Enzymes
| UniProtKB help_outline | 1 proteins |
Reaction participants Show >> << Hide
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Namehelp_outline
[protein]-C-terminal glycine
Identifier
RHEA-COMP:15093
Reactive part
help_outline
- Name help_outline C-terminal glycine residue Identifier CHEBI:83148 Charge -1 Formula C2H3NO2 SMILEShelp_outline [O-]C(=O)CN-* 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 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
[protein]-C-terminal O-(ADP-D-ribosyl)-glycine
Identifier
RHEA-COMP:15095
Reactive part
help_outline
- Name help_outline C-terminal O-(ADP-D-ribosyl)-glycine residue Identifier CHEBI:142558 Charge -2 Formula C17H23N6O15P2 SMILEShelp_outline O(C(=O)CN*)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 1 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:58268 | RHEA:58269 | RHEA:58270 | RHEA:58271 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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| Gene Ontology help_outline |
Publications
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Ubiquitin Modification by the E3 Ligase/ADP-Ribosyltransferase Dtx3L/Parp9.
Yang C.S., Jividen K., Spencer A., Dworak N., Ni L., Oostdyk L.T., Chatterjee M., Kusmider B., Reon B., Parlak M., Gorbunova V., Abbas T., Jeffery E., Sherman N.E., Paschal B.M.
ADP-ribosylation of proteins is emerging as an important regulatory mechanism. Depending on the family member, ADP-ribosyltransferases either conjugate a single ADP-ribose to a target or generate ADP-ribose chains. Here we characterize Parp9, a mono-ADP-ribosyltransferase reported to be enzymatica ... >> More
ADP-ribosylation of proteins is emerging as an important regulatory mechanism. Depending on the family member, ADP-ribosyltransferases either conjugate a single ADP-ribose to a target or generate ADP-ribose chains. Here we characterize Parp9, a mono-ADP-ribosyltransferase reported to be enzymatically inactive. Parp9 undergoes heterodimerization with Dtx3L, a histone E3 ligase involved in DNA damage repair. We show that the Dtx3L/Parp9 heterodimer mediates NAD<sup>+</sup>-dependent mono-ADP-ribosylation of ubiquitin, exclusively in the context of ubiquitin processing by E1 and E2 enzymes. Dtx3L/Parp9 ADP-ribosylates the carboxyl group of Ub Gly76. Because Gly76 is normally used for Ub conjugation to substrates, ADP-ribosylation of the Ub carboxyl terminus precludes ubiquitylation. Parp9 ADP-ribosylation activity therefore restrains the E3 function of Dtx3L. Mutation of the NAD<sup>+</sup> binding site in Parp9 increases the DNA repair activity of the heterodimer. Moreover, poly(ADP-ribose) binding to the Parp9 macrodomains increases E3 activity. Dtx3L heterodimerization with Parp9 enables NAD<sup>+</sup> and poly(ADP-ribose) regulation of E3 activity. << Less