oxalate + H⁺ $rightleftharpoons$ formate + CO₂

Thus, the two substrates of this enzyme are oxalate and H⁺, whereas its two products are 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. This enzyme participates in glyoxylate and dicarboxylate metabolism.

Structural studies

As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes , , , , and .

References

• HAYAISHI O, JAKOBY WB, OHMURA E "Enzymatic decarboxylation of oxalic acid". J. Biol. Chem. 222 435–46.
• Tanner A, Bornemann S "Bacillus subtilis YvrK is an acid-induced oxalate decarboxylase". J. Bacteriol. 182 5271–3.
• Tanner A, Bowater L, Fairhurst SA, Bornemann S "Oxalate decarboxylase requires manganese and dioxygen for activity Overexpression and characterization of Bacillus subtilis YvrK and YoaN". J. Biol. Chem. 276 43627–34.

External links

The CAS registry number for this enzyme class is .

Gene Ontology (GO) codes