Glycolate Oxidases family (GOX)
Glycolate oxidase belongs to a large group of oxidoreductases that act on alpha-hydroxy acids and which are FMN-containing flavoproteins [PUBMED:2324094, PUBMED:2271624, PUBMED:1939137].
Proteins belonging to this superfamily are structurally related and are the following: Lactate dehydrogenase (EC), which consists of a dehydrogenase domain and a haem-binding domain called cytochrome b2 and which catalyses the conversion of lactate into pyruvate. Glycolate oxidase (EC) ((S)-2-hydroxy-acid oxidase), a peroxisomal enzyme that catalyses the conversion of glycolate and oxygen to glyoxylate and hydrogen peroxide. Long chain alpha-hydroxy acid oxidase from rat (EC), a peroxisomal enzyme. Lactate 2-monooxygenase (EC) (lactate oxidase) from Mycobacterium smegmatis, which catalyses the conversion of lactate and oxygen to acetate, carbon dioxide and water. (S)-mandelate dehydrogenase from Pseudomonas putida (gene mdlB), which catalyses the reduction of (S)-mandelate to benzoylformate.
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