Oxalate decarboxylase

From Wikipedia, the free encyclopedia

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

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.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1UW8, 2UY8, 2UY9, 2UYA, and 2UYB.

[edit] References

IUBMB entry for 4.1.1.2
BRENDA references for 4.1.1.2 (Recommended.)
PubMed references for 4.1.1.2
PubMed Central references for 4.1.1.2
Google Scholar references for 4.1.1.2
HAYAISHI O, JAKOBY WB, OHMURA E (1956). "Enzymatic decarboxylation of oxalic acid". J. Biol. Chem. 222: 435–46. PMID 13367015.
Tanner A, Bornemann S (2000). "Bacillus subtilis YvrK is an acid-induced oxalate decarboxylase". J. Bacteriol. 182: 5271–3. doi:10.1128/JB.182.18.5271-5273.2000. PMID 10960116.
Tanner A, Bowater L, Fairhurst SA, Bornemann S (2001). "Oxalate decarboxylase requires manganese and dioxygen for activity Overexpression and characterization of Bacillus subtilis YvrK and YoaN". J. Biol. Chem. 276: 43627–34. doi:10.1074/jbc.M107202200. PMID 11546787.