Summary: Copper amine oxidase, enzyme domain
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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 oxidase (copper-containing) (AOC) (EC 184.108.40.206 and EC 220.127.116.11; formerly EC 18.104.22.168) is a family of amine oxidase enzymes which includes both primary-amine oxidase and diamine oxidase; these enzymes catalyze the oxidation of a wide range of biogenic amines including many neurotransmitters, histamine and xenobiotic amines. They 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; one AOC enzyme (AOC3) functions as a vascular adhesion protein (VAP-1) in some mammalian tissues.
Human proteins containing this domain
- "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 . PMID 20155950.; Chang CM, Klema VJ, Johnson BJ, Mure M, Klinman JP, Wilmot CM (March 2010).
- 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 . 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. doi:10.1042/bj1990187. PMC . 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 & Ogata K (1965). "Amine oxidases of microorganisms. Part II. Purification and crystallisation of amine oxidase of Aspergillus niger". Agric. Biol. Chem. 29: 649–654. doi:10.1271/bbb1961.29.649.
- Yamada H, Adachi O & Ogata K (1965). "Amine oxidases of microorganisms. Part III. Properties of amine oxidase of Aspergillus niger". Agric. Biol. Chem. 29: 864–869. doi:10.1271/bbb1961.29.864.
- Yamada H, Adachi O & Ogata K (1965). "Amine oxidases of microorganisms. Part IV. Further properties of amine oxidase of Aspergillus niger". Agric. Biol. Chem. 29: 912–917. doi:10.1271/bbb1961.29.912.
- Boyer, P.D., Lardy, H. and Myrback, K. (Eds.), The Enzymes, 2nd ed., vol. 8, Academic Press, New York, 1963, p. 313-335.
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Copper amine oxidase, enzyme domain Provide feedback
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). This family corresponds to the catalytic domain of the enzyme.
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 IPR015798
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 the C-terminal catalytic domain of copper amine oxidases, and has a super-sandwich fold consisting of 18 beta-strands in 2 sheets [PUBMED:8591028]. A domain with a similar structural fold can be found as the third domain in lysyl oxidase PplO [PUBMED:14690425].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|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)|
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
The graphic that is shown by default represents the longest sequence with a given architecture. Each row contains the following information:
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This clan is composed of a beta-sandwich that was first observed in domain 5 of beta-galactosidase, then as the central domain of copper amine oxidase, the C-terminal domain of chondroitinase, the C-terminal domain of hyaluronate lyase, the N-terminal domain of maltose phosphorylase and in Galactose Mutarotase . All these enzymes act on a sugar substrate.
The clan contains the following 31 members:Aldose_epim Bgal_small_N Cu_amine_oxid DUF1926 DUF4432 DUF4450 DUF4968 DUF5054 DUF5107 DUF5127 Gal_mutarotas_2 Gal_mutarotas_3 GH97_N Glucodextran_N Glyco_hyd_65N_2 Glyco_hydr_116N Glyco_hydro_36N Glyco_hydro_38 Glyco_hydro_38C Glyco_hydro_52 Glyco_hydro_65N Glyco_hydro_81 Glyco_hydro_92N Glyco_transf_36 Hepar_II_III Lyase_8 MdoG NtCtMGAM_N Rhamnogal_lyase RhgB_N YidC_periplas
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|Author:||Bateman A , Finn RD|
|Number in seed:||328|
|Number in full:||4540|
|Average length of the domain:||365.50 aa|
|Average identity of full alignment:||32 %|
|Average coverage of the sequence by the domain:||57.92 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||20|
|Download:||download the raw HMM for this family|
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For all of the domain matches in a full alignment, we count the number that are found on all sequences in the alignment. This total is shown in the purple box.
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There are 8 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_oxid domain has been found. There are 247 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 sequence.
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