Flavin-containing amine oxidoreductase

Flavin-containing amine oxidoreductases are a family of various amine oxidases, including maize polyamine oxidase (PAO),[2] 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.[3] In lower eukaryotes such as aspergillus and in bacteria the main role of amine oxidases is to provide a source of ammonium.[4] 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.[2] Other members of this family include tryptophan 2-monooxygenase, putrescine oxidase, corticosteroid-binding proteins, and antibacterial glycoproteins.

Flavin-containing amine oxidoreductase
Structure of polyamine oxidase.[1]
Identifiers
SymbolAmino_oxidase
PfamPF01593
Pfam clanCL0053
InterProIPR001613
PROSITEPDOC00755
SCOPe1b37 / SUPFAM
OPM superfamily119
OPM protein2z5x
Membranome251

Human proteins containing this domain

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

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gollark: Purposes.
gollark: This will make it periodically look up helloboi.osmarks.net and put in A/AAAA records for it.

References
  1. Binda C, Coda A, Angelini R, Federico R, Ascenzi P, Mattevi A (March 1999). "A 30-angstrom-long U-shaped catalytic tunnel in the crystal structure of polyamine oxidase". Structure. 7 (3): 265–76. doi:10.1016/s0969-2126(99)80037-9. PMID 10368296.
  2. 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.
  3. 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.
  4. 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.
This article incorporates text from the public domain Pfam and InterPro: IPR002937
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