Flavin containing amine oxidoreductase

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Flavin containing amine oxidoreductase
Identifiers
Symbol	Amino_oxidase
Pfam	PF01593
InterPro	IPR002937
PROSITE	PDOC00755
SCOP	1b37
OPM family	128
OPM protein	1sez
Available PDB structures: 1tdoA:61-499 1tdkA:61-499 1tdnA:61-499 1reoA:61-499 1f8sD:61-499 1f8rD:61-499 1sezA:23-490 1z6lA:18-504 1yy5B:18-504 1xpqD:18-504 1rsgB:18-504 1yvvB:12-62 2babA:16-60 2bacA:16-60 2b9xA:16-60 2b9wA:16-60 2b9yA:16-60 2ba9A:16-60 1h86B:42-483 1b5qB:42-483 1h83B:42-483 1h84C:42-483 1b37C:42-483 1h81A:42-483 1h82B:42-483 1o5wC:23-460 1ojdF:14-451 2bk3B:14-451 2c64A:14-451 2bk5A:14-451 2c67B:14-451 1s2yA:14-451 2bybB:14-451 1ojcB:14-451 2bk4B:14-451 2c66A:14-451 1s3bA:14-451 1s2qA:14-451 1ojaA:14-451 1ojbA:14-451 1gosA:14-451 2c65A:14-451 1oj9B:14-451 1h8rA:14-451 1s3eA:14-451 2bxrA:23-460 2bxsB:23-460 1h8qA:23-460

Flavin containing amine oxidoreductases are a family of various amine oxidases, including maize polyamine oxidase (PAO)^[1], L-amino acid oxidases (LAO) and various flavin containing monoamine oxidases (MAO). The aligned region includes the flavin binding site of these enzymes. In vertebrates MAO plays an important role in regulating the intracellular levels of amines via their 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 oxidise 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.

[edit] Human proteins containing this domain

AOF1; AOF2; IL4I1; MAOA; MAOB; PAOX; PPOX; SMOX;

[edit] References

^ ^a ^b Schinina ME, Mariottini P, Tavladoraki P, Cecconi F, Manera F, Rea G, Federico R, Angelini R, Di Agostino S (1998). "Maize polyamine oxidase: primary structure from protein and cDNA sequencing". FEBS Lett. 426 (1): 62–66. doi:10.1016/S0014-5793(98)00311-1. PMID 9598979.
^ Tsugeno Y, Ito A (1997). "A key amino acid responsible for substrate selectivity of monoamine oxidase A and B". J. Biol. Chem. 272 (22): 14033–14036. doi:10.1074/jbc.272.22.14033. PMID 9162023.
^ Lerch K, Schilling B (1995). "Cloning, sequencing and heterologous expression of the monoamine oxidase gene from Aspergillus niger". Mol. Gen. Genet. 247 (4): 430–438. doi:10.1007/BF00293144. PMID 7770050.