oxalate decarboxylase | |||||||||
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Oxalate decarboxylase hexamer, Bacillus subtilis | |||||||||
Identifiers | |||||||||
EC no. | 4.1.1.2 | ||||||||
CAS no. | 9024-97-9 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, an oxalate decarboxylase (EC 4.1.1.2) is an oxalate degrading 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
- HAYAISHI O, JAKOBY WB, OHMURA E (1956). "Enzymatic decarboxylation of oxalic acid". J. Biol. Chem. 222 (1): 435–46. doi:10.1016/S0021-9258(19)50807-9. PMID 13367015.
- Tanner A, Bornemann S (2000). "Bacillus subtilis YvrK is an acid-induced oxalate decarboxylase". J. Bacteriol. 182 (18): 5271–3. doi:10.1128/JB.182.18.5271-5273.2000. PMC 94680. 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 (47): 43627–34. doi:10.1074/jbc.M107202200. PMID 11546787.
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