Structural and biochemical studies reveal differences in the catalytic mechanisms of mammalian and Drosophila melanogaster thioredoxin reductases

Biochemistry

Volumn 46, Issue 16, 2007, Pages 4694-4705

  Eckenroth, Brian E ^a   Rould, Mark A ^b   Hondal, Robert J ^a   Everse, Stephen J ^a  

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

^b UNIVERSITY OF VERMONT   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCATALYSTS; BIOCHEMISTRY; CHEMICAL BONDS; CONFORMATIONS; CRYSTAL STRUCTURE; REDOX REACTIONS;

DISULFIDE BOND; DROSOPHILA MELANOGASTER THIOREDOXIN REDUCTASES; MAMMALIAN THIOREDOXIN; SELENOCYSTEINE (SEC);

ENZYMES;

CYSTEINE; DISULFIDE; GLUTATHIONE; GLUTATHIONE REDUCTASE; HISTIDINE; OXIDOREDUCTASE; PYRIDINE NUCLEOTIDE; SELENOCYSTEINE; TETRAPEPTIDE; THIOREDOXIN REDUCTASE;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; CRYSTAL STRUCTURE; DISULFIDE BOND; DROSOPHILA MELANOGASTER; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME DEGRADATION; ENZYME KINETICS; ENZYME STRUCTURE; ENZYME SUBSTRATE; MAMMAL; MITOCHONDRION; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; OXIDATION; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTON TRANSPORT; RING OPENING; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; ANIMALS; CATALYSIS; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; CYSTEINE; DITHIONITROBENZOIC ACID; DROSOPHILA MELANOGASTER; MICE; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; OLIGOPEPTIDES; SELENOCYSTEINE; THIOREDOXIN REDUCTASE (NADPH);

DROSOPHILA MELANOGASTER; MAMMALIA;

EID: 34247479503     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi602394p     Document Type: Article

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