FAD-oxidase
| FAD linked oxidases, C-terminal domain | |||||||
|---|---|---|---|---|---|---|---|
p-cresol methylhydroxylase: alteration of the structure of the flavoprotein subunit upon its binding to the cytochrome subunit | |||||||
| Identifiers | |||||||
| Symbol | FAD-oxidase_C | ||||||
| Pfam | PF02913 | ||||||
| Pfam clan | CL0277 | ||||||
| InterPro | IPR004113 | ||||||
| SCOP2 | 1ahu / SCOPe / SUPFAM | ||||||
| |||||||
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.