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Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity.
Open accessAbstract
Homogeneous native and recombinant porcine liver thioltransferase (glutaredoxin), bovine thymus and human placenta thioltransferase (glutaredoxin) were examined for dehydroascorbate reductase activity (EC 1.8.5.1) involving the direct catalytic reduction of dehydroascorbic acid (DHA) by glutathione. Each enzyme had substantial activity with apparent Km and Vmax for dehydroascorbate between 0.2 and 2.2 mM and 6-27 nmol min-1, respectively, and for gluathione between 1.6 and 8.7 mM and 11-30 nmol min-1, respectively. In the presence of purified bovine liver thioredoxin reductase, homogeneous bovine liver thioredoxin failed to reduce DHA to ascorbic acid as measured by NADPH oxidation. Highly purified bovine liver protein disulfide isomerase (PDI) reacted directly with DHA and GSH to catalyze the reduction of DHA to ascorbic acid. The apparent Km for DHA was 1.0 mM and the Vmax was 8 nmol min-1, and for GSH were 3.9 mM and 14 nmol min-1, respectively. These results suggest that thioltransferase and PDI contribute to the regeneration of oxidized ascorbic acid in mammalian cells, and based on their cellular location, thioltransferase is proposed to be the major cytoplasmic activity, whereas interaction of DHA with microsomal membrane PDI may catalyze regeneration of ascorbic acid and initiate oxidation of intralumenal protein thiols to disulfides.
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Cites
The role of ascorbate in the prolyl hydroxylase reaction
Myllylä, R., Kuutti-Savolainen, E.-R., & Kivirikko, K. I. (1978) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(78)91010-0 · Cited by 213
Cited by
Ascorbic Acid in Plants: Biosynthesis and Function
Smirnoff, N., & Wheeler, G. L. (2000) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230008984166 · Cited by 852
Vitamin C. Biosynthesis, recycling and degradation in mammals
Linster, C. L., & Van Schaftingen, E. (2007) · The FEBS Journal · doi:10.1111/j.1742-4658.2006.05607.x · Cited by 757
Thioredoxin and Related Molecules–From Biology to Health and Disease
Lillig, C. H., & Holmgren, A. (2007) · Antioxidants & Redox Signaling · doi:10.1089/ars.2007.9.25 · Cited by 724
Intracellular Antioxidants: from Chemical to Biochemical Mechanisms
Chaudière, J., & Ferrari-Iliou, R. (1999) · Food and Chemical Toxicology · doi:10.1016/s0278-6915(99)00090-3 · Cited by 671
Lillig, C. H., Berndt, C., & Holmgren, A. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.06.003 · Cited by 561
Metadata
- Authors
- Wells, W. W., Xu, D. P., Yang, Y. F., & Rocque, P. A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1990-09
- Volume
- 265
- Issue
- 26
- Pages
- 15361-15364
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1503977217
- Cited by
- 450
- References
- 1
- FWCI
- 4.73
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Wells, W. W., Xu, D. P., Yang, Y. F., & Rocque, P. A. (1990). Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity. Journal of Biological Chemistry. https://doi.org/10.1016/s0021-9258(18)55401-6
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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