| oxalyl-CoA decarboxylase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Oxalyl-CoA decarboxylase homotetramer, Oxalobacter formigenes | |||||||||
| Identifiers | |||||||||
| EC no. | 4.1.1.8 | ||||||||
| CAS no. | 9024-96-8 | ||||||||
| 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 | ||||||||
| |||||||||
The enzyme oxalyl-CoA decarboxylase (OXC) (EC 4.1.1.8), primarily produced by the gastrointestinal bacterium Oxalobacter formigenes, catalyzes the chemical reaction
- oxalyl-CoA formyl-CoA + CO2
OXC belongs to the family of lyases, specifically the carboxy-lyases (decarboxylases), which cleave carbon-carbon bonds. The systematic name of this enzyme class is oxalyl-CoA carboxy-lyase (formyl-CoA-forming). Other names in common use include oxalyl coenzyme A decarboxylase, and oxalyl-CoA carboxy-lyase. This enzyme participates in glyoxylate and dicarboxylate metabolism. It employs one cofactor, thiamin diphosphate (TPP), and plays a key role in catabolism of oxalate, a highly toxic compound that is a product of the oxidation of carbohydrates in many bacteria and plants.[1] Oxalyl-CoA decarboxylase is extremely important for the elimination of ingested oxalates found in human foodstuffs like coffee, tea, and chocolate,[2] and the ingestion of such foods in the absence of Oxalobacter formigenes in the gut can result in kidney disease or even death as a result of oxalate poisoning.[3]
- ^ Baetz AL, Allison MJ (July 1990). "Purification and characterization of formyl-coenzyme A transferase from Oxalobacter formigenes". Journal of Bacteriology. 172 (7): 3537–40. doi:10.1128/jb.172.7.3537-3540.1990. PMC 213325. PMID 2361939.
- ^ Gasińska A, Gajewska D (2007). "Tea and coffee as the main sources of oxalate in diets of patients with kidney oxalate stones". Roczniki Panstwowego Zakladu Higieny. 58 (1): 61–7. PMID 17711092.
- ^ Turroni S, Bendazzoli C, Dipalo SC, Candela M, Vitali B, Gotti R, Brigidi P (August 2010). "Oxalate-degrading activity in Bifidobacterium animalis subsp. lactis: impact of acidic conditions on the transcriptional levels of the oxalyl coenzyme A (CoA) decarboxylase and formyl-CoA transferase genes". Applied and Environmental Microbiology. 76 (16): 5609–20. Bibcode:2010ApEnM..76.5609T. doi:10.1128/AEM.00844-10. PMC 2918965. PMID 20601517.