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

  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. doi:10.1073/pnas.1518537113. PMC 4720323. PMID 26712008.
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