Oxalate oxidoreductase

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 oxidoreductase
Identifiers
EC no.1.2.7.10
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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NCBIproteins
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

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  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.
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