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Oxalate Decarboxylase, Active Bacterial recombinant protein
YvrK
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | O34714 |
|---|---|
| Concentration | 2 |
| Calculated MW | 45.9 kDa (384 aa + NT 6xHis-tag) |
| Gene ID | 938620 |
|---|---|
| Gene Symbol | OxdC |
| Other Names | YvrK |
| Gene Source | Bacillus Subtilis |
| Source | E. coli |
| Assay&Purity | SDS-PAGE; ≥98% |
| Assay2&Purity2 | N/A; |
| Recombinant | Yes |
| Target/Specificity | Oxalate decarboxylase |
| Format | Liquid |
| Storage | -80°C; 2 mg/mL solution in 20 mM Tris, pH 8 containing 20% glycerol. |
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Provided below are standard protocols that you may find useful for product applications.
Background
Oxalate decarboxylase (OxdC, EC4.1.1.2) is a manganese-containing enzyme, which decomposes oxalic acid and oxalate. With OxdC catalysis, oxalate is split into formate and CO2. This enzyme belongs to the family of lyases, specifically the carboxy-lyases, which cleave carbon-carbon bonds. The systematic name of this enzyme class is oxalate carboxy-lyase (formate-forming). This enzyme is also called oxalate carboxy-lyase. The enzyme is composed of two cupin domains, each of which contains a Mn (II) ion. This enzyme participates in glyoxylate and dicarboxylate metabolism. This enzyme has been recognized for diagnostics in diverse biotechnological applications such as the clinical assay of oxalate in blood and urine, therapeutics, process industry, and agriculture to lower oxalate levels in foods and the environment. The recombinant protein made from the Bacillus Subtilis sequence includes OxdC with N-terminal His-tag.
References
Wipat A.,et al.Microbiology 144:1593-1600(1998).
Kunst F.,et al.Nature 390:249-256(1997).
Tanner A.,et al.J. Bacteriol. 182:5271-5273(2000).
Tanner A.,et al.J. Biol. Chem. 276:43627-43634(2001).
MacLellan S.R.,et al.Mol. Microbiol. 69:954-967(2008).
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