1998
DOI: 10.1074/jbc.273.15.8581
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Rat and Calf Thioredoxin Reductase Are Homologous to Glutathione Reductase with a Carboxyl-terminal Elongation Containing a Conserved Catalytically Active Penultimate Selenocysteine Residue

Abstract: We have determined the sequence of 23 peptides from bovine thioredoxin reductase covering 364 amino acid residues. The result was used to identify a rat cDNA clone (2.19 kilobase pairs), which contained an open reading frame of 1496 base pairs encoding a protein with 498 residues. The bovine and rat thioredoxin reductase sequences revealed a close homology to glutathione reductase including the conserved active site sequence (Cys-Val-Asn-Val-Gly-Cys). This also confirmed the identity of a previously published … Show more

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Cited by 245 publications
(257 citation statements)
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“…1) [13,16]. The major feature distinguishing TrxR from GR is the C-terminal extension with a cysteine-selenocysteinecontaining second redox active site [23]. This mobile reduction site enables the acceptance of different substrates.…”
Section: Resultsmentioning
confidence: 99%
“…1) [13,16]. The major feature distinguishing TrxR from GR is the C-terminal extension with a cysteine-selenocysteinecontaining second redox active site [23]. This mobile reduction site enables the acceptance of different substrates.…”
Section: Resultsmentioning
confidence: 99%
“…The mammalian TrxR directly reduces not only Trx from different species but also many nondisulfide substrates, such as selenite (8), lipid hydroperoxides (9), and H 2 O 2 (10). Sequencing and cloning demonstrated that cytosolic human and rat TrxR are highly similar to GR (11,12) and not to its E. coli counterpart (13). The sequence contains one active-site sequence motif-Cys 59 -Val-Asn-Val-Gly-Cys 64 -identical to the redox-active disulfide of GR (14).…”
mentioning
confidence: 99%
“…The sequence contains one active-site sequence motif-Cys 59 -Val-Asn-Val-Gly-Cys 64 -identical to the redox-active disulfide of GR (14). The Cterminal end contains an extension of 16 residues with a penultimate selenocysteine (SeCys) residue within the unique sequence, Gly-Cys-SeCys-Gly conserved in all mammalian TrxR reported to date (12,(15)(16)(17)(18)(19). The SeCys residue is essential for the catalytic activity of TrxR, because either its removal by carboxypeptidase digestion (12) or its modification by alkylation (12,20) leads to inactivation.…”
mentioning
confidence: 99%
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“…Although most selenoproteins contain Sec in the N-terminal portion or in the middle of the protein, TR contains Sec as a C-terminal penultimate residue [35,38,102], which is essential for enzyme activity [ 1,42,52]. TR is a homodimer consisting of two identical 55-kd subunits, each containing a ravin adenine dinucleotide cofactor.…”
Section: (8) Thioredoxin Reductase (Tr)mentioning
confidence: 99%