| Description | A number of oxidoreductases that act on alpha-hydroxy acids and which are FMN-containing flavoproteins have been shown [ , , ] to be structurally related. These enzymes are:Lactate dehydrogenase ( ), 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 ( ) ((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 ( ), a peroxisomal enzyme. Lactate 2-monooxygenase ( ) (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.The first step in the reaction mechanism of these enzymes is the abstraction of the proton from the α-carbon of the substrate producing a carbanion which can subsequently attach to the N5 atom of FMN. A conserved histidine has been shown [ ] to be involved in the removal of the proton. The region around this active site residue is highly conserved and contains an arginine residue which is involved in substrate binding. | Name | FMN-dependent dehydrogenase |
| Short Name | FMN-dep_DH | Type | Domain |
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