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- Name help_outline ADP-α-D-glucose Identifier CHEBI:57498 Charge -2 Formula C16H23N5O15P2 InChIKeyhelp_outline WFPZSXYXPSUOPY-ROYWQJLOSA-L SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)O[C@H]2O[C@H](CO)[C@@H](O)[C@H](O)[C@H]2O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 10 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline α-D-glucose 1-phosphate Identifier CHEBI:58601 Charge -2 Formula C6H11O9P InChIKeyhelp_outline HXXFSFRBOHSIMQ-VFUOTHLCSA-L SMILEShelp_outline OC[C@H]1O[C@H](OP([O-])([O-])=O)[C@H](O)[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 41 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline α-maltose 1-phosphate Identifier CHEBI:63576 Charge -2 Formula C12H21O14P InChIKeyhelp_outline VRKQBSISJQUWFI-QUYVBRFLSA-L SMILEShelp_outline OC[C@H]1O[C@H](O[C@H]2[C@H](O)[C@@H](O)[C@H](O[C@@H]2CO)OP([O-])([O-])=O)[C@H](O)[C@@H](O)[C@@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 3 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline ADP Identifier CHEBI:456216 (Beilstein: 3783669) help_outline Charge -3 Formula C10H12N5O10P2 InChIKeyhelp_outline XTWYTFMLZFPYCI-KQYNXXCUSA-K SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 841 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline H+ Identifier CHEBI:15378 Charge 1 Formula H InChIKeyhelp_outline GPRLSGONYQIRFK-UHFFFAOYSA-N SMILEShelp_outline [H+] 2D coordinates Mol file for the small molecule Search links Involved in 9,521 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:50692 | RHEA:50693 | RHEA:50694 | RHEA:50695 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Metabolic network for the biosynthesis of intra- and extracellular alpha-glucans required for virulence of Mycobacterium tuberculosis.
Koliwer-Brandl H., Syson K., van de Weerd R., Chandra G., Appelmelk B., Alber M., Ioerger T.R., Jacobs W.R. Jr., Geurtsen J., Bornemann S., Kalscheuer R.
Mycobacterium tuberculosis synthesizes intra- and extracellular α-glucans that were believed to originate from separate pathways. The extracellular glucose polymer is the main constituent of the mycobacterial capsule that is thought to be involved in immune evasion and virulence. However, the role ... >> More
Mycobacterium tuberculosis synthesizes intra- and extracellular α-glucans that were believed to originate from separate pathways. The extracellular glucose polymer is the main constituent of the mycobacterial capsule that is thought to be involved in immune evasion and virulence. However, the role of the α-glucan capsule in pathogenesis has remained enigmatic due to an incomplete understanding of α-glucan biosynthetic pathways preventing the generation of capsule-deficient mutants. Three separate and potentially redundant pathways had been implicated in α-glucan biosynthesis in mycobacteria: the GlgC-GlgA, the Rv3032 and the TreS-Pep2-GlgE pathways. We now show that α-glucan in mycobacteria is exclusively assembled intracellularly utilizing the building block α-maltose-1-phosphate as the substrate for the maltosyltransferase GlgE, with subsequent branching of the polymer by the branching enzyme GlgB. Some α-glucan is exported to form the α-glucan capsule. There is an unexpected convergence of the TreS-Pep2 and GlgC-GlgA pathways that both generate α-maltose-1-phosphate. While the TreS-Pep2 route from trehalose was already known, we have now established that GlgA forms this phosphosugar from ADP-glucose and glucose 1-phosphate 1000-fold more efficiently than its hitherto described glycogen synthase activity. The two routes are connected by the common precursor ADP-glucose, allowing compensatory flux from one route to the other. Having elucidated this unexpected configuration of the metabolic pathways underlying α-glucan biosynthesis in mycobacteria, an M. tuberculosis double mutant devoid of α-glucan could be constructed, showing a direct link between the GlgE pathway, α-glucan biosynthesis and virulence in a mouse infection model. << Less
PLoS Pathog. 12:E1005768-E1005768(2016) [PubMed] [EuropePMC]
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Study of two glycosyltransferases related to polysaccharide biosynthesis in <i>Rhodococcus jostii</i> RHA1.
Cereijo A.E., Ferretti M.V., Iglesias A.A., Alvarez H.M., Asencion Diez M.D.
The bacterial genus <i>Rhodococcus</i> comprises organisms performing oleaginous behaviors under certain growth conditions and ratios of carbon and nitrogen availability. <i>Rhodococci</i> are outstanding producers of biofuel precursors, where lipid and glycogen metabolisms are closely related. Th ... >> More
The bacterial genus <i>Rhodococcus</i> comprises organisms performing oleaginous behaviors under certain growth conditions and ratios of carbon and nitrogen availability. <i>Rhodococci</i> are outstanding producers of biofuel precursors, where lipid and glycogen metabolisms are closely related. Thus, a better understanding of rhodococcal carbon partitioning requires identifying catalytic steps redirecting sugar moieties to storage molecules. Here, we analyzed two GT4 glycosyl-transferases from <i>Rhodococcus jostii</i> (<i>Rjo</i>GlgAb and <i>Rjo</i>GlgAc) annotated as α-glucan-α-1,4-glucosyl transferases, putatively involved in glycogen synthesis. Both enzymes were produced in <i>Escherichia coli</i> cells, purified to homogeneity, and kinetically characterized. <i>Rjo</i>GlgAb and <i>Rjo</i>GlgAc presented the "canonical" glycogen synthase activity and were actives as maltose-1P synthases, although to a different extent. Then, <i>Rjo</i>GlgAc is a homologous enzyme to the mycobacterial GlgM, with similar kinetic behavior and glucosyl-donor preference. <i>Rjo</i>GlgAc was two orders of magnitude more efficient to glucosylate glucose-1P than glycogen, also using glucosamine-1P as a catalytically efficient aglycon. Instead, <i>Rjo</i>GlgAb exhibited both activities with similar kinetic efficiency and preference for short-branched α-1,4-glucans. Curiously, <i>Rjo</i>GlgAb presented a super-oligomeric conformation (higher than 15 subunits), representing a novel enzyme with a unique structure-to-function relationship. Kinetic results presented herein constitute a hint to infer on polysaccharides biosynthesis in <i>rhodococci</i> from an enzymological point of view. << Less
Biol Chem 405:325-340(2024) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.