The penultimate selenocysteine residue at the C-terminus of mammalian thioredoxin reductase plays an obligatory role in the NADPH-disulfide oxidoreductase catalytic mechanism

BioFactors

Volumn 11, Issue 1-2, 2000, Pages 79-81

  Gorlatov, Sergey N ^a   Stadtman, Thressa C ^a  

^a NATIONAL HEART LUNG AND BLOOD INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MAMMALIA;

DISULFIDE; OXIDOREDUCTASE; SELENOCYSTEINE; THIOREDOXIN REDUCTASE;

ANIMAL; ARTICLE; BINDING SITE; CATALYSIS; CHEMISTRY; HUMAN; METABOLISM; STRUCTURE ACTIVITY RELATION;

ANIMALS; BINDING SITES; CATALYSIS; DISULFIDES; HUMANS; NADH, NADPH OXIDOREDUCTASES; SELENOCYSTEINE; STRUCTURE-ACTIVITY RELATIONSHIP; THIOREDOXIN REDUCTASE (NADPH);

EID: 0033628852     PISSN: 09516433     EISSN: None     Source Type: Journal    
DOI: 10.1002/biof.5520110123     Document Type: Article

References (7)

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2. L.D. Arscott, S. Gromer, R.H. Schirmer, K. Becker and C.H. Williams, Jr., 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, Proc. Nat. Acad. Sci. USA 94 (1997), 3621-3626.
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5. V.N. Gladyshev, K.-T. Jeang and T.C. Stadtman, Selenocysteine, identified as the penultimate residue in human T-cell thioredoxin reductase, corresponds to TGA in the human placental gene, Proc. Nat. Acad. Sci. USA 93 (1996), 6146-6151.
6. S.-Y. Liu and T.C. Stadtman, Heparin-binding properties of selenium-containing thioredoxin reductase from HeLa cells and human lung adenocarcinoma cells, Proc. Nat. Acad. Sci. USA 94 (1997), 6138-6141.
7. S.N. Gorlatov and T.C. Stadtman, Human thioredoxin reductase from HeLa cells: selective alkylation of Selenocysteine in the protein inhibits enzyme activity and reduction with NADPH influences affinity to heparin, Proc. Nat. Acad. Sci. USA 95 (1998) (in press).