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NAD(P)-binding protein
FAD-dependent oxidoreductase
This family consists of various amine oxidases, including maze polyamine oxidase (PAO) [1] and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. The family also contains phytoene dehydrogenases and related enzymes. In vertebrates MAO plays an important role regulating the intracellular levels of amines via there oxidation; these include various neurotransmitters, neurotoxins and trace amines [2]. In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium [3]. PAOs in plants, bacteria and protozoa oxidase spermidine and spermine to an aminobutyral, diaminopropane and hydrogen peroxide and are involved in the catabolism of polyamines [1]. Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid binding proteins and antibacterial glycoproteins. [1]. 9598979. Maize polyamine oxidase: primary structure from protein and cDNA. sequencing.. Tavladoraki P, Schinina ME, Cecconi F, Agostino SD, Manera F,. Rea G, Mariottini P, Federico R, Angelini R;. FEBS Lett 1998;426:62-66.. [2]. 9162023. A key amino acid responsible for substrate selectivity of. monoamine oxidase A and B.. Tsugeno Y, Ito A;. J Biol Chem 1997;272:14033-14036.. [3]. 7770050. Cloning, sequencing and heterologous expression of the monoamine. oxidase gene from Aspergillus niger.. Schilling B, Lerch K;. Mol Gen Genet 1995;247:430-438. (from Pfam)
NAD(P)/FAD-dependent oxidoreductase
NAD(P)/FAD-dependent oxidoreductase catalyzes the transfer of electrons from one molecule, the electron donor or reductant, to another molecule, the electron acceptor or oxidant; similar to flavin-containing L-amino-acid oxidase that catalyzes the oxidative deamination of predominantly hydrophobic and aromatic L-amino acids
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