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FAD-oxidase
| Field | Value |
|---|---|
| Symbol | FAD-oxidase_C |
| Name | FAD linked oxidases, C-terminal domain |
| image | PDB 1wve EBI.jpg |
| 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 |
| SCOP | 1ahu |
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.
References
References
- (April 1997). "Crystallization and preliminary X-ray analysis of the flavoenzyme vanillyl-alcohol oxidase from Penicillium simplicissimum". Proteins.
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