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

Biochemistry

Volumn 44, Issue 5, 2005, Pages 1583-1594

  Mure, Minae ^a,b   Kurtis, Christian R ^c   Brown, Doreen E ^d   Rogers, Melanie S ^d   Tambyrajah, Winston S ^c   Saysell, Colin ^c   Wilmot, Carrie M ^e   Phillips, Simon E V ^c   Knowles, Peter F ^c   Dooley, David M ^d   McPherson, Michael J ^c  

^a UNIVERSITY OF KANSAS   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c UNIVERSITY OF LEEDS   (United Kingdom)

^d MONTANA STATE UNIVERSITY   (United States)

^e UNIVERSITY OF MINNESOTA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

COMPOUNDING (CHEMICAL); COPPER; ESCHERICHIA COLI; RAMAN SCATTERING; SPECTROMETERS; SPECTRUM ANALYZERS; X RAY CRYSTALLOGRAPHY;

DEPROTONATION; INCUBATIONS; WILD-TYPE ESCHERICHIA COLI COPPER AMINE OXIDASE (WT-ECAO);

ENZYMES;

2 HYDRAZINOPYRIDINE; 2,4,5 TRIHYDROXYPHENYLALANINE QUINONE; AMINE OXIDASE (COPPER CONTAINING); PHENYLALANINE DERIVATIVE; PYRIDINE DERIVATIVE; UNCLASSIFIED DRUG;

ARTICLE; CATALYSIS; CHELATION; CRYSTAL STRUCTURE; ELECTRON SPIN RESONANCE; ENZYME ACTIVE SITE; ESCHERICHIA COLI; HYDROGEN BOND; NONHUMAN; PH; PRIORITY JOURNAL; PROTON TRANSPORT; RAMAN SPECTROMETRY; SITE DIRECTED MUTAGENESIS; SYNTHESIS; WILD TYPE; X RAY CRYSTALLOGRAPHY;

AMINE OXIDASE (COPPER-CONTAINING); ASPARAGINE; ASPARTIC ACID; AZO COMPOUNDS; BINDING SITES; CATIONS, DIVALENT; CHELATING AGENTS; COBALT; COPPER; CRYSTALLOGRAPHY, X-RAY; ENZYME INHIBITORS; ENZYME STABILITY; ESCHERICHIA COLI PROTEINS; GLUTAMIC ACID; HYDROGEN-ION CONCENTRATION; MUTAGENESIS, SITE-DIRECTED; PHENYLALANINE; PYRIDONES; RESORCINOLS; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; SPECTROPHOTOMETRY, ULTRAVIOLET; SPECTRUM ANALYSIS, RAMAN; TYROSINE;

ESCHERICHIA COLI; NEGIBACTERIA;

EID: 20844443638     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0479860     Document Type: Article

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