The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.
Metabolic Enzymes of Mycobacteria Linked to Antioxidant Defense by a Thioredoxin-Like Protein
Abstract
Mycobacterium tuberculosis (Mtb) mounts a stubborn defense against oxidative and nitrosative components of the immune response. Dihydrolipoamide dehydrogenase (Lpd) and dihydrolipoamide succinyltransferase (SucB) are components of α-ketoacid dehydrogenase complexes that are central to intermediary metabolism. We find that Lpd and SucB support Mtb's antioxidant defense. The peroxiredoxin alkyl hydroperoxide reductase (AhpC) is linked to Lpd and SucB by an adaptor protein, AhpD. The 2.0 angstrom AhpD crystal structure reveals a thioredoxin-like active site that is responsive to lipoamide. We propose that Lpd, SucB (the only lipoyl protein detected in Mtb), AhpD, and AhpC together constitute a nicotinamide adenine dinucleotide (reduced)–dependent peroxidase and peroxynitrite reductase. AhpD thus represents a class of thioredoxin-like molecules that enables an antioxidant defense.
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Cites
Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequence
Cole, S. T., Brosch, R., Parkhill, J., Garnier, T., Churcher, C., Harris, D., Gordon, S. V., Eiglmeier, K., Gas, S., Barry, C. E., et al. (1998) · Nature · doi:10.1038/31159 · Cited by 7,847
Protein Structure Comparison by Alignment of Distance Matrices
Holm, L., & Sander, C. (1993) · Journal of Molecular Biology · doi:10.1006/jmbi.1993.1489 · Cited by 3,984
Nathan, C., & Shiloh, M. U. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.16.8841 · Cited by 1,469
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Cited by
Nitric Oxide and Peroxynitrite in Health and Disease
Pacher, P., Beckman, J. S., & Liaudet, L. (2007) · Physiological Reviews · doi:10.1152/physrev.00029.2006 · Cited by 6,390
Structure, mechanism and regulation of peroxiredoxins
Wood, Z. A., Schröder, E., Robin Harris, J., & Poole, L. B. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(02)00003-8 · Cited by 2,544
The thioredoxin antioxidant system
Lu, J., & Holmgren, A. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2013.07.036 · Cited by 2,055
Oxidant signals and oxidative stress
Finkel, T. (2003) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(03)00002-4 · Cited by 1,393
Mycobacterial persistence requires the utilization of host cholesterol
Pandey, A. K., & Sassetti, C. M. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0711159105 · Cited by 1,064
Metadata
- Authors
- Bryk, R., Lima, C. D., Erdjument-Bromage, H., Tempst, P., & Nathan, C.
- Venue
- Science
- Published
- 2002-02-08
- Volume
- 295
- Issue
- 5557
- Pages
- 1073-1077
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1979955102
- Cited by
- 404
- References
- 3
- FWCI
- 7.56
- Type
- journal article
- Language
- en
- Open access
- closed
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- Bryk, R., Lima, C. D., Erdjument-Bromage, H., Tempst, P., & Nathan, C. (2002). Metabolic Enzymes of Mycobacteria Linked to Antioxidant Defense by a Thioredoxin-Like Protein. Science. https://doi.org/10.1126/science.1067798
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