Isotope effects reveal that para-substituted benzylamines are poor reactivity probes of the quinoprotein mechanism for aromatic amine dehydrogenase

Biochemistry

Volumn 46, Issue 32, 2007, Pages 9250-9259

  Hothi, Parvinder ^a   Roujeinikova, Anna ^a   Khadra, Khalid Abu ^a   Lee, Michael ^b   Cullis, Paul ^b   Leys, David ^a   Scrutton, Nigel S ^a  

^a UNIVERSITY OF MANCHESTER   (United Kingdom)

^b UNIVERSITY OF LEICESTER   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC AMINE DEHYDROGENASES; KINETIC ISOTOPE EFFECTS (KIE);

BINDING SITES; CATALYSIS; CRYSTALLOGRAPHY; ENZYMES; ISOTOPES; SUBSTITUTION REACTIONS;

AMINES;

ARALKYLAMINE DEHYDROGENASE; BENZYLAMINE DERIVATIVE; DEUTERIUM; ISOTOPE; OXIDOREDUCTASE; PHENETHYLAMINE; PROTEIN; UNCLASSIFIED DRUG;

ARTICLE; CRYSTALLOGRAPHY; ENZYME ACTIVE SITE; ENZYME KINETICS; ENZYME MECHANISM; ENZYME SUBSTRATE COMPLEX; PRIORITY JOURNAL; PROTON TRANSPORT; QUANTITATIVE STRUCTURE ACTIVITY RELATION; REACTION ANALYSIS;

BENZYLAMINES; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; DEUTERIUM; HYDROGEN BONDING; ISOTOPE LABELING; KINETICS; OXIDOREDUCTASES ACTING ON CH-NH GROUP DONORS; PHENETHYLAMINES; QUANTITATIVE STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 34547901822     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi7007239     Document Type: Article

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