FAD-oxidase

{{Infobox protein family

| Symbol = FAD-oxidase_C

| Name = FAD linked oxidases, C-terminal domain

| image = PDB 1wve EBI.jpg

| width =

| caption = p-cresol methylhydroxylase: alteration of the structure of the flavoprotein subunit upon its binding to the cytochrome subunit

| Pfam = PF02913

| Pfam_clan = CL0277

| InterPro = IPR004113

| SMART =

| PROSITE =

| MEROPS =

| SCOP = 1ahu

| TCDB =

| OPM family =

| OPM protein =

| CAZy =

| CDD =

}}

In molecular biology FAD-oxidases are a family of FAD-dependent oxidoreductases. They are flavoproteins that contain a covalently bound FAD group which is attached to a histidine via an 8-alpha-(N3-histidyl)-riboflavin linkage. The region around the histidine that binds the FAD group is conserved in these enzymes.{{cite journal | vauthors = Mattevi A, Fraaije MW, Coda A, van Berkel WJ | title = Crystallization and preliminary X-ray analysis of the flavoenzyme vanillyl-alcohol oxidase from Penicillium simplicissimum | journal = Proteins | volume = 27 | issue = 4 | pages = 601–3 | date = April 1997 | pmid = 9141139 | doi = 10.1002/(SICI)1097-0134(199704)27:4<601::AID-PROT12>3.0.CO;2-O | url = https://pure.rug.nl/ws/files/3211668/1997ProteinsMattevi.pdf }}