Summary: Copper amine oxidase, N3 domain
This is the Wikipedia entry entitled "Amine oxidase (copper-containing)". More...
The Wikipedia text that you see displayed here is a download from Wikipedia. This means that the information we display is a copy of the information from the Wikipedia database. The button next to the article title ("Edit Wikipedia article") takes you to the edit page for the article directly within Wikipedia. You should be aware you are not editing our local copy of this information. Any changes that you make to the Wikipedia article will not be displayed here until we next download the article from Wikipedia. We currently download new content on a nightly basis.
Does Pfam agree with the content of the Wikipedia entry ?
Pfam has chosen to link families to Wikipedia articles. In some case we have created or edited these articles but in many other cases we have not made any direct contribution to the content of the article. The Wikipedia community does monitor edits to try to ensure that (a) the quality of article annotation increases, and (b) vandalism is very quickly dealt with. However, we would like to emphasise that Pfam does not curate the Wikipedia entries and we cannot guarantee the accuracy of the information on the Wikipedia page.
Editing Wikipedia articles
Before you edit for the first time
Wikipedia is a free, online encyclopedia. Although anyone can edit or contribute to an article, Wikipedia has some strong editing guidelines and policies, which promote the Wikipedia standard of style and etiquette. Your edits and contributions are more likely to be accepted (and remain) if they are in accordance with this policy.
You should take a few minutes to view the following pages:
How your contribution will be recorded
Anyone can edit a Wikipedia entry. You can do this either as a new user or you can register with Wikipedia and log on. When you click on the "Edit Wikipedia article" button, your browser will direct you to the edit page for this entry in Wikipedia. If you are a registered user and currently logged in, your changes will be recorded under your Wikipedia user name. However, if you are not a registered user or are not logged on, your changes will be logged under your computer's IP address. This has two main implications. Firstly, as a registered Wikipedia user your edits are more likely seen as valuable contribution (although all edits are open to community scrutiny regardless). Secondly, if you edit under an IP address you may be sharing this IP address with other users. If your IP address has previously been blocked (due to being flagged as a source of 'vandalism') your edits will also be blocked. You can find more information on this and creating a user account at Wikipedia.
If you have problems editing a particular page, contact us at email@example.com and we will try to help.
The community annotation is a new facility of the Pfam web site. If you have problems editing or experience problems with these pages please contact us.
Amine oxidase (copper-containing) Edit Wikipedia article
|PDB structures||RCSB PDB PDBe PDBsum|
|Gene Ontology||AmiGO / EGO|
|Copper amine oxidase, enzyme domain|
|Copper amine oxidase N-terminal domain|
crystal structure of e. coli amine oxidase anaerobically reduced with beta-phenylethylamine
|Copper amine oxidase, N2 domain|
crystal structure of a eukaryotic (pea seedling) copper-containing amine oxidase at 2.2a resolution
|Copper amine oxidase, N3 domain|
crystal structure of hansenula polymorpha amine oxidase in complex with xe to 1.6 angstroms
Amine oxidases (AO) 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 18.104.22.168) and copper-containing (EC 22.214.171.124). Copper-containing AO act as a disulphide-linked homodimer. They catalyse the oxidation of primary amines to aldehydes, with the subsequent release of ammonia and hydrogen peroxide, which requires one copper ion per subunit and topaquinone as cofactor:
- RCH2NH2 + H2O + O2 RCHO + NH3 + H2O2
This enzyme belongs to oxidoreductases, specifically those acting on the CH-NH2 group of donors with oxygen as acceptor. The systematic name of this enzyme class is amine:oxygen oxidoreductase (deaminating) (copper-containing). This enzyme participates in 8 metabolic pathways: urea cycle and metabolism of amino groups, glycine, serine and threonine metabolism, histidine metabolism, tyrosine metabolism, phenylalanine metabolism, tryptophan metabolism, beta-alanine metabolism, and alkaloid biosynthesis ii. It has 2 cofactors: copper, and PQQ.
The copper amine oxidase 3-dimensional structure was determined through X-ray crystallography. The copper amine oxidases occur as mushroom-shaped homodimers of 70-95 kDa, each monomer containing a copper ion and a covalently bound redox cofactor, topaquinone (TPQ). TPQ is formed by post-translational modification of a conserved tyrosine residue. The copper ion is coordinated with three histidine residues and two water molecules in a distorted square pyramidal geometry, and has a dual function in catalysis and TPQ biogenesis. The catalytic domain is the largest of the 3-4 domains found in copper amine oxidases, and consists of a beta sandwich of 18 strands in two sheets. The active site is buried and requires a conformational change to allow the substrate access.
The N2 and N3 N-terminal domains share a common structural fold, its core consisting of alpha-beta(4), where the helix is packed against the coiled anti-parallel beta-sheets. An additional domain is found at the N-terminal of some copper amine oxidases, as well as in related proteins such as cell wall hydrolase and N-acetylmuramoyl-L-alanine amidase. This domain consists of a five-stranded antiparallel beta-sheet twisted around an alpha helix.
In eukaryotes they have a broader range of functions, including cell differentiation and growth, wound healing, detoxification and cell signalling as well as functioning as a vascular adhesion protein (VAP-1) in some mammalian tissues.
Human proteins containing this domain
- PDB 3LOY; Chang CM, Klema VJ, Johnson BJ, Mure M, Klinman JP, Wilmot CM (March 2010). "Kinetic and structural analysis of substrate specificity in two copper amine oxidases from Hansenula polymorpha". Biochemistry 49 (11): 2540–50. doi:10.1021/bi901933d. PMC 2851405. PMID 20155950.
- Convery MA, Phillips SE, McPherson MJ, Yadav KD, Knowles PF, Parsons MR, Wilmot CM, Blakeley V, Corner AS (1995). "Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution". Structure 3 (11): 1171–1184. doi:10.1016/s0969-2126(01)00253-2. PMID 8591028.
- Murray JM, Convery MA, Phillips SE, McPherson MJ, Knowles PF, Parsons MR, Wilmot CM, Blakeley V, Corner AS, Alton G, Palcic MM (1997). "Catalytic mechanism of the quinoenzyme amine oxidase from Escherichia coli: exploring the reductive half-reaction". Biochemistry 36 (7): 1608–1620. doi:10.1021/bi962205j. PMID 9048544.
- Tanizawa K, Guss JM, Freeman HC, Yamaguchi H, Wilce MC, Dooley DM, Matsunami H, Mcintire WS, Ruggiero CE (1997). "Crystal structures of the copper-containing amine oxidase from Arthrobacter globiformis in the holo and apo forms: implications for the biogenesis of topaquinone". Biochemistry 36 (51): 16116–16133. doi:10.1021/bi971797i. PMID 9405045.
- Parsons MR, Convery MA, Wilmot CM, Yadav KD, Blakeley V, Corner AS, Phillips SE, McPherson MJ, Knowles PF (November 1995). "Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution". Structure 3 (11): 1171–84. doi:10.1016/s0969-2126(01)00253-2. PMID 8591028.
- Wilmot CM, Hajdu J, McPherson MJ, Knowles PF, Phillips SE (November 1999). "Visualization of dioxygen bound to copper during enzyme catalysis". Science 286 (5445): 1724–8. doi:10.1126/science.286.5445.1724. PMID 10576737.
- Guss JM, Freeman HC, Kumar V, Wilce MC, Dooley DM, Harvey I, Mcguirl MA, Zubak VM (1996). "Crystal structure of a eukaryotic (pea seedling) copper-containing amine oxidase at 2.2 A resolution". Structure 4 (8): 943–955. doi:10.1016/s0969-2126(96)00101-3. PMID 8805580.
- Ameyama M, Hayashi M, Matsushita K, Shinagawa E, Adachi O (1984). "Microbial-production of pyrroloquinoline quinone". Agric. Biol. Chem. 48: 561–565. doi:10.1271/bbb1961.48.561.
- Augustinsson KB, Olsson B (1959). "Esterases in the milk and blood plasma of swine. I. Substrate specificity and electrophoresis studies". Biochem. J. 71 (3): 477–84. PMC 1196820. PMID 13638253.
- Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 8, Academic Press, New York, 1963, p. 337-351.
- Buffoni F, Blaschko H (1964). "Benzylamine oxidase and histaminase: purification and crystallization of an enzyme from pig plasma". Proceedings of the Royal Society B 161: 153–67. doi:10.1098/rspb.1964.0086. PMID 14224405.
- Haywood GW, Large PJ (1981). "Microbial oxidation of amines. Distribution, purification and properties of two primary-amine oxidases from the yeast Candida boidinii grown on amines as sole nitrogen source". Biochem. J. 199 (1): 187–201. PMC 1163349. PMID 7337701.
- McEwen CM Jr (1965). "Human plasma monoamine oxidase. 1. Purification and identification". J. Biol. Chem. 240 (5): 2003–10. PMID 5888801.
- Mondovi B, Costa MT, Agro AF, Rotilio G (1967). "Pyridoxal phosphate as a prosthetic group of pig kidney diamine oxidase". Arch. Biochem. Biophys. 119 (1): 373–81. doi:10.1016/0003-9861(67)90468-7. PMID 4964016.
- Yamada H, Adachi O and Ogata K (1965). "Amine oxidases of microorganisms. Part II. Purification and crystallisation of amine oxidase of Aspergillus niger". Agric. Biol. Chem. 29: 649–654.
- Yamada H, Adachi O and Ogata K (1965). "Amine oxidases of microorganisms. Part III. Properties of amine oxidase of Aspergillus niger". Agric. Biol. Chem. 29: 864–869.
- Yamada H, Adachi O and Ogata K (1965). "Amine oxidases of microorganisms. Part IV. Further properties of amine oxidase of Aspergillus niger". Agric. Biol. Chem. 29: 912–917.
- Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 8, Academic Press, New York, 1963, p. 313-335.
Copper amine oxidase, N3 domain Provide feedback
This domain is the second or third structural domain in copper amine oxidases, it is known as the N3 domain. Its function is uncertain. The catalytic domain can be found in PF01179. Copper amine oxidases are a ubiquitous and novel group of quinoenzymes that catalyse the oxidative deamination of primary amines to the corresponding aldehydes, with concomitant reduction of molecular oxygen to hydrogen peroxide. The enzymes are dimers of identical 70-90 kDa subunits, each of which contains a single copper ion and a covalently bound cofactor formed by the post-translational modification of a tyrosine side chain to 2,4,5-trihydroxyphenylalanine quinone (TPQ).
Parsons MR, Convery MA, Wilmot CM, Yadav KD, Blakeley V, Corner AS, Phillips SE, McPherson MJ, Knowles PF; , Structure 1995;3:1171-1184.: Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution. PUBMED:8591028 EPMC:8591028
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR015802
Amine oxidases (AO) are enzymes that catalyse 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) and copper-containing (EC). Copper-containing AO act as a disulphide-linked homodimer. They catalyse the oxidation of primary amines to aldehydes, with the subsequent release of ammonia and hydrogen peroxide, which requires one copper ion per subunit and topaquinone as cofactor [PUBMED:8591028]:
Copper-containing amine oxidases are found in bacteria, fungi, plants and animals. In prokaryotes, the enzyme enables various amine substrates to be used as sources of carbon and nitrogen [PUBMED:9048544, PUBMED:9405045]. In eukaryotes they have a broader range of functions, including cell differentiation and growth, wound healing, detoxification and cell signalling [PUBMED:8805580].
The copper amine oxidases occur as mushroom-shaped homodimers of 70-95 kDa, each monomer containing a copper ion and a covalently bound redox cofactor, topaquinone (TPQ). TPQ is formed by post-translational modification of a conserved tyrosine residue. The copper ion is coordinated with three histidine residues and two water molecules in a distorted square pyramidal geometry, and has a dual function in catalysis and TPQ biogenesis. The catalytic domain is the largest of the 3-4 domains found in copper amine oxidases, and consists of a beta sandwich of 18 strands in two sheets. The active site is buried and requires a conformational change to allow the substrate access. The two N-terminal domains share a common structural fold, its core consisting of a five-stranded antiparallel beta sheet twisted around an alpha helix. The D1 domains from the two subunits comprise the stalk, of the mushroom-shaped dimer, and interact with each other but do not pack tightly against each other [PUBMED:8591028, PUBMED:10576737].
This entry represents one (N3) of the two N-terminal domains (N2/N3) that share a similar structure.
|Molecular function||primary amine oxidase activity (GO:0008131)|
|copper ion binding (GO:0005507)|
|quinone binding (GO:0048038)|
|Biological process||oxidation-reduction process (GO:0055114)|
|amine metabolic process (GO:0009308)|
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
- the number of residues in the sequence
- the Pfam graphic itself.
Loading domain graphics...
Copper amine oxidase (CuAO) are comprised of three of four domains. In the case of the four domain CuAO, the N-terminal domain (termed N1, and is not present in the three domain CuAO) and the C-terminal catalytic domain sandwich two repeated domains (termed N2 and N3). The function of these two homologous domains is uncertain. N2 and N3 both have a cystatin-like fold .
The clan contains the following 2 members:Cu_amine_oxidN2 Cu_amine_oxidN3
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the NCBI sequence database using the family HMM
- alignment generated by searching the metagenomics sequence database using the family HMM
You can see the alignments as HTML or in three different sequence viewers:
- Pfam viewer
- an HTML-based viewer that uses DAS to retrieve alignment fragments on request
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
Format an alignment
If you find these logos useful in your own work, please consider citing the following article:
Note: You can also download the data file for the tree.
Curation and family details
|Author:||Bateman A, Finn RD|
|Number in seed:||17|
|Number in full:||943|
|Average length of the domain:||100.70 aa|
|Average identity of full alignment:||23 %|
|Average coverage of the sequence by the domain:||14.32 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||11|
|Download:||download the raw HMM for this family|
Weight segments by...
Change the size of the sunburst
selected sequences to HMM
a FASTA-format file
- 0 sequences
- 0 species
How the sunburst is generated
Colouring and labels
Anomalies in the taxonomy tree
Missing taxonomic levels
Unmapped species names
Too many species/sequences
The tree shows the occurrence of this domain across different species. More...
You can use the tree controls to manipulate how the interactive tree is displayed:
- show/hide the summary boxes
- highlight species that are represented in the seed alignment
- expand/collapse the tree or expand it to a given depth
- select a sub-tree or a set of species within the tree and view them graphically or as an alignment
- save a plain text representation of the tree
There are 3 interactions for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Cu_amine_oxidN3 domain has been found. There are 180 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
Loading structure mapping...