Member database | Pfam |
Pfam type | domain |
Short name | FAD_binding_4 |
Clan | FAD_PCMH |
Author | Bashton M;0000-0002-6847-1525 Bateman A;0000-0002-6982-4660 |
Sequence Ontology | 0000417 |
Description
This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) 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 form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyses the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidises the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan
[2].
References
1.Crystal structures and inhibitor binding in the octameric flavoenzyme vanillyl-alcohol oxidase: the shape of the active-site cavity controls substrate specificity. Mattevi A, Fraaije MW, Mozzarelli A, Olivi L, Coda A, van Berkel WJ. Structure 5, 907-20, (1997). View articlePMID: 9261083
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