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Decaprenylphosphoryl arabinofuranose, the donor of the D-arabinofuranosyl residues of mycobacterial arabinan, is formed via a two-step epimerization of decaprenylphosphoryl ribose

(2005) JOURNAL OF BACTERIOLOGY. 187(23). p.8020-8025
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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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Chicago
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.
APA
Mikušová, K., Huang, H., Yagi, T., Holsters, M., Vereecke, D., D’Haeze, W., Scherman, M. S., et al. (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.
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.
MLA
Mikušová, Katarína, Hairong Huang, Tetsuya Yagi, 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 187.23 (2005): 8020–8025. Print.
@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       = {Miku\v{s}ov{\'a}, Katar{\'i}na 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},
  keyword      = {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://dx.doi.org/10.1128/JB.187.23.8020-8025.2005},
  volume       = {187},
  year         = {2005},
}

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