Why is mammalian thioredoxin reductase 1 so dependent upon the use of selenium?

Biochemistry

Volumn 53, Issue 3, 2014, Pages 554-565

  Lothrop, Adam P ^a   Snider, Gregg W ^a   Ruggles, Erik L ^a   Hondal, Robert J ^a  

^a UNIVERSITY OF VERMONT COLLEGE OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CAENORHABDITIS ELEGANS; DROSOPHILA MELANOGASTER; HIGH MOLECULAR WEIGHT; MECHANISTIC DIFFERENCES; PLASMODIUM FALCIPARUM; SUBSTRATE UTILIZATION; THIOREDOXIN REDUCTASE; THIOREDOXIN REDUCTASE 1;

AMINO ACIDS; CATALYST ACTIVITY; ENZYMES; MAMMALS; MOLECULES; REDOX REACTIONS; SELENIUM; SELENIUM COMPOUNDS; SEMICONDUCTING SELENIUM COMPOUNDS;

SUBSTRATES;

AMINO ACID; DNA; MITOCHONDRIAL ENZYME; SELENIUM; SELENOCYSTEINE; THIOREDOXIN; THIOREDOXIN REDUCTASE 1;

AMINO ACID SEQUENCE; ARTICLE; CAENORHABDITIS ELEGANS; CATALYSIS; CYTOSOL; DROSOPHILA MELANOGASTER; ELECTRON; ENZYME ACTIVITY; ENZYME ASSAY; ENZYME KINETICS; ENZYME SUBSTRATE; MAMMAL; MITOCHONDRION; MOLECULE; MOUSE; MUTANT; NONHUMAN; NUCLEOPHILICITY; OXIDATION REDUCTION REACTION; PEPTIDE SYNTHESIS; PLASMODIUM FALCIPARUM; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PURIFICATION;

AMINO ACID SEQUENCE; ANIMALS; CATTLE; CYSTINE; GLUTATHIONE REDUCTASE; HUMANS; KINETICS; MICE; MOLECULAR SEQUENCE DATA; MUTATION; ORGANOSELENIUM COMPOUNDS; OXIDATION-REDUCTION; SELENIUM; SELENOCYSTEINE; SEQUENCE ALIGNMENT; SUBSTRATE SPECIFICITY; THIOREDOXIN REDUCTASE 1;

EID: 84893484616     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi400651x     Document Type: Article

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