| Description | This group represents alpha-hydroxy acid FMN-dependent dehydrogenases, including human glycolate oxidase (GO), L-lactate oxidase (LOX) [ ] and bacterial L-lactate dehydrogenase. GO catalyses the FMN-dependent oxidation of glycolate to glyoxylate and glyoxylate to oxalate. The latter is a key metabolite in kidney stone formation. 4-carboxy-5-dodecylsulphanyl-1,2,3-triazole (CDST) is an inhibitor of this enzyme. In contrast to most alpha-hydroxy acid oxidases, including spinach glycolate oxidase, a loop region, known as loop 4, is completely visible when the GO active site contains a small ligand. Since this is an unique structural feature, it has the potential to be a target for drugs to decrease glycolate and glyoxylate levels in primary hyperoxaluria type 1 patients who have the inability to convert peroxisomal glyoxylate to glycine [].This entry also includes the fungal protein FUB9 by virtue of sequence similarity to the FMN-dependent alpha-hydroxy acid dehydrogenase family. FUB9 is an oxidase that is part of the gene cluster that mediates the biosynthesis of fusaric acid [ ]. | Name | Alpha-hydroxy acid dehydrogenase, FMN-dependent |
| Short Name | Alpha-hydoxy_acid_DH_FMN | Type | Family |
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