Copper Amine Oxidase
From Proteopedia
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=== Modified Residue === | === Modified 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.]] | [[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.]] | ||
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== Reaction == | == Reaction == | ||
| + | Copper amine oxidase catalyzes the oxidation of a primary amine to an aldehyde, yielding hydrogen peroxide and free ammonia. An example of this is the oxidation of [http://en.wikipedia.org/wiki/Tyramine | tyramine]: | ||
| + | [[Image:Tyramine oxidation.png|The oxidation of tyramine.]] | ||
== References == | == References == | ||
<references /> | <references /> | ||
Revision as of 02:51, 13 March 2011
| 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. |
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2d1w is a copper amine oxidase found in Arthrobacter globiformis.
Contents |
Structure
Ligand
A closeup of the Cu2+ .
Modified Residue
Reaction
Copper amine oxidase catalyzes the oxidation of a primary amine to an aldehyde, yielding hydrogen peroxide and free ammonia. An example of this is the oxidation of | tyramine:
References
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Raymond Lyle, Alexander Berchansky, OCA, Jaime Prilusky


