Mure, Minae <br/><br/>
Active site rearrangement of the 2-hydrazinopyridine adduct in Escherichia coli amine oxidase to an azo copper(II) chelate form: a key role for tyrosine 369 in controlling the mobility of the TPQ-2HP adduct.  [electronic resource] 

 -  Biochemistry  Feb 2005 
 - 1583-94 p.  digital 
<br/><br/> Publication Type: Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S. 
<br/><br/><label>ISSN: </label>0006-2960 
<br/><br/><label>Standard No.: </label>10.1021/bi0479860  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amine Oxidase (Copper-Containing)--antagonists & inhibitors<br/>Asparagine--genetics<br/>Aspartic Acid--genetics<br/>Azo Compounds--chemistry<br/>Binding Sites--genetics<br/>Cations, Divalent--chemistry<br/>Chelating Agents--chemistry<br/>Cobalt--chemistry<br/>Copper--chemistry<br/>Crystallography, X-Ray<br/>Enzyme Inhibitors--chemistry<br/>Enzyme Stability--genetics<br/>Escherichia coli Proteins--antagonists & inhibitors<br/>Glutamic Acid--genetics<br/>Hydrogen-Ion Concentration<br/>Mutagenesis, Site-Directed<br/>Phenylalanine--genetics<br/>Pyridones--chemistry<br/>Resorcinols--chemistry<br/>Spectrometry, Mass, Electrospray Ionization<br/>Spectrophotometry, Ultraviolet<br/>Spectrum Analysis, Raman<br/>Tyrosine--genetics