Alpha-hydroxy acid dehydrogenase, FMN-dependent (IPR012133)

Short name: Alpha-hydoxy_acid_DH_FMN

Overlapping homologous superfamilies

Family relationships


This group represents an alpha-hydroxy acid dehydrogenase, which is FMN-dependent. Human glycolate oxidase (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 inhibiter 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 [PMID: 18215067]. In addition, L-Lactate oxidase (LOX) belongs to a family of flavin mononucleotide (FMN)-dependent alpha-hydroxy acid-oxidizing enzymes [PMID: 18367206]. 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 [PMID: 25372119].

GO terms

Biological Process

GO:0055114 oxidation-reduction process

Molecular Function

GO:0010181 FMN binding
GO:0016491 oxidoreductase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
  • cd02809 (alpha_hydroxyacid_oxid_FMN)