Enzymes
| UniProtKB help_outline | 1,112 proteins |
Reaction participants Show >> << Hide
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Namehelp_outline
L-glutamyl-[protein]
Identifier
RHEA-COMP:10208
Reactive part
help_outline
- Name help_outline L-glutamate residue Identifier CHEBI:29973 Charge -1 Formula C5H6NO3 SMILEShelp_outline C(*)(=O)[C@@H](N*)CCC(=O)[O-] 2D coordinates Mol file for the small molecule Search links Involved in 11 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 1,142 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
5-O-(ADP-D-ribosyl)-L-glutamyl-[protein]
Identifier
RHEA-COMP:15089
Reactive part
help_outline
- Name help_outline 5-O-(ADP-D-ribosyl)-L-glutamate residue Identifier CHEBI:142540 Charge -2 Formula C20H26N6O16P2 SMILEShelp_outline O(C(=O)CC[C@H](N*)C(*)=O)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 (Beilstein: 383619; 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 60 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:58224 | RHEA:58225 | RHEA:58226 | RHEA:58227 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Family-wide analysis of poly(ADP-ribose) polymerase activity.
Vyas S., Matic I., Uchima L., Rood J., Zaja R., Hay R.T., Ahel I., Chang P.
The poly(adenosine diphosphate (ADP)-ribose) polymerase (PARP) protein family generates ADP-ribose (ADPr) modifications onto target proteins using NAD(+) as substrate. Based on the composition of three NAD(+) coordinating amino acids, the H-Y-E motif, each PARP is predicted to generate either poly ... >> More
The poly(adenosine diphosphate (ADP)-ribose) polymerase (PARP) protein family generates ADP-ribose (ADPr) modifications onto target proteins using NAD(+) as substrate. Based on the composition of three NAD(+) coordinating amino acids, the H-Y-E motif, each PARP is predicted to generate either poly(ADPr) (PAR) or mono(ADPr) (MAR). However, the reaction product of each PARP has not been clearly defined, and is an important priority since PAR and MAR function via distinct mechanisms. Here we show that the majority of PARPs generate MAR, not PAR, and demonstrate that the H-Y-E motif is not the sole indicator of PARP activity. We identify automodification sites on seven PARPs, and demonstrate that MAR and PAR generating PARPs modify similar amino acids, suggesting that the sequence and structural constraints limiting PARPs to MAR synthesis do not limit their ability to modify canonical amino-acid targets. In addition, we identify cysteine as a novel amino-acid target for ADP-ribosylation on PARPs. << Less
Nat. Commun. 5:4426-4426(2014) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.