D
IPR006094

FAD linked oxidase, N-terminal

InterPro entry
Short nameOxid_FAD_bind_N
Overlapping
homologous
superfamilies
 
domain relationships

Description

Various enzymes use FAD as a co-factor, most of these enzymes are oxygen-dependent oxidoreductases, containing a covalently bound FAD group which is attached to a histidine via an 8-alpha-(N3-histidyl)-riboflavin linkage. One of the enzymes Vanillyl-alcohol oxidase (VAO,
1.1.3.38
) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110
[1]
. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyses the oxidation of a wide variety of substrates, ranging from aromatic amines to 4-alkylphenols. Other enzymes included in this family are MurB family members UDP-N-acetylenolpyruvoylglucosamine reductases involved in the biosynthesis of peptidoglycan
[2]
, D-lactate dehydrogenases among many others oxidoreductases.

References

1.Structural analysis of flavinylation in vanillyl-alcohol oxidase. Fraaije MW, van Den Heuvel RH, van Berkel WJ, Mattevi A. J. Biol. Chem. 275, 38654-8, (2000). View articlePMID: 10984479

2.The structure of the substrate-free form of MurB, an essential enzyme for the synthesis of bacterial cell walls. Benson TE, Walsh CT, Hogle JM. Structure 4, 47-54, (1996). View articlePMID: 8805513

GO terms

biological process

  • None

cellular component

  • None

Cross References

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