Copper Amine Oxidase

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Contents 1 Structure 1.1 Ligand 1.2 Modified Residue 2 Reaction 3 References

Structure

Template:STRUCTURE 2d1w 2d1w is a copper amine oxidase found in Arthrobacter globiformis. The structure of this enzyme was determined by Murakawa et al. in 2005 ^[1]. It consists of a dimer containing 638 residues, and there is a copper ligand located near the center of each subunit.

Ligand

The Cu²⁺ ligand is coordinated by three histidine residues and is located near the active site of the enzyme.

Modified Residue

Residue 382 consists of a modified residue, derived from tyrosine, that joins two peptide chains, much like a disulfide bridge would.

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:

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