Misplaced Pages

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. This enzyme catalyses the following chemical reaction:

oxalate + oxidized ferredoxin ${\displaystyle \rightleftharpoons }$ 2 CO₂ + reduced ferredoxin

This enzyme contains thiamine diphosphate and 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 CO₂.

References

1. 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.
2. 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.
3. 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)

• Biology

This enzyme-related article is a stub. You can help Misplaced Pages by expanding it.

• v
• t
• e

• EC 1.2.7
• Enzyme stubs