The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Three pathways for trehalose biosynthesis in mycobacteria
Abstract
Trehalose is present as a free disaccharide in the cytoplasm of mycobacteria and as a component of cell-wall glycolipids implicated in tissue damage associated with mycobacterial infection. To obtain an overview of trehalose metabolism, we analysed data from the Mycobacterium tuberculosis genome project and identified ORFs with homology to genes encoding enzymes from three trehalose biosynthesis pathways previously characterized in other bacteria. Functional assays using mycobacterial extracts and recombinant enzymes derived from these ORFs demonstrated that mycobacteria can produce trehalose from glucose 6-phosphate and UDP-glucose (the OtsA-OtsB pathway) from glycogen-like alpha(1-->4)-linked glucose polymers (the TreY-TreZ pathway) and from maltose (the TreS pathway). Each of the pathways was found to be active in both rapid-growing Mycobacterium smegmatis and slow-growing Mycobacterium bovis BCG. The presence of a disrupted treZ gene in Mycobacterium leprae suggests that this pathway is not functional in this organism. The presence of multiple biosynthetic pathways indicates that trehalose plays an important role in mycobacterial physiology.
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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
Detecting Protein Function and Protein-Protein Interactions from Genome Sequences
Marcotte, E. M., Pellegrini, M., Ng, H.-L., Rice, D. W., Yeates, T. O., & Eisenberg, D. (1999) · Science · doi:10.1126/science.285.5428.751 · Cited by 1,670
Cited by
Structure of mycobacterial maltokinase, the missing link in the essential GlgE-pathway
Fraga, J., Maranha, A., Mendes, V., Pereira, P. J. B., Empadinhas, N., & Macedo-Ribeiro, S. (2015) · Scientific Reports · doi:10.1038/srep08026 · Cited by 819
Burroughs, A. M., Allen, K. N., Dunaway-Mariano, D., & Aravind, L. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.06.049 · Cited by 438
The Trehalose Myth Revisited: Introduction to a Symposium on Stabilization of Cells in the Dry State
Crowe, J. H., Crowe, L. M., Oliver, A. E., Tsvetkova, N., Wolkers, W., & Tablin, F. (2001) · Cryobiology · doi:10.1006/cryo.2001.2353 · Cited by 428
Abiotic Stress - Plant Responses and Applications in Agriculture
(2013) · InTech eBooks · doi:10.5772/45842 · Cited by 381
The revisited genome of Pseudomonas putida KT2440 enlightens its value as a robust metabolic chassis
Belda, E., van Heck, R. G. A., José Lopez‐Sanchez, M., Cruveiller, S., Barbe, V., Fraser, C., Klenk, H., Petersen, J., Morgat, A., Nikel, P. I., et al. (2016) · Environmental Microbiology · doi:10.1111/1462-2920.13230 · Cited by 338
Metadata
- Authors
- De Smet, K. A. L., Weston, A., Brown, I. N., Young, D. B., & Robertson, B. D.
- Venue
- Microbiology
- Publisher
- Microbiology Society
- Published
- 2000-01-01
- Volume
- 146
- Issue
- 1
- Pages
- 199-208
- ISSN
- 1350-0872 (ISSN-L)
- 1465-2080
- OpenAlex
- W1642015145
- Cited by
- 265
- References
- 2
- FWCI
- 3.62
- Type
- journal article
- Language
- en
- Open access
- closed
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- De Smet, K. A. L., Weston, A., Brown, I. N., Young, D. B., & Robertson, B. D. (2000). Three pathways for trehalose biosynthesis in mycobacteria. Microbiology. https://doi.org/10.1099/00221287-146-1-199
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