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Identification and Characterization of TRP14, a Thioredoxin-related Protein of 14 kDa: New insights into the specificity of thioredoxin function

Title
Identification and Characterization of TRP14, a Thioredoxin-related Protein of 14 kDa: New insights into the specificity of thioredoxin function
Authors
Jeong W.Yoon H.W.Lee S.-R.Rhee S.G.
Ewha Authors
이서구이승록정우진
SCOPUS Author ID
이서구scopusscopus; 정우진scopus
Issue Date
2004
Journal Title
Journal of Biological Chemistry
ISSN
0021-9258JCR Link
Citation
vol. 279, no. 5, pp. 3142 - 3150
Indexed
SCI; SCIE; SCOPUS WOS scopus
Abstract
We have identified and characterized a 14-kDa human thioredoxin (Trx)-related protein designated TRP14. This cytosolic protein was expressed in all tissues and cell types examined, generally in smaller amounts than Trx1. Although TRP14 contains five cysteines, only the two Cys residues in its WCPDC motif were exposed and redox sensitive. Unlike Trx1, which was an equally good substrate for both Trx reductase 1 (TrxR1) and TrxR2, oxidized TRP14 was reduced by TrxR1 but not by TrxR2. Biochemical characterization of TRP14 suggested that, like Trx1, TRP14 is a disulfide reductase; its active site cysteine is sufficiently nucleophilic with the pKa value of 6.1; and its redox potential (-257 mV) is similar to those of other cellular thiol reductants. However, although TRP14 reduced small disulfide-containing peptides, it did not reduce the disulfides of known Trx1 substrates, ribonucleotide reductase, peroxiredoxin, and methionine sulfoxide reductase. These results suggest that TRP14 and Trx1 might act on distinct substrate proteins.
DOI
10.1074/jbc.M307932200
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일반대학원 > 생명·약학부 > Journal papers
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