Rat and calf thioredoxin reductase are homologous to glutathione reductase with a carboxyl-terminal elongation containing a conserved catalytically active penultimate selenocysteine residue

Journal of Biological Chemistry

Volumn 273, Issue 15, 1998, Pages 8581-8591

  Zhong, Liangwei ^a   Arnér, Elias S J ^a   Ljung, Johanna ^a   Åslund, Fredrik ^a   Holmgren, Arne ^a  

^a KAROLINSKA INSTITUTE   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

GLUTATHIONE REDUCTASE; THIOREDOXIN REDUCTASE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CATTLE; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME STRUCTURE; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; RAT; SEQUENCE HOMOLOGY; STRUCTURE ANALYSIS;

AMINO ACID SEQUENCE; ANIMALS; BASE SEQUENCE; BINDING SITES; CATALYSIS; CATTLE; CLONING, MOLECULAR; CONSENSUS SEQUENCE; CONSERVED SEQUENCE; DNA, COMPLEMENTARY; GLUTATHIONE REDUCTASE; HUMANS; LIVER; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NADP; NUCLEIC ACID CONFORMATION; PEPTIDE FRAGMENTS; PYRIDINES; RATS; SELENIUM; SELENOCYSTEINE; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SEQUENCE HOMOLOGY, NUCLEIC ACID; THIOREDOXIN REDUCTASE (NADPH); THYMUS GLAND;

BOS TAURUS; BOVINAE; EUKARYOTA;

EID: 0032502720     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.273.15.8581     Document Type: Article

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