Details in the catalytic mechanism of mammalian thioredoxin reductase 1 revealed using point mutations and juglone-coupled enzyme activities

Free Radical Biology and Medicine

Volumn 94, Issue , 2016, Pages 110-120

  Xu, Jianqiang ^a,b   Cheng, Qing ^b   Arnér, Elias S J ^b  

^a DALIAN UNIVERSITY OF TECHNOLOGY   (China)

^b KAROLINSKA INSTITUTE   (Sweden)

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; CYSTEINE; DISULFIDE; DITHIOL DERIVATIVE; FLAVINE ADENINE NUCLEOTIDE; JUGLONE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE OXIDASE; SELENOCYSTEINE; SUPEROXIDE; THIOREDOXIN REDUCTASE 1; AMINO ACID; NAPHTHOQUINONE; TXNRD1 PROTEIN, HUMAN;

AMINO ACID SUBSTITUTION; ARTICLE; ARYLATION; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; CYTOTOXICITY; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME MECHANISM; NONHUMAN; POINT MUTATION; PRIORITY JOURNAL; PROTEIN MOTIF; RAT; CATALYSIS; CHEMISTRY; ENZYME SPECIFICITY; GENETICS; HUMAN; METABOLISM; MUTATION; OXIDATION REDUCTION REACTION;

AMINO ACIDS; CATALYSIS; CYSTEINE; HUMANS; MUTATION; NADPH OXIDASES; NAPHTHOQUINONES; OXIDATION-REDUCTION; POINT MUTATION; SELENOCYSTEINE; SUBSTRATE SPECIFICITY; SUPEROXIDES; THIOREDOXIN REDUCTASE 1;

EID: 84959322213     PISSN: 08915849     EISSN: 18734596     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2016.02.013     Document Type: Article

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