The mechanism of thioredoxin reductase from human placenta is similar to the mechanisms of lipoamide dehydrogenase and glutathione reductase and is distinct from the mechanism of thioredoxin reductase from Escherichia coli

Proceedings of the National Academy of Sciences of the United States of America

Volumn 94, Issue 8, 1997, Pages 3621-3626

  Arscott, L David ^a   Gromer, Stephan ^b   Schirmer, R Heiner ^b   Becker, Katja ^b   Williams Jr , Charles H ^a,c,d  

^a UNIVERSITY OF MICHIGAN   (United States)

^b UNIVERSITY OF HEIDELBERG   (Germany)

^c UNIVERSITY OF MICHIGAN MEDICAL SCHOOL   (United States)

^d VETERANS AFFAIRS MEDICAL CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DIHYDROLIPOAMIDE DEHYDROGENASE; GLUTATHIONE REDUCTASE; NITROSOUREA DERIVATIVE; THIOREDOXIN REDUCTASE;

AMINO ACID SEQUENCE; ARTICLE; ENZYME MECHANISM; ENZYME STRUCTURE; ESCHERICHIA COLI; NONHUMAN; PHYLOGENY; PLACENTA; PRIORITY JOURNAL; SEQUENCE HOMOLOGY; STRUCTURE ANALYSIS;

DIHYDROLIPOAMIDE DEHYDROGENASE; ESCHERICHIA COLI; EVOLUTION, MOLECULAR; FEMALE; GLUTATHIONE REDUCTASE; HUMANS; NADP; PLACENTA; PREGNANCY; SUBSTRATE SPECIFICITY; THIOREDOXIN REDUCTASE (NADPH);

EID: 0030887844     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.94.8.3621     Document Type: Article

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