Copper Amine Oxidase

From Proteopedia

proteopedia linkproteopedia link

This Sandbox is Reserved from January 10, 2010, through April 10, 2011 for use in BCMB 307-Proteins course taught by Andrea Gorrell at the University of Northern British Columbia, Prince George, BC, Canada.

To get started: Click the edit this page tab at the top. Save the page after each step, then edit it again. Click the 3D button (when editing, above the wikitext box) to insert Jmol. show the Scene authoring tools, create a molecular scene, and save it. Copy the green link into the page. Add a description of your scene. Use the buttons above the wikitext box for bold, italics, links, headlines, etc. More help: Help:Editing

Template:STRUCTURE 2d1w

Contents 1 Structure 2 Reaction 2.1 Overview 2.2 Mechanism 3 Additional Resources 4 References

Structure

2d1w is a copper amine oxidase derived from Arthrobacter globiformis, and is classified as classified as EC 1.4.3.6 in the EC number classification of enzymes. It belongs to the larger class of oxidoreductases. The structure of this enzyme was determined by Murakawa et al. in 2005, by x-ray diffraction^[1]. It consists of a disulfide-linked homodimer, with each subunit containing 638 residues. 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 modified tyrosine residue, which is similar in structure to a cofactor in many other copper amine oxidases, topa quinone^[2]. The active site of the enzyme is located near the center of the homodimer, which is connected to the outside of the enzyme by an extensively hydrated channel. It is suspected that the water helps to carry O₂ to the active site^[3].

Reaction

Overview

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:

Mechanism

Additional Resources

• Entry 2D1W in the RCSB Protein Data Bank
• The Biosynthesis of Topa Quinone Cofactor in Bacterial Amine Oxidases

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
3. ↑ Mure M, Mills SA, Klinman JP. Catalytic mechanism of the topa quinone containing copper amine oxidases. Biochemistry. 2002 Jul 30;41(30):9269-78. PMID:12135347