FAD-oxidase
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.[1]
| 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 | ||||||||
| SCOPe | 1ahu / SUPFAM | ||||||||
| |||||||||
References
- Mattevi A, Fraaije MW, Coda A, van Berkel WJ (April 1997). "Crystallization and preliminary X-ray analysis of the flavoenzyme vanillyl-alcohol oxidase from Penicillium simplicissimum" (PDF). Proteins. 27 (4): 601–3. doi:10.1002/(SICI)1097-0134(199704)27:4<601::AID-PROT12>3.0.CO;2-O. PMID 9141139.
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