Enzymes
| UniProtKB help_outline | 4,040 proteins |
| GO Molecular Function help_outline |
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Reaction participants Show >> << Hide
- Name help_outline dTDP-β-L-rhamnose Identifier CHEBI:57510 (Beilstein: 4078636) help_outline Charge -2 Formula C16H24N2O15P2 InChIKeyhelp_outline ZOSQFDVXNQFKBY-CGAXJHMRSA-L SMILEShelp_outline C[C@@H]1O[C@H](OP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H](C[C@@H]2O)n2cc(C)c(=O)[nH]c2=O)[C@H](O)[C@H](O)[C@H]1O 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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Namehelp_outline
L-arginyl-[protein]
Identifier
RHEA-COMP:10532
Reactive part
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- Name help_outline L-arginine residue Identifier CHEBI:29965 Charge 1 Formula C6H13N4O SMILEShelp_outline O=C(*)[C@@H](N*)CCCNC(=[NH2+])N 2D coordinates Mol file for the small molecule Search links Involved in 29 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline dTDP Identifier CHEBI:58369 Charge -3 Formula C10H13N2O11P2 InChIKeyhelp_outline UJLXYODCHAELLY-XLPZGREQSA-K SMILEShelp_outline Cc1cn([C@H]2C[C@H](O)[C@@H](COP([O-])(=O)OP([O-])([O-])=O)O2)c(=O)[nH]c1=O 2D coordinates Mol file for the small molecule Search links Involved in 31 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 9,176 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
Nω-(α-L-rhamnosyl)-L-arginyl-[protein]
Identifier
RHEA-COMP:17096
Reactive part
help_outline
- Name help_outline Nω-(α-L-rhamnosyl)-L-arginyl residue Identifier CHEBI:167445 Charge 1 Formula C12H23N4O5 SMILEShelp_outline O=C(*)[C@@H](N*)CCCNC(=[NH2+])N[C@@H]1O[C@H]([C@@H]([C@H]([C@H]1O)O)O)C 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:66692 | RHEA:66693 | RHEA:66694 | RHEA:66695 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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| Gene Ontology help_outline |
Publications
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Arginine-rhamnosylation as new strategy to activate translation elongation factor P.
Lassak J., Keilhauer E.C., Fuerst M., Wuichet K., Goedeke J., Starosta A.L., Chen J.M., Soegaard-Andersen L., Rohr J., Wilson D.N., Haeussler S., Mann M., Jung K.
Ribosome stalling at polyproline stretches is common and fundamental. In bacteria, translation elongation factor P (EF-P) rescues such stalled ribosomes, but only when it is post-translationally activated. In Escherichia coli, activation of EF-P is achieved by (R)-β-lysinylation and hydroxylation ... >> More
Ribosome stalling at polyproline stretches is common and fundamental. In bacteria, translation elongation factor P (EF-P) rescues such stalled ribosomes, but only when it is post-translationally activated. In Escherichia coli, activation of EF-P is achieved by (R)-β-lysinylation and hydroxylation of a conserved lysine. Here we have unveiled a markedly different modification strategy in which a conserved arginine of EF-P is rhamnosylated by a glycosyltransferase (EarP) using dTDP-L-rhamnose as a substrate. This is to our knowledge the first report of N-linked protein glycosylation on arginine in bacteria and the first example in which a glycosylated side chain of a translation elongation factor is essential for function. Arginine-rhamnosylation of EF-P also occurs in clinically relevant bacteria such as Pseudomonas aeruginosa. We demonstrate that the modification is needed to develop pathogenicity, making EarP and dTDP-L-rhamnose-biosynthesizing enzymes ideal targets for antibiotic development. << Less