1 Contains
| DB identifier | Type | Name |
|---|---|---|
| IPR008259 | Active_site | FMN-dependent alpha-hydroxy acid dehydrogenase, active site |
| Type: | Domain | Name: | FMN-dependent dehydrogenase |
| 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 alpha-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. | Short Name: | FMN-dep_DH |
| DB identifier | Type | Name |
|---|---|---|
| IPR008259 | Active_site | FMN-dependent alpha-hydroxy acid dehydrogenase, active site |
