Enzymes
| UniProtKB help_outline | 5,019 proteins |
| GO Molecular Function help_outline |
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Reaction participants Show >> << Hide
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Namehelp_outline
L-aspartyl-[protein]
Identifier
RHEA-COMP:9867
Reactive part
help_outline
- Name help_outline L-aspartate residue Identifier CHEBI:29961 Charge -1 Formula C4H4NO3 SMILEShelp_outline C(*)(=O)[C@@H](N*)CC([O-])=O 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 NAD+ Identifier CHEBI:57540 (Beilstein: 3868403) help_outline Charge -1 Formula C21H26N7O14P2 InChIKeyhelp_outline BAWFJGJZGIEFAR-NNYOXOHSSA-M SMILEShelp_outline NC(=O)c1ccc[n+](c1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2O[C@H]([C@H](O)[C@@H]2O)n2cnc3c(N)ncnc23)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 1,207 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
4-O-(ADP-D-ribosyl)-L-aspartyl-[protein]
Identifier
RHEA-COMP:13832
Reactive part
help_outline
- Name help_outline 4-O-(ADP-D-ribosyl)-L-aspartyl residue Identifier CHEBI:138102 Charge -2 Formula C19H24N6O16P2 SMILEShelp_outline O(C(=O)C[C@@H](C(*)=O)N*)C1O[C@H](COP(OP(=O)(OC[C@H]2O[C@H]([C@@H]([C@@H]2O)O)N3C=NC4=C3N=CN=C4N)[O-])(=O)[O-])[C@H]([C@H]1O)O 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 nicotinamide Identifier CHEBI:17154 (CAS: 98-92-0) help_outline Charge 0 Formula C6H6N2O InChIKeyhelp_outline DFPAKSUCGFBDDF-UHFFFAOYSA-N SMILEShelp_outline NC(=O)c1cccnc1 2D coordinates Mol file for the small molecule Search links Involved in 61 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:54424 | RHEA:54425 | RHEA:54426 | RHEA:54427 | |
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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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Identification of a class of protein ADP-ribosylating sirtuins in microbial pathogens.
Rack J.G., Morra R., Barkauskaite E., Kraehenbuehl R., Ariza A., Qu Y., Ortmayer M., Leidecker O., Cameron D.R., Matic I., Peleg A.Y., Leys D., Traven A., Ahel I.
Sirtuins are an ancient family of NAD(+)-dependent deacylases connected with the regulation of fundamental cellular processes including metabolic homeostasis and genome integrity. We show the existence of a hitherto unrecognized class of sirtuins, found predominantly in microbial pathogens. In con ... >> More
Sirtuins are an ancient family of NAD(+)-dependent deacylases connected with the regulation of fundamental cellular processes including metabolic homeostasis and genome integrity. We show the existence of a hitherto unrecognized class of sirtuins, found predominantly in microbial pathogens. In contrast to earlier described classes, these sirtuins exhibit robust protein ADP-ribosylation activity. In our model organisms, Staphylococcus aureus and Streptococcus pyogenes, the activity is dependent on prior lipoylation of the target protein and can be reversed by a sirtuin-associated macrodomain protein. Together, our data describe a sirtuin-dependent reversible protein ADP-ribosylation system and establish a crosstalk between lipoylation and mono-ADP-ribosylation. We propose that these posttranslational modifications modulate microbial virulence by regulating the response to host-derived reactive oxygen species. << Less
Mol. Cell 59:309-320(2015) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.