Catalytic and structural role of a conserved active site histidine in berberine bridge enzyme

Biochemistry

Volumn 51, Issue 31, 2012, Pages 6139-6147

  Wallner, Silvia ^a   Winkler, Andreas ^a,c   Riedl, Sabrina ^a,d   Dully, Corinna ^a   Horvath, Stefanie ^a   Gruber, Karl ^b   MacHeroux, Peter ^a  

^a GRAZ UNIVERSITY OF TECHNOLOGY   (Austria)

^b UNIVERSITY OF GRAZ   (Austria)

^c MAX PLANCK INSTITUTE FOR MEDICAL RESEARCH   (Germany)

^d ERICH SCHMID INSTITUTE OF MATERIALS SCIENCE   (Austria)

Author keywords

[No Author keywords available]

Indexed keywords

ACTIVE SITE; ACTIVE SITE RESIDUES; FLAVIN COFACTOR; HYDROGEN BONDING NETWORK; HYDROXYL GROUPS; MIDPOINT POTENTIALS; NEGATIVE CHARGE; OXIDATIVE CYCLIZATION; REDOX POTENTIALS; REDUCED-STATE; SIDE-CHAINS; STABILIZING EFFECTS; STRUCTURAL CHARACTERIZATION; STRUCTURAL ORGANIZATION; STRUCTURAL REARRANGEMENT; WILD-TYPE ENZYMES;

AMINO ACIDS; CATALYSIS; KINETIC PARAMETERS; REDOX REACTIONS;

ENZYMES;

ALANINE; BERBERINE; HISTIDINE; HYDROXYL GROUP; QUERCETIN;

ARTICLE; BIOCHEMICAL COMPOSITION; CATALYSIS; CRYSTAL STRUCTURE; CRYSTALLIZATION; ENZYME ACTIVE SITE; GEL FILTRATION CHROMATOGRAPHY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HYDROGEN BOND; MOLECULAR INTERACTION; OXIDATION REDUCTION POTENTIAL; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN STABILITY; PROTEIN STRUCTURE; SITE DIRECTED MUTAGENESIS; STEADY STATE; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; WILD TYPE;

BIOCATALYSIS; CATALYTIC DOMAIN; CONSERVED SEQUENCE; CYSTEINE; ENZYME STABILITY; HISTIDINE; KINETICS; MODELS, MOLECULAR; OXIDATION-REDUCTION; OXIDOREDUCTASES, N-DEMETHYLATING; OXYGEN; PHOTOCHEMICAL PROCESSES;

EID: 84864700906     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300411n     Document Type: Article

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