Literature summary extracted from

Scarpellini, M.; Gaetjens, J.; Martin, O.J.; Kampf, J.W.; Sherman, S.E.; Pecoraro, V.L.
Modeling the resting state of oxalate oxidase and oxalate decarboxylase enzymes (2008), Inorg. Chem., 47, 3584-3593.

Crystallization (Commentary)

EC Number	Crystallization (Comment)	Organism
1.2.3.4	in complex with Mn2+ and N3O-donor aminocarboxylate ligands	Hordeum vulgare

Metals/Ions

EC Number	Metals/Ions	Comment	Organism	Structure
1.2.3.4	Mn2+	-	Hordeum vulgare
4.1.1.2	Mn2+	dependent on	Bacillus subtilis
4.1.1.2	Mn2+	dependent on	Thermotoga maritima

Organism

EC Number	Organism	UniProt	Comment	Textmining
1.2.3.4	Hordeum vulgare	-	-	-
4.1.1.2	Bacillus subtilis	-	-	-
4.1.1.2	Thermotoga maritima	-	-	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
1.2.3.4	oxalic acid + O2 + 2 H+	-	Hordeum vulgare	2 CO2 + H2O2	-	?
4.1.1.2	oxalate + H+	-	Bacillus subtilis	formate + CO2	-	?
4.1.1.2	oxalate + H+	-	Thermotoga maritima	formate + CO2	-	?

Synonyms

EC Number	Synonyms	Comment	Organism
1.2.3.4	OxOx	-	Hordeum vulgare
4.1.1.2	OXDC	-	Bacillus subtilis
4.1.1.2	OXDC	-	Thermotoga maritima

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Release 2023.1 (January 2023)