Oxalate oxidoreductase
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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
Quick Facts Identifiers, EC no. ...
Oxalate oxidoreductase | |||||||||
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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 | ||||||||
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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]