Essential role of selenium in the catalytic activities of mammalian thioredoxin reductase revealed by characterization of recombinant enzymes with selenocysteine mutations

Journal of Biological Chemistry

Volumn 275, Issue 24, 2000, Pages 18121-18128

  Zhong, Liangwei ^a   Holmgren, Arne ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; FLAVINE ADENINE NUCLEOTIDE; GLUTATHIONE REDUCTASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; SELENIUM; SELENOCYSTEINE; SERINE; THIOREDOXIN; THIOREDOXIN REDUCTASE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME KINETICS; ENZYME MECHANISM; ENZYME STRUCTURE; NUCLEOTIDE SEQUENCE; PKA; PRIORITY JOURNAL; REDUCTION; STRUCTURE ACTIVITY RELATION;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ANIMALS; CATALYSIS; COS CELLS; ERYTHROCYTES; GLUTATHIONE REDUCTASE; HUMANS; HYDROGEN PEROXIDE; KINETICS; MOLECULAR SEQUENCE DATA; MUTAGENESIS, SITE-DIRECTED; OXIDATION-REDUCTION; PROTEIN STRUCTURE, SECONDARY; RATS; RECOMBINANT PROTEINS; SELENIUM; SELENOCYSTEINE; SPECTROPHOTOMETRY, ATOMIC; STRUCTURE-ACTIVITY RELATIONSHIP; THIOREDOXIN REDUCTASE (NADPH);

ESCHERICHIA COLI; FELIS CATUS; MAMMALIA;

EID: 0034674566     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M000690200     Document Type: Article

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