Decaprenylphosphoryl arabinofuranose, the donor of the D-arabinofuranosyl residues of mycobacterial arabinan, is formed via a two-step epimerization of decaprenylphosphoryl ribose
- Author
- Katarína Mikušová, Hairong Huang, Tetsuya Yagi, Marcella Holsters (UGent) , Danny Vereecke (UGent) , Wim D'Haeze (UGent) , Michael S Scherman, Patrick J Brennan, Michael R McNeil and Dean C Crick
- Organization
- Abstract
- The major cell wall polysaccharide of mycobacteria is a branched-chain arabinogalactan in which arabinan chains are attached to the 5 carbon of some of the 6-linked galactofuranose residues; these arabinan chains are composed exclusively Of D-arabinofuranose (Araf) residues. The immediate precursor of the polymerized Araf is decaprenylphosphoryl-D-Araf, which is derived from 5-phosphoribose 1-diphosphate (pRpp) in an undefined manner. On the basis of time course, feedback, and chemical reduction experiment results we propose that decaprenylphosphoryl-Araf is synthesized by the following sequence of events. (i) pRpp is transferred to a decaprenyl-phosphate molecule to form decaprenylphosphoryi-beta-D-5-phosphoribose. (ii) Decaprenylphosphoryi-beta-D-5-phosphoribose is dephosphorylated to form decaprenylphosphoryl-beta-D-ribose. (iii) The hydroxyl group at the 2 position of the ribose is oxidized and is likely to form decaprenylphosphoryl-2-keto-beta-D-erythro-pentofuranose. (iv) Decaprenylphosphoryl-2-keto-beta-D-erythro-pentofuranose is reduced to form decaprenylphosphoryl-beta-D-Araf. Thus, the epimerization of the ribosyl to an arabinosyl residue occurs at the lipid-linked level; this is the first report of an epimerase that utilizes a lipid-linked sugar as a substrate. On the basis of similarity to proteins implicated in the arabinosylation of the Azorhizobium caulidans nodulation factor, two genes were cloned from the Mycobacterium tuberculosis genome and expressed in a heterologous host, and the protein was purified. Together, these proteins (Rv3790 and Rv3791) are able to catalyze the epimerization, although neither protein individually is sufficient to support the activity.
- Keywords
- GLUCOSE, SMEGMATIS, ENZYME, RMLC, ARABINOGALACTAN, TUBERCULOSIS, BIOSYNTHESIS, CELL-WALL, ESCHERICHIA-COLI
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Citation
Please use this url to cite or link to this publication: http://hdl.handle.net/1854/LU-331196
- MLA
- Mikušová, Katarína, et al. “Decaprenylphosphoryl Arabinofuranose, the Donor of the D-Arabinofuranosyl Residues of Mycobacterial Arabinan, Is Formed via a Two-Step Epimerization of Decaprenylphosphoryl Ribose.” JOURNAL OF BACTERIOLOGY, vol. 187, no. 23, 2005, pp. 8020–25, doi:10.1128/JB.187.23.8020-8025.2005.
- APA
- Mikušová, K., Huang, H., Yagi, T., Holsters, M., Vereecke, D., D’Haeze, W., … Crick, D. C. (2005). Decaprenylphosphoryl arabinofuranose, the donor of the D-arabinofuranosyl residues of mycobacterial arabinan, is formed via a two-step epimerization of decaprenylphosphoryl ribose. JOURNAL OF BACTERIOLOGY, 187(23), 8020–8025. https://doi.org/10.1128/JB.187.23.8020-8025.2005
- Chicago author-date
- Mikušová, Katarína, Hairong Huang, Tetsuya Yagi, Marcella Holsters, Danny Vereecke, Wim D’Haeze, Michael S Scherman, Patrick J Brennan, Michael R McNeil, and Dean C Crick. 2005. “Decaprenylphosphoryl Arabinofuranose, the Donor of the D-Arabinofuranosyl Residues of Mycobacterial Arabinan, Is Formed via a Two-Step Epimerization of Decaprenylphosphoryl Ribose.” JOURNAL OF BACTERIOLOGY 187 (23): 8020–25. https://doi.org/10.1128/JB.187.23.8020-8025.2005.
- Chicago author-date (all authors)
- Mikušová, Katarína, Hairong Huang, Tetsuya Yagi, Marcella Holsters, Danny Vereecke, Wim D’Haeze, Michael S Scherman, Patrick J Brennan, Michael R McNeil, and Dean C Crick. 2005. “Decaprenylphosphoryl Arabinofuranose, the Donor of the D-Arabinofuranosyl Residues of Mycobacterial Arabinan, Is Formed via a Two-Step Epimerization of Decaprenylphosphoryl Ribose.” JOURNAL OF BACTERIOLOGY 187 (23): 8020–8025. doi:10.1128/JB.187.23.8020-8025.2005.
- Vancouver
- 1.Mikušová K, Huang H, Yagi T, Holsters M, Vereecke D, D’Haeze W, et al. Decaprenylphosphoryl arabinofuranose, the donor of the D-arabinofuranosyl residues of mycobacterial arabinan, is formed via a two-step epimerization of decaprenylphosphoryl ribose. JOURNAL OF BACTERIOLOGY. 2005;187(23):8020–5.
- IEEE
- [1]K. Mikušová et al., “Decaprenylphosphoryl arabinofuranose, the donor of the D-arabinofuranosyl residues of mycobacterial arabinan, is formed via a two-step epimerization of decaprenylphosphoryl ribose,” JOURNAL OF BACTERIOLOGY, vol. 187, no. 23, pp. 8020–8025, 2005.
@article{331196, abstract = {{The major cell wall polysaccharide of mycobacteria is a branched-chain arabinogalactan in which arabinan chains are attached to the 5 carbon of some of the 6-linked galactofuranose residues; these arabinan chains are composed exclusively Of D-arabinofuranose (Araf) residues. The immediate precursor of the polymerized Araf is decaprenylphosphoryl-D-Araf, which is derived from 5-phosphoribose 1-diphosphate (pRpp) in an undefined manner. On the basis of time course, feedback, and chemical reduction experiment results we propose that decaprenylphosphoryl-Araf is synthesized by the following sequence of events. (i) pRpp is transferred to a decaprenyl-phosphate molecule to form decaprenylphosphoryi-beta-D-5-phosphoribose. (ii) Decaprenylphosphoryi-beta-D-5-phosphoribose is dephosphorylated to form decaprenylphosphoryl-beta-D-ribose. (iii) The hydroxyl group at the 2 position of the ribose is oxidized and is likely to form decaprenylphosphoryl-2-keto-beta-D-erythro-pentofuranose. (iv) Decaprenylphosphoryl-2-keto-beta-D-erythro-pentofuranose is reduced to form decaprenylphosphoryl-beta-D-Araf. Thus, the epimerization of the ribosyl to an arabinosyl residue occurs at the lipid-linked level; this is the first report of an epimerase that utilizes a lipid-linked sugar as a substrate. On the basis of similarity to proteins implicated in the arabinosylation of the Azorhizobium caulidans nodulation factor, two genes were cloned from the Mycobacterium tuberculosis genome and expressed in a heterologous host, and the protein was purified. Together, these proteins (Rv3790 and Rv3791) are able to catalyze the epimerization, although neither protein individually is sufficient to support the activity.}}, author = {{Mikušová, Katarína and Huang, Hairong and Yagi, Tetsuya and Holsters, Marcella and Vereecke, Danny and D'Haeze, Wim and Scherman, Michael S and Brennan, Patrick J and McNeil, Michael R and Crick, Dean C}}, issn = {{0021-9193}}, journal = {{JOURNAL OF BACTERIOLOGY}}, keywords = {{GLUCOSE,SMEGMATIS,ENZYME,RMLC,ARABINOGALACTAN,TUBERCULOSIS,BIOSYNTHESIS,CELL-WALL,ESCHERICHIA-COLI}}, language = {{eng}}, number = {{23}}, pages = {{8020--8025}}, title = {{Decaprenylphosphoryl arabinofuranose, the donor of the D-arabinofuranosyl residues of mycobacterial arabinan, is formed via a two-step epimerization of decaprenylphosphoryl ribose}}, url = {{http://doi.org/10.1128/JB.187.23.8020-8025.2005}}, volume = {{187}}, year = {{2005}}, }
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