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
SymbolFAD-oxidase_C
PfamPF02913
Pfam clanCL0277
InterProIPR004113
SCOP21ahu / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

References

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  1. ^ 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.
This article incorporates text from the public domain Pfam and InterPro: IPR004113