Literature summary for 1.2.7.10 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 .

Search for more literature for 1.2.7.10

Organism

Organism	UniProt	Comment	Textmining
Moorella thermoacetica	Q2RI41 and Q2RI42 and Q2RI40	Q2RI41 i.e. subunit alpha, Q2RI42 i.e. subunit beta, Q2RI40 i.e. subunit delta	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
oxalate + methyl viologen	-	Moorella thermoacetica	2 CO2 + reduced methyl viologen	-	?

Synonyms

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

General Information

General Information	Comment	Organism
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

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Release 2023.1 (January 2023)