Copper Amine Oxidase

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{{STRUCTURE_2d1w | PDB=2d1w | SCENE= }}
{{STRUCTURE_2d1w | PDB=2d1w | SCENE= }}
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2d1w is a [http://en.wikipedia.org/wiki/Amine_oxidase_%28copper-containing%29 copper amine oxidase] found in [http://en.wikipedia.org/wiki/Arthrobacter_globiformis Arthrobacter globiformis].
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2d1w is a [http://en.wikipedia.org/wiki/Amine_oxidase_%28copper-containing%29 copper amine oxidase] derived from [http://en.wikipedia.org/wiki/Arthrobacter_globiformis Arthrobacter globiformis]. The structure of this enzyme was determined by Murakawa et al. in 2005, by x-ray diffraction<ref>PMID:16487484</ref>. It consists of a homodimer, with each subunit containing 638 residues, one of which is a modified tyrosine residue. Each subunit also contains a copper ligand,<scene name='Sandbox_Reserved_331/Copper_ligand/5'> shown here</scene>, near the active site, which is coordinated by three histidine residues. Located near the Cu<sup>2+</sup> ligand is a cofactor, topa quinone, both of which play a central role in the enzyme's activity<ref>PMID:8591028</ref>.
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The structure of this enzyme was determined by Murakawa et al. in 2005 <ref>PMID:16487484</ref>. It consists of a dimer containing 638 residues, and there is a copper ligand located near the center of each subunit.
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=== Ligand ===
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The Cu<sup>2+</sup> ligand<scene name='Sandbox_Reserved_331/Copper_ligand/5'> (shown here)</scene> is coordinated by three histidine residues and is located near the active site of the enzyme.
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=== Modified Residue ===
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Residue 382 consists of a modified residue, derived from tyrosine, that joins two peptide chains, much like a disulfide bridge would.
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[[Image:TTS.png|left|frame|alt=3-((3E)-4-HYDROXY-3-{[2-(4-HYDROXYPHENYL)ETHYL]IMINO}-6-OXOCYCLOHEXA-1,4-DIEN-1-YL)ALANINE.|Residue 382 is a modified tyrosine residue.]]
[[Image:TTS.png|left|frame|alt=3-((3E)-4-HYDROXY-3-{[2-(4-HYDROXYPHENYL)ETHYL]IMINO}-6-OXOCYCLOHEXA-1,4-DIEN-1-YL)ALANINE.|Residue 382 is a modified tyrosine residue.]]

Revision as of 17:28, 31 March 2011

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Structure

Template:STRUCTURE 2d1w 2d1w is a copper amine oxidase derived from Arthrobacter globiformis. The structure of this enzyme was determined by Murakawa et al. in 2005, by x-ray diffraction[1]. It consists of a homodimer, with each subunit containing 638 residues, one of which is a modified tyrosine residue. Each subunit also contains a copper ligand,, near the active site, which is coordinated by three histidine residues. Located near the Cu2+ ligand is a cofactor, topa quinone, both of which play a central role in the enzyme's activity[2].

Residue 382 is a modified tyrosine residue.
Residue 382 is a modified tyrosine residue.


Reaction

Copper amine oxidase catalyzes the oxidation of a primary amine to the corresponding aldehyde, yielding hydrogen peroxide and free ammonia. An example of this is the oxidation of tyramine:

The oxidation of tyramine.

References

  1. ↑ Murakawa T, Okajima T, Kuroda S, Nakamoto T, Taki M, Yamamoto Y, Hayashi H, Tanizawa K. Quantum mechanical hydrogen tunneling in bacterial copper amine oxidase reaction. Biochem Biophys Res Commun. 2006 Apr 7;342(2):414-23. Epub 2006 Feb 8. PMID:16487484 doi:10.1016/j.bbrc.2006.01.150
  2. ↑ Parsons MR, Convery MA, Wilmot CM, Yadav KD, Blakeley V, Corner AS, Phillips SE, McPherson MJ, Knowles PF. Crystal structure of a quinoenzyme: copper amine oxidase of Escherichia coli at 2 A resolution. Structure. 1995 Nov 15;3(11):1171-84. PMID:8591028

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