Oxalate decarboxylase

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

oxalate + H⁺ 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 1UW8, 2UY8, 2UY9, 2UYA, and 2UYB.

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. 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. PMID 11546787.

External links

The CAS registry number for this enzyme class is 9024-97-9.

• IUBMB entry for 4.1.1.2

• KEGG entry for 4.1.1.2

• BRENDA entry for 4.1.1.2

• NiceZyme view of 4.1.1.2

• EC2PDB: PDB structures for 4.1.1.2

• PRIAM entry for 4.1.1.2

• PUMA2 entry for 4.1.1.2

• IntEnz: Integrated Enzyme entry for 4.1.1.2

• MetaCyc entry for 4.1.1.2

• Atomic-resolution structures of enzymes belonging to this class

Gene Ontology (GO) codes

• EGO entry for GO code 0046564: oxalate decarboxylase

• AMIGO entry for GO code 0046564: oxalate decarboxylase

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