Oxalate—CoA ligase
| oxalate-CoA ligase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 6.2.1.8 | ||||||||
| CAS number | 37318-57-3 | ||||||||
| 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 / EGO | ||||||||
| |||||||||
In enzymology, an oxalate-CoA ligase (EC 6.2.1.8) is an enzyme that catalyzes the chemical reaction
- ATP + oxalate + CoA AMP + diphosphate + oxalyl-CoA
The 3 substrates of this enzyme are ATP, oxalate, and coenzyme A (CoA), whereas its 3 products are AMP, diphosphate, and oxalyl-CoA.
This enzyme belongs to the family of ligases, specifically those forming carbon-sulfur bonds as acid-thiol ligases. The systematic name of this enzyme class is oxalate:CoA ligase (AMP-forming). Other names in common use include oxalyl-CoA synthetase, and oxalyl coenzyme A synthetase. This enzyme participates in glyoxylate and dicarboxylate metabolism.
Organisms with Oxalate-CoA Ligases include:
Arabidopsis thaliana[1]
Saccharomyces cerevisiae [2]
References
- ↑ http://www.plantcell.org/content/24/3/1217.full
- ↑ Foster J, Nakata PA (2014). "An oxalyl-CoA synthetase is important for oxalate metabolism in Saccharomyces cerevisiae". FEBS Lett. 588: 160–6. doi:10.1016/j.febslet.2013.11.026. PMID 24291261.
- Giovanelli J (1966). "Oxalyl-coenzyme A synthetase from pea seeds". Biochim. Biophys. Acta. 118 (1): 124–43. doi:10.1016/s0926-6593(66)80151-0. PMID 4288975.
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