Oxalate oxidoreductase
| Oxalate oxidoreductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC number | 1.2.7.10 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
Oxalate oxidoreductases (EC 1.2.7.10) (OOR) are a relatively recently discovered group of enzymes that break down oxalate, a problematic molecule nutritionally. The first one to have been characterized has the systematic name oxalate:ferredoxin oxidoreductase.[1][2] This enzyme catalyses the following chemical reaction:
- oxalate + oxidized ferredoxin 2 CO2 + reduced ferredoxin
This enzyme contains thiamine diphosphate and [4Fe-4S] clusters.
Another OOR from acetogenic bacteria, a thiamine pyrophosphate(TPP)-dependent OOR, had its mechanism of action decoded step by step under X-ray crystallography to rather simplistically (one-carbon) split oxalate, producing low-potential electrons and C02.[3]
References
- ↑ Daniel, S.L.; Pilsl, C.; Drake, H.L. (2004). "Oxalate metabolism by the acetogenic bacterium Moorella thermoacetica". FEMS Microbiol. Lett. 231 (1): 39–43. doi:10.1016/S0378-1097(03)00924-8. PMID 14769464.
- ↑ Pierce, E.; Becker, D.F.; Ragsdale, S.W. (2010). "Identification and characterization of oxalate oxidoreductase, a novel thiamine pyrophosphate-dependent 2-oxoacid oxidoreductase that enables anaerobic growth on oxalate". J. Biol. Chem. 285 (52): 40515–40524. doi:10.1074/jbc.M110.155739. PMC 3003350
. PMID 20956531. - ↑ http://www.pnas.org/content/early/2015/12/23/1518537113.full.pdf
External links
- Oxalate oxidoreductase at the US National Library of Medicine Medical Subject Headings (MeSH)
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