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Literature summary extracted from

  • Pierce, E.; Mansoorabadi, S.O.; Can, M.; Reed, G.H.; Ragsdale, S.W.
    Properties of intermediates in the catalytic cycle of oxalate oxidoreductase and its suicide inactivation by pyruvate (2017), Biochemistry, 56, 2824-2835 .
    View publication on PubMedView publication on EuropePMC

Organism

EC Number Organism UniProt Comment Textmining
1.2.7.10 Moorella thermoacetica Q2RI41 and Q2RI42 and Q2RI40 Q2RI41 i.e. subunit alpha, Q2RI42 i.e. subunit beta, Q2RI40 i.e. subunit delta
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Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.2.7.10 oxalate + methyl viologen
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Moorella thermoacetica 2 CO2 + reduced methyl viologen
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Synonyms

EC Number Synonyms Comment Organism
1.2.7.10 Moth_1591 gene name, subunit beta Moorella thermoacetica
1.2.7.10 Moth_1592 gene name, subunit alpha Moorella thermoacetica
1.2.7.10 Moth_1593 gene name, subunit delta Moorella thermoacetica
1.2.7.10 OOR
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Moorella thermoacetica

General Information

EC Number General Information Comment Organism
1.2.7.10 physiological function CoA has no effect on catalysis by OOR. OOR binds pyruvate and catalyzes decarboxylation to form the same hydroxyethylidine-thiamine diphosphate intermediate and one-electron transfer to generate the hydroxyethylidine-thiamine diphosphate radical as does pyruvate:ferredoxin oxidoreductase, EC 1.2.7.1. In OOR, this intermediate remains stranded at the active site as a covalent inhibitor. OOR generates an oxalate-derived adduct with thiamine diphosphate (oxalyl-TPP) that undergoes decarboxylation and one-electron transfer to form a radical intermediate remaining bound to thiamine diphosphate Moorella thermoacetica