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]
Producer: 20050607Description: 1583-94 p. digitalISSN:- 0006-2960
- Amine Oxidase (Copper-Containing) -- antagonists & inhibitors
- Asparagine -- genetics
- Aspartic Acid -- genetics
- Azo Compounds -- chemistry
- Binding Sites -- genetics
- Cations, Divalent -- chemistry
- Chelating Agents -- chemistry
- Cobalt -- chemistry
- Copper -- chemistry
- Crystallography, X-Ray
- Enzyme Inhibitors -- chemistry
- Enzyme Stability -- genetics
- Escherichia coli Proteins -- antagonists & inhibitors
- Glutamic Acid -- genetics
- Hydrogen-Ion Concentration
- Mutagenesis, Site-Directed
- Phenylalanine -- genetics
- Pyridones -- chemistry
- Resorcinols -- chemistry
- Spectrometry, Mass, Electrospray Ionization
- Spectrophotometry, Ultraviolet
- Spectrum Analysis, Raman
- Tyrosine -- genetics
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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.
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