Enzymes
| UniProtKB help_outline | 1 proteins |
| Enzyme class help_outline |
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- Name help_outline 4-O-[1-D-ribitylphospho-(2R)-1-glycerylphospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate Identifier CHEBI:133892 Charge -4 Formula C79H132N2O29P4 InChIKeyhelp_outline KFPAGFLTIOIHLD-WDHAKQNGSA-J SMILEShelp_outline O(P(OP(O[C@H]1O[C@@H]([C@H]([C@@H]([C@H]1NC(=O)C)O)O[C@@H]2O[C@@H]([C@H]([C@@H]([C@H]2NC(=O)C)O)OP(OC[C@@H](COP(OC[C@H]([C@H]([C@H](CO)O)O)O)([O-])=O)O)([O-])=O)CO)CO)([O-])=O)([O-])=O)C/C=C(/C)\CC/C=C(/C)\CC/C=C(\CC/C=C(\CC/C=C(\CC/C=C(\CC/C=C(\CC/C=C(\CC/C=C(/CC/C=C(/CCC=C(C)C)\C)\C)/C)/C)/C)/C)/C)/C 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline CDP-L-ribitol Identifier CHEBI:57608 Charge -2 Formula C14H23N3O15P2 InChIKeyhelp_outline DPJKHFICSGCNIR-HRENORGGSA-L SMILEShelp_outline C=1N(C(N=C(C1)N)=O)[C@@H]2O[C@@H]([C@H]([C@H]2O)O)COP(OP(OC[C@H]([C@H]([C@H](CO)O)O)O)(=O)[O-])(=O)[O-] 2D coordinates Mol file for the small molecule Search links Involved in 7 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Name help_outline
4-O-[poly(D-ribitylphospho)-D-ribitylphospho-(2R)-glycerylphospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphate
Identifier
CHEBI:133894
Charge
-5
Formula
(C5H10O7P)n.C79H132N2O29P4
Search links
Involved in 2 reaction(s)
Find proteins in UniProtKB for this molecule
Form(s) in this reaction:
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Identifier: RHEA-COMP:12833Polymer name: 4-O-[(D-ribitylphospho)(n)-D-ribitylphospho-(2R)-glycerylphospho]-N-acetyl-β-D-mannosaminyl-(1→4)-N-acetyl-α-D-glucosaminyl di-trans,octa-cis-undecaprenyl diphosphatePolymerization index help_outline nFormula C79H132N2O29P4(C5H10O7P)nCharge (-4)(-1)nMol File for the polymer
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- Name help_outline CMP Identifier CHEBI:60377 Charge -2 Formula C9H12N3O8P InChIKeyhelp_outline IERHLVCPSMICTF-XVFCMESISA-L SMILEShelp_outline Nc1ccn([C@@H]2O[C@H](COP([O-])([O-])=O)[C@@H](O)[C@H]2O)c(=O)n1 2D coordinates Mol file for the small molecule Search links Involved in 164 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 9,431 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:44668 | RHEA:44669 | RHEA:44670 | RHEA:44671 | |
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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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Staphylococcus aureus and Bacillus subtilis W23 make polyribitol wall teichoic acids using different enzymatic pathways.
Brown S., Meredith T., Swoboda J., Walker S.
Wall teichoic acids (WTAs) are anionic polymers that play key roles in bacterial cell shape, cell division, envelope integrity, biofilm formation, and pathogenesis. B. subtilis W23 and S. aureus both make polyribitol-phosphate (RboP) WTAs and contain similar sets of biosynthetic genes. We use in v ... >> More
Wall teichoic acids (WTAs) are anionic polymers that play key roles in bacterial cell shape, cell division, envelope integrity, biofilm formation, and pathogenesis. B. subtilis W23 and S. aureus both make polyribitol-phosphate (RboP) WTAs and contain similar sets of biosynthetic genes. We use in vitro reconstitution combined with genetics to show that the pathways for WTA biosynthesis in B. subtilis W23 and S. aureus are different. S. aureus requires a glycerol-phosphate primase called TarF in order to make RboP-WTAs; B. subtilis W23 contains a TarF homolog, but this enzyme makes glycerol-phosphate polymers and is not involved in RboP-WTA synthesis. Instead, B. subtilis TarK functions in place of TarF to prime the WTA intermediate for chain extension by TarL. This work highlights the enzymatic diversity of the poorly characterized family of phosphotransferases involved in WTA biosynthesis in Gram-positive organisms. << Less
Chem. Biol. 17:1101-1110(2010) [PubMed] [EuropePMC]
This publication is cited by 4 other entries.