| 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 heme-binding domain called cytochrome b2 and which catalyzes the conversion of lactate into pyruvate. Glycolate oxidase ( ) ((S)-2-hydroxy-acid oxidase), a peroxisomal enzyme that catalyzes 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 catalyzes the conversion of lactate and oxygen to acetate, carbon dioxide and water. (S)-mandelate dehydrogenase from Pseudomonas putida (gene mdlB), which catalyzes 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. Three-dimensional structures of FMN-dependent alpha-hydroxy acid dehydrogenases show a common fold with a TIM barrel structure.This entry represents the FMN hydroxy acid dehydrogenase domain. | Name | FMN hydroxy acid dehydrogenase domain |
| Short Name | FMN_HAD | Type | Domain |
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