The reaction is catalysed in the reverse direction. The enzyme, isolated from the bacterium Mycobacterium smegmatis, is involved, along with EC 1.1.98.3, decaprenylphospho-β-D-ribofuranose 2-oxidase, in the epimerization of trans,octacis-decaprenylphospho-β-D-ribofuranose to trans,octacis-decaprenylphospho-β-D-arabinoofuranose, the arabinosyl donor for the biosynthesis of mycobacterial cell wall arabinan polymers.
The enzyme appears in viruses and cellular organisms
The reaction is catalysed in the reverse direction. The enzyme, isolated from the bacterium Mycobacterium smegmatis, is involved, along with EC 1.1.98.3, decaprenylphospho-beta-D-ribofuranose 2-oxidase, in the epimerization of trans,octacis-decaprenylphospho-beta-D-ribofuranose to trans,octacis-decaprenylphospho-beta-D-arabinoofuranose, the arabinosyl donor for the biosynthesis of mycobacterial cell wall arabinan polymers.
Substrates: decaprenylphospho-beta-D-ribofuranose 2-oxidase DprE1 and decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase DprE2 together catalyze the epimerization of decaprenylphosphoryl-beta-D-ribofuranose to decaprenylphosphoryl-beta-D-arabinofuranose. Neither protein individually is sufficient to support the activity Products: -
Substrates: decaprenylphospho-beta-D-ribofuranose 2-oxidase DprE1 and decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase DprE2 together catalyze the epimerization of decaprenylphosphoryl-beta-D-ribofuranose to decaprenylphosphoryl-beta-D-arabinofuranose. Neither protein individually is sufficient to support the activity Products: -
Substrates: decaprenylphosphoryl-beta-D-ribofuranose 2'-epimerase is constituted of decaprenylphospho-beta-D-ribofuranose 2-oxidase DprE1 and decaprenylphospho-beta-D-erythro-pentofuranosid-2-ulose 2-reductase DprE2 that together catalyze the epimerization of decaprenylphosphoryl-beta-D-ribofuranose to decaprenylphosphoryl-beta-D-arabinofuranose Products: -
more than a ten-fold decrease in the number of colony-forming units is observed with both human and mouse primary cells at a N-(2-(4-methoxyphenoxy)ethyl)-3,5-dinitrobenzamide concentrations above 5 microM, compound is also highly active against multidrug-resistant and extensively drug-resistant clinical isolates. N-(2-(4-methoxyphenoxy)ethyl)-3,5-dinitrobenzamide shows a clear-cut effect on the synthesis of the arabinan domains of arabinogalactan and lipoarabinomannan, and inhibition of decaprenyl-phospho-arabinose formation in the treated extracts concurrent with the accumulation of decaprenylphospho-ribose. Target of the inhibitors is probably the heteromeric decaprenylphospho-ribose 29 epimerase encoded by the dprE1/dprE2 genes
more than a ten-fold decrease in the number of colony-forming units is observed with both human and mouse primary cells at a N-(2-(benzyloxy)ethyl)-3,5-dinitrobenzamide concentrations above 5 microM, compound is also highly active against multidrug-resistant and extensively drug-resistant clinical isolates. N-(2-(benzyloxy)ethyl)-3,5-dinitrobenzamide shows a clear-cut effect on the synthesis of the arabinan domains of arabinogalactan and lipoarabinomannan, and inhibition of decaprenyl-phospho-arabinose formation in the treated extracts concurrent with the accumulation of decaprenylphospho-ribose. Target of the inhibitors is probably the heteromeric decaprenylphospho-ribose 29 epimerase encoded by the dprE1/dprE2 genes
Structure, dynamics, and interaction of Mycobacterium tuberculosis (Mtb) DprE1 and DprE2 examined by molecular modeling, simulation, and electrostatic studies.
decaprenylphosphoryl-beta-D-ribofuranose 2'-epimerase is constituted of DprE1 and DprE2 that together catalyze the epimerization of decaprenylphosphoryl-beta-D-ribofuranose to decaprenylphosphoryl-beta-D-arabinofuranose
decaprenylphosphoryl-D-arabinofuranose is synthesized by the following sequence of events: 5-phosphoribose 1-diphosphate is transferred to a decaprenyl-phosphate molecule to form decaprenylphosphoryl-beta-D-5-phosphoribose. Decaprenylphosphoryl-beta-D-5-phosphoribose is dephosphorylated to form decaprenylphosphoryl-beta-D-ribose. The hydroxyl group at the 2 position of the ribose is oxidized and is likely to form decaprenylphosphoryl-2-keto-beta-D-erythro-pentofuranose. Decaprenylphosphoryl-2-keto-beta-D-erythro-pentofuranose is reduced to form decaprenylphosphoryl-beta-D-arabinofuranose. Thus, the epimerization of the ribosyl to an arabinosyl residue occurs at the lipid-linked level
decaprenylphosphoryl-D-arabinofuranose is synthesized by the following sequence of events: 5-phosphoribose 1-diphosphate is transferred to a decaprenyl-phosphate molecule to form decaprenylphosphoryl-beta-D-5-phosphoribose. Decaprenylphosphoryl-beta-D-5-phosphoribose is dephosphorylated to form decaprenylphosphoryl-beta-D-ribose. The hydroxyl group at the 2 position of the ribose is oxidized and is likely to form decaprenylphosphoryl-2-keto-beta-D-erythro-pentofuranose. Decaprenylphosphoryl-2-keto-beta-D-erythro-pentofuranose is reduced to form decaprenylphosphoryl-beta-D-arabinofuranose. Thus, the epimerization of the ribosyl to an arabinosyl residue occurs at the lipid-linked level
developed of an assay method based on the visualization of mycobacterium replication within host cells and application for the search of compounds that are able to chase the pathogen from its hideout
developed of an assay method based on the visualization of mycobacterium replication within host cells and application for the search of compounds that are able to chase the pathogen from its hideout
Decaprenylphosphoryl arabinofuranose, the donor of the D-arabinofuranosyl residues of mycobacterial arabinan, is formed via a two-step epimerization of decaprenylphosphoryl ribose
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