Structure and mechanism of sanguinarine reductase, an enzyme of alkaloid detoxification

Journal of Biological Chemistry

Volumn 285, Issue 24, 2010, Pages 18397-18406

  Vogel, Matthias ^a   Lawson, Michael ^a   Sippl, Wolfgang ^a   Conrad, Udo ^b   Roos, Werner ^a  

^a MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

^b LEIBNIZ INSTITUTE OF PLANT GENETICS AND CROP PLANT RESEARCH IPK   (Germany)

Author keywords

[No Author keywords available]

Indexed keywords

A PLANTS; AMINO ACID SEQUENCE; CATALYTIC PROCESS; CATALYTIC SITES; CATALYTIC TRIAD; CELL WALLS; CYTOTOXIC EFFECTS; IN-SILICO SCREENING; RECOMBINANT ENZYMES; ROSSMANN FOLD; SANGUINARINE; SELECTIVE CATALYSTS; SEQUENCE SIMILARITY; SITE DIRECTED MUTAGENESIS; SPATIAL CONFORMATION; STRUCTURAL SIMILARITY; THREE-DIMENSIONAL MODEL; THREE-DIMENSIONAL STRUCTURE; THRESHOLD CONCENTRATIONS; X-RAY STRUCTURE;

AMINO ACIDS; ANIMAL CELL CULTURE; CATALYSTS; CELL CULTURE; DETOXIFICATION; ENZYMES; ORGANIC ACIDS; THREE DIMENSIONAL;

ENZYME ACTIVITY;

EPIMERASE; HYDROXYSTEROID DEHYDROGENASE; NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE BINDING REDUCTASE; OXIDOREDUCTASE; RECOMBINANT ENZYME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE BINDING REDUCTASE; SANGUINARINE REDUCTASE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; CATALYSIS; COMPUTER ANALYSIS; CONTROLLED STUDY; CRYSTAL STRUCTURE; DETOXIFICATION; ENZYME ACTIVE SITE; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME ENGINEERING; ENZYME MECHANISM; ENZYME STRUCTURE; ESCHSCHOLTZIA; NONHUMAN; NUCLEOTIDE SEQUENCE; PLANT CELL CULTURE; PRIORITY JOURNAL; SEQUENCE HOMOLOGY; SITE DIRECTED MUTAGENESIS; STRUCTURAL HOMOLOGY;

AMINO ACID SEQUENCE; AMINO ACIDS; BENZOPHENANTHRIDINES; BIOCHEMISTRY; CATALYSIS; CYTOPLASM; ESCHSCHOLZIA; ISOQUINOLINES; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; NADP; OXIDOREDUCTASES; OXIDOREDUCTASES ACTING ON CH-NH GROUP DONORS; PEPTIDES; PLANT PROTEINS; PLANTS; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID;

BACTERIA (MICROORGANISMS); ESCHSCHOLZIA CALIFORNICA; PAPAVERACEAE;

EID: 77953305612     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.088989     Document Type: Article

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