| Oxalate oxidoreductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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.[ further explanation needed]
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 CO2. [3]
References
- ^ Daniel SL, Pilsl C, Drake HL (February 2004). "Oxalate metabolism by the acetogenic bacterium Moorella thermoacetica". FEMS Microbiology Letters. 231 (1): 39–43. doi: 10.1016/S0378-1097(03)00924-8. PMID 14769464.
- ^ Pierce E, Becker DF, Ragsdale SW (December 2010). "Identification and characterization of oxalate oxidoreductase, a novel thiamine pyrophosphate-dependent 2-oxoacid oxidoreductase that enables anaerobic growth on oxalate". The Journal of Biological Chemistry. 285 (52): 40515–24. doi: 10.1074/jbc.M110.155739. PMC 3003350. PMID 20956531.
- ^ Gibson MI, Chen PY, Johnson AC, Pierce E, Can M, Ragsdale SW, Drennan CL (January 2016). "One-carbon chemistry of oxalate oxidoreductase captured by X-ray crystallography". Proceedings of the National Academy of Sciences of the United States of America. 113 (2): 320–5. Bibcode: 2016PNAS..113..320G. doi: 10.1073/pnas.1518537113. PMC 4720323. PMID 26712008.
External links
- Oxalate+oxidoreductase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
 | This enzyme-related article is a stub. You can help Wikipedia by expanding it. |
| Oxalate oxidoreductase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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.[ further explanation needed]
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 CO2. [3]
References
- ^ Daniel SL, Pilsl C, Drake HL (February 2004). "Oxalate metabolism by the acetogenic bacterium Moorella thermoacetica". FEMS Microbiology Letters. 231 (1): 39–43. doi: 10.1016/S0378-1097(03)00924-8. PMID 14769464.
- ^ Pierce E, Becker DF, Ragsdale SW (December 2010). "Identification and characterization of oxalate oxidoreductase, a novel thiamine pyrophosphate-dependent 2-oxoacid oxidoreductase that enables anaerobic growth on oxalate". The Journal of Biological Chemistry. 285 (52): 40515–24. doi: 10.1074/jbc.M110.155739. PMC 3003350. PMID 20956531.
- ^ Gibson MI, Chen PY, Johnson AC, Pierce E, Can M, Ragsdale SW, Drennan CL (January 2016). "One-carbon chemistry of oxalate oxidoreductase captured by X-ray crystallography". Proceedings of the National Academy of Sciences of the United States of America. 113 (2): 320–5. Bibcode: 2016PNAS..113..320G. doi: 10.1073/pnas.1518537113. PMC 4720323. PMID 26712008.
External links
- Oxalate+oxidoreductase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
|
| This enzyme-related article is a stub. You can help Wikipedia by expanding it. |