Oxalate degrading enzyme

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The oxalate anion is equivalent to two molecules of carbon dioxide to which two electrons have been added. Removal of these electrons in a redox reaction may permit liberation of carbon dioxide. Structure of oxalate.svg
The oxalate anion is equivalent to two molecules of carbon dioxide to which two electrons have been added. Removal of these electrons in a redox reaction may permit liberation of carbon dioxide.

An oxalate degrading enzyme is a type of enzyme that catalyzes the biodegradation of oxalate. Enzymes in this class include oxalate oxidase, oxalate decarboxylase, oxalyl-CoA decarboxylase, and formyl-CoA transferase.

Contents

Specific enzymes

Oxalate oxidase (Enzyme Commission number EC 1.2.3.4 [2] )occurs mainly in plants. It can degrade oxalic acid into carbon dioxide and hydrogen peroxide. [3]

Oxalate decarboxylase (OXDC,EC 4.1.1.2) is a kind of oxalate degrading enzyme containing Mn2+, [4] found mainly in fungi or some bacteria. Brown rot fungi secrete oxalate to break down cellulose fibers of wood, but deploy this enzyme to permit regulatory control over the total quantity of oxalate present. [5] It can appear in the absence of other cofactors under the action of the degradation of oxalic acid directly to form formic acid and CO2.

Oxalyl-CoA decarboxylase(EC 4.1.1.8)mainly mediates degradation of bacterial oxalic acid.

Formyl-CoA transferase (EC 2.8.3.16)mediates the exchange of oxalyl and formyl groups on coenzyme A, interconverting formyl-CoA and oxalyl-CoA.

Calcium oxalate stones and oxalate degrading enzymes

Calcium oxalate is the main component of the most common type of kidney stone in humans.

Related Research Articles

<span class="mw-page-title-main">Oxalic acid</span> Simplest dicarboxylic acid

Oxalic acid is an organic acid with the systematic name ethanedioic acid and chemical formula HO−C(=O)−C(=O)−OH, also written as (COOH)2 or (CO2H)2 or H2C2O4. It is the simplest dicarboxylic acid. It is a white crystalline solid that forms a colorless solution in water. Its name comes from the fact that early investigators isolated oxalic acid from flowering plants of the genus Oxalis, commonly known as wood-sorrels. It occurs naturally in many foods. Excessive ingestion of oxalic acid or prolonged skin contact can be dangerous.

In biochemistry, a lyase is an enzyme that catalyzes the breaking of various chemical bonds by means other than hydrolysis and oxidation, often forming a new double bond or a new ring structure. The reverse reaction is also possible. For example, an enzyme that catalyzed this reaction would be a lyase:

<span class="mw-page-title-main">Oxalyl chloride</span> Chemical compound

Oxalyl chloride is an organic chemical compound with the formula Cl−C(=O)−C(=O)−Cl. This colorless, sharp-smelling liquid, the diacyl chloride of oxalic acid, is a useful reagent in organic synthesis.

<span class="mw-page-title-main">Malonyl-CoA decarboxylase</span> Class of enzymes

Malonyl-CoA decarboxylase, is found in bacteria and humans and has important roles in regulating fatty acid metabolism and food intake, and it is an attractive target for drug discovery. It is an enzyme associated with Malonyl-CoA decarboxylase deficiency. In humans, it is encoded by the MLYCD gene.

Oxalobacter formigenes is a Gram negative oxalate-degrading anaerobic bacterium that was first isolated from the gastrointestinal tract of a sheep in 1985. To date, the bacterium has been found to colonize the large intestines of numerous vertebrates, including humans, and has even been isolated from freshwater sediment. It processes oxalate by decarboxylation into formate, producing energy for itself in the process.

<span class="mw-page-title-main">Wood-decay fungus</span> Any species of fungus that digests moist wood, causing it to rot

A wood-decay or xylophagous fungus is any species of fungus that digests moist wood, causing it to rot. Some species of wood-decay fungi attack dead wood, such as brown rot, and some, such as Armillaria, are parasitic and colonize living trees. Excessive moisture above the fibre saturation point in wood is required for fungal colonization and proliferation. In nature, this process causes the breakdown of complex molecules and leads to the return of nutrients to the soil. Wood-decay fungi consume wood in various ways; for example, some attack the carbohydrates in wood, and some others decay lignin. The rate of decay of wooden materials in various climates can be estimated by empirical models.

<span class="mw-page-title-main">Oxalate oxidase</span>

In enzymology, an oxalate oxidase (EC 1.2.3.4) is an oxalate degrading enzyme that catalyzes the chemical reaction:

In enzymology, a manganese peroxidase (EC 1.11.1.13) is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Methylmalonyl-CoA carboxytransferase</span>

In enzymology, a methylmalonyl-CoA carboxytransferase is an enzyme that catalyzes the chemical reaction

In enzymology, a formyl-CoA transferase is an enzyme that catalyzes the chemical reaction

In enzymology, an oxalate CoA-transferase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Oxalate decarboxylase</span>

In enzymology, an oxalate decarboxylase (EC 4.1.1.2) is an oxalate degrading enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Oxalyl-CoA decarboxylase</span>

The enzyme oxalyl-CoA decarboxylase (OXC) (EC 4.1.1.8), primarily produced by the gastrointestinal bacterium Oxalobacter formigenes, catalyzes the chemical reaction

In enzymology, an oxalate—CoA ligase is an enzyme that catalyzes the chemical reaction

<span class="mw-page-title-main">Dioxane tetraketone</span> Chemical compound

Dioxane tetraketone (or 1,4-dioxane-2,3,5,6-tetrone) is an organic compound with the formula C4O6. It is an oxide of carbon (an oxocarbon), which can be viewed as the fourfold ketone of dioxane. It can also be viewed as the cyclic dimer of oxiranedione (C2O3), the hypothetical anhydride of oxalic acid.

<span class="mw-page-title-main">Fungal extracellular enzyme activity</span> Enzymes produced by fungi and secreted outside their cells

Extracellular enzymes or exoenzymes are synthesized inside the cell and then secreted outside the cell, where their function is to break down complex macromolecules into smaller units to be taken up by the cell for growth and assimilation. These enzymes degrade complex organic matter such as cellulose and hemicellulose into simple sugars that enzyme-producing organisms use as a source of carbon, energy, and nutrients. Grouped as hydrolases, lyases, oxidoreductases and transferases, these extracellular enzymes control soil enzyme activity through efficient degradation of biopolymers.

<span class="mw-page-title-main">Coenzyme A transferases</span> Coenzyme A transferases

Coenzyme A transferases (CoA-transferases) are transferase enzymes that catalyze the transfer of a coenzyme A group from an acyl-CoA donor to a carboxylic acid acceptor. Among other roles, they are responsible for transfer of CoA groups during fermentation and metabolism of ketone bodies. These enzymes are found in all three domains of life.

<small>L</small>-Tryptophan decarboxylase Enzyme

L-Tryptophan decarboxylase is an enzyme distinguished by the substrate L-tryptophan.

Oxalobacter aliiformigenes is a Gram negative, non-spore-forming, oxalate-degrading anaerobic bacterium that was first isolated from human fecal samples. O. aliiformigenes consumes oxalate as its main carbon source but is negative for indole production and negative for sulfate and nitrate reduction. Cells appear rod shaped, though occasionally present as curved, and do not possess flagella.

Oxalobacter paraformigenes is a Gram negative, non-spore-forming, oxalate-degrading anaerobic bacterium that was first isolated from human fecal samples. O. paraformigenes may have a role in calcium oxalate kidney stone disease because of its unique ability to utilize oxalate as its primary carbon source.

References

  1. Gibson, Marcus I.; et al. (2016-01-12). "One-carbon chemistry of oxalate oxidoreductase captured by X-ray crystallography" (PDF). Proceedings of the National Academy of Sciences. PNAS. 113 (2): 320–325. doi:10.1073/pnas.1518537113.
  2. Daniel L. Purich, R. Donald Allison (Jan 4, 2003). The Enzyme Reference: A Comprehensive Guidebook to Enzyme Nomenclature, Reactions, and Methods . Academic Press. p.  633. ISBN   9780125680417.
  3. G. Alan Rose, ed. (2012-12-06). Oxalate Metabolism in Relation to Urinary Stone. Springer. p. 50. ISBN   9781447116264.
  4. ENZYME entry: EC 4.1.1.2, ExPASy Bioinformatics Resource Portal, accessed 19 March 2017.
  5. Hastrup, Anne Christine Steenkjær; Green, Frederick III; Lebow, Patricia K.; Jensen, Bo (2012). "Enzymatic oxalic acid regulation correlated with wood degradation in four brown-rot fungi" (PDF). International Biodeterioration and Biodegradation. 75: 109–114. doi:10.1016/j.ibiod.2012.05.030.