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PROSITE documentation PDOC00895

Copper amine oxidase signatures

Description:

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].

Last update:

July 1999 / Patterns and text revised.

Technical section:

PROSITE methods (with tools and information) covered by this documentation:

COPPER_AMINE_OXID_1, PS01164; Copper amine oxidase topaquinone signature  (PATTERN)
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.
• Retrieve an alignment of Swiss-Prot true positive hits:
  Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS01164
• Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS01164
• Scan Swiss-Prot/TrEMBL entries against PS01164
• view ligand binding statistics
Matching PDB structures: 1A2V 1AV4 1AVK 1AVL ... [ALL]
COPPER_AMINE_OXID_2, PS01165; Copper amine oxidase copper-binding site signature  (PATTERN)
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.
• Retrieve an alignment of Swiss-Prot true positive hits:
  Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format
• Retrieve the sequence logo from the alignment
• Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS01165
• Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS01165
• Scan Swiss-Prot/TrEMBL entries against PS01165
• view ligand binding statistics
Matching PDB structures: 1A2V 1AV4 1AVK 1AVL ... [ALL]

References:

1 AuthorsKnowles P.F., Dooley D.M.
Source(In) Metal ions in biological systems; Sigel H., Sigel A., Eds., 30:361- 403, Marcel Dekker, New-York, (1993).
2 AuthorsParsons 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.
TitleCrystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution.
SourceStructure 3:1171-1184(1995).
PubMed ID8591028

Copyright:

This PROSITE entry is copyright by the Swiss Institute of Bioinformatics (SIB). There are no restrictions on its use by non-profit institutions as long as its content is in no way modified and this statement is not removed. Usage by and for commercial entities requires a license agreement (See http://www.isb-sib.ch/announce/or email to license@isb-sib.ch).

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