An oxidative N-demethylase reveals PAS transition from ubiquitous sensor to enzyme

Nature

Volumn 539, Issue 7630, 2016, Pages 593-597

  Ortmayer, Mary ^a   Lafite, Pierre ^a,b   Menon, Binuraj R K ^a   Tralau, Tewes ^a,c   Fisher, Karl ^a   Denkhaus, Lukas ^a   Scrutton, Nigel S ^a   Rigby, Stephen E J ^a   Munro, Andrew W ^a   Hay, Sam ^a   Leys, David ^a  

^a UNIVERSITY OF MANCHESTER   (United Kingdom)

^b UNIVERSITÉ D'ORLÉANS   (France)

^c FEDERAL INSTITUTE FOR RISK ASSESSMENT   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

AMINE OXIDASE (FLAVIN CONTAINING); BINDING PROTEIN; DIMETHYLAMINE; FLAVINE MONONUCLEOTIDE; HEME; N DEMETHYLASE; OXYGEN; PAS PROTEIN; PROTON; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; TETRAHYDROFOLIC ACID; UNCLASSIFIED DRUG; 5,6,7,8-TETRAHYDROFOLIC ACID; COENZYME; IRON SULFUR PROTEIN; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; PROTEIN SUBUNIT; TETRAHYDROFOLIC ACID DERIVATIVE;

CATALYSIS; CHEMICAL BINDING; ENZYME ACTIVITY; LIGAND; MOLECULAR ANALYSIS; ORGANIC ACID; OXIDATION; POLARIZATION;

ALPHA CHAIN; ARTICLE; BINDING SITE; CATALYSIS; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ELECTRON; ENZYME SUBSTRATE; NONHUMAN; OXIDATION REDUCTION POTENTIAL; OXYGEN AFFINITY; PRIORITY JOURNAL; PROTEIN BINDING; UBIQUITINATION; CHEMISTRY; COENZYME; ENZYMOLOGY; METABOLISM; MOLECULAR MODEL; OXIDATION REDUCTION REACTION; PROTEIN DOMAIN; PROTEIN SUBUNIT; PSEUDOMONAS MENDOCINA; X RAY CRYSTALLOGRAPHY;

BINDING SITES; COENZYMES; CRYSTALLOGRAPHY, X-RAY; DIMETHYLAMINES; FLAVIN MONONUCLEOTIDE; HEME; IRON-SULFUR PROTEINS; MODELS, MOLECULAR; NADP; OXIDATION-REDUCTION; OXIDOREDUCTASES, N-DEMETHYLATING; OXYGEN; PROTEIN DOMAINS; PROTEIN SUBUNITS; PSEUDOMONAS MENDOCINA; TETRAHYDROFOLATES;

EID: 85016144548     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature20159     Document Type: Article

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