to Control Ca-Oxalate Kidney Stone Formation

Lung, Hui-yu; Cornelius, Janet G.; Peck, Ammon B.

doi:10.1016/s0272-6386(12)80627-5

Cited by 26 publications

(21 citation statements)

References 9 publications

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“…Membranes were blocked by incubation in 1% gelatin in 10 mM Tris-HCl [pH 8], 150 mM NaCl, and 0.1% Tween 20. The recombinant oxalyl-CoA decarboxylase was detected by using pooled anti-oxalyl-CoA decarboxylase monoclonal antibodies (29) and visualized with rabbit anti-mouse immunoglobulin M alkaline phosphatase secondary antibody. As a positive control, lysates of E. coli cells overexpressing oxalyl-CoA decarboxylase of O. formigenes were used.…”

Section: Methodsmentioning

confidence: 99%

Characterization and Heterologous Expression of the Oxalyl Coenzyme A Decarboxylase Gene from Bifidobacterium lactis

Federici

Vitali

Gotti

et al. 2004

Appl Environ Microbiol

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Section: Methodsmentioning

confidence: 99%

Characterization and Heterologous Expression of the Oxalyl Coenzyme A Decarboxylase Gene from Bifidobacterium lactis

Federici

Vitali

Gotti

et al. 2004

Appl Environ Microbiol

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“…Aside from the implantation of immobilized OXO or the oral administration of recombinant enzymes, there has been a longstanding interest in the potential of gene therapy for treatment of these life-threatening conditions. Although their eventual aim was to clone and utilize the fungal oxalate decarboxylase gene (263; B. Finlayson and A. Peck, 3 November 1988, PCT patent application), success was first achieved in the cloning of the bacterial equivalent (186,187), the oxalyl coenzyme A decarboxylase from Oxalobacter formigenes, an anaerobic oxalate-degrading bacterium found in the mammalian intestine (4,15,165). It is hoped that the increased understanding of the oxalate-degrading enzymes described in this review will soon lead to further advances in this important area of human therapy.…”

Section: Human Gene Therapymentioning

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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“…The oxalylCoA decarboxylase gene from O. formigenes was cloned with the prospect of using it in gene therapy to control kidney stone formation (Lung et al, 1991). Aerobic Pseudomonas oxalaticus OX1 grows on formate generated by the decarboxylation of oxalate which is activated by binding to coenzyme A (Dijkhuizen et al, 1977).…”

Section: Oxalic Acidmentioning

confidence: 99%

Biological detoxification of fungal toxins and its use in plant breeding, feed and food production

1999

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Cloning and Expression of the Oxalyl-CoA Decarboxylase Gene From the Bacterium, Oxalobacter formigenes: Prospects for Gene Therapy to Control Ca-Oxalate Kidney Stone Formation

Cited by 26 publications

References 9 publications

Characterization and Heterologous Expression of the Oxalyl Coenzyme A Decarboxylase Gene from Bifidobacterium lactis

Characterization and Heterologous Expression of the Oxalyl Coenzyme A Decarboxylase Gene from Bifidobacterium lactis

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

Biological detoxification of fungal toxins and its use in plant breeding, feed and food production

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