{PDOC00895}
{PS01164; COPPER_AMINE_OXID_1}
{PS01165; COPPER_AMINE_OXID_2}
{BEGIN}
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* Copper amine oxidase signatures *
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Amine oxidases  (AO)  [1]  are  enzymes  that catalyze the oxidation of a wide
range of  biogenic  amines  including  many  neurotransmitters,  histamine and
xenobiotic amines.  There are two classes of amine oxidases: flavin-containing
(EC 1.4.3.4) and copper-containing (EC 1.4.3.6).

Copper-containing AO is found in bacteria, fungi, plants and animals, it is an
homodimeric enzyme  that  binds one copper ion per subunit as well as a 2,4,5-
trihydroxyphenylalanine quinone (or topaquinone) (TPQ) cofactor. This cofactor
is derived from a tyrosine residue.

We have  derived  two signature patterns for copper AO, the first one contains
the tyrosine  which  give  rises  to  the  TPQ  cofactor  while the second one
contains one of the three histidines that bind the copper atom [2].

-Consensus pattern: [LIVM]-[LIVMA]-[LIVMF]-x(4)-[ST]-x(2)-N-Y-[DE]-[YN]
                    [The first Y gives rises to TPQ]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: 1.

-Consensus pattern: T-x-[GS]-x(2)-H-[LIVMF]-x(3)-E-[DE]-x-P
                    [H is a copper ligand]
-Sequences known to belong to this class detected by the pattern: ALL,  except
 for lentil AO.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Last update: July 1999 / Patterns and text revised.

[ 1] Knowles P.F., Dooley D.M.
     (In) Metal ions in biological systems; Sigel H., Sigel A., Eds., 30:361-
     403, Marcel Dekker, New-York, (1993).
[ 2] Parsons M.R., Convery M.A., Wilmot C.M., Yadav K.D.S., Blakeley V.,
     Corner A.S., Phillips S.E.V., McPherson M.J., Knowles P.F.
     "Crystal structure of a quinoenzyme: copper amine oxidase of
     Escherichia coli at 2 A resolution."
     Structure 3:1171-1184(1995).
     PubMed=8591028;

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