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Namehelp_outline
S-(ADP-D-ribosyl)-L-cysteinyl-[protein]
Identifier
RHEA-COMP:14624
Reactive part
help_outline
- Name help_outline S-(ADP-D-ribosyl)-L-cysteine residue Identifier CHEBI:140607 Charge -2 Formula C18H24N6O14P2S SMILEShelp_outline N1(C2=C(C(=NC=N2)N)N=C1)[C@@H]3O[C@H](COP(OP(OC[C@H]4OC(SC[C@H](N*)C(=O)*)[C@@H]([C@@H]4O)O)(=O)[O-])(=O)[O-])[C@H]([C@H]3O)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 H2O Identifier CHEBI:15377 (CAS: 7732-18-5) help_outline Charge 0 Formula H2O InChIKeyhelp_outline XLYOFNOQVPJJNP-UHFFFAOYSA-N SMILEShelp_outline [H]O[H] 2D coordinates Mol file for the small molecule Search links Involved in 6,648 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline ADP-D-ribose Identifier CHEBI:57967 Charge -2 Formula C15H21N5O14P2 InChIKeyhelp_outline SRNWOUGRCWSEMX-TYASJMOZSA-L SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OC[C@H]2OC(O)[C@H](O)[C@@H]2O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 24 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
L-cysteinyl-[protein]
Identifier
RHEA-COMP:10131
Reactive part
help_outline
- Name help_outline L-cysteine residue Identifier CHEBI:29950 Charge 0 Formula C3H5NOS SMILEShelp_outline C(=O)(*)[C@@H](N*)CS 2D coordinates Mol file for the small molecule Search links Involved in 132 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:58240 | RHEA:58241 | RHEA:58242 | RHEA:58243 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Identification of ADP-ribosylation site in human glutamate dehydrogenase isozymes.
Choi M.M., Huh J.W., Yang S.J., Cho E.H., Choi S.Y., Cho S.W.
When the influence of ADP-ribosylation on the activities of the purified human glutamate dehydrogenase isozymes (hGDH1 and hGDH2) was measured in the presence of 100 microM NAD+ for 60 min, hGDH isozymes were inhibited by up to 75%. If incubations were performed for longer time periods up to 3 h, ... >> More
When the influence of ADP-ribosylation on the activities of the purified human glutamate dehydrogenase isozymes (hGDH1 and hGDH2) was measured in the presence of 100 microM NAD+ for 60 min, hGDH isozymes were inhibited by up to 75%. If incubations were performed for longer time periods up to 3 h, the inhibition of hGDH isozymes did not increased further. This phenomenon may be related to the reversibility of ADP-ribosylation in mitochondria. ADP-ribosylated hDGH isozymes were reactivated by Mg2+-dependent mitochondrial ADP-ribosylcysteine hydrolase. The stoichiometry between incorporated ADP-ribose and GDH subunits shows a modification of one subunit per catalytically active homohexamer. Since ADP and GTP had no effects on the extent of modification, it would appear that the ADP-ribosylation is unlikely to occur in allosteric sites. It has been proposed that Cys residue may be involved in the ADP-ribosylation of GDH, although identification of the reactive Cys residue has not been reported. To identify the reactive Cys residue involved in the ADP-ribosylation, we performed cassette mutagenesis at three different positions (Cys59, Cys119, and Cys274) using synthetic genes of hGDH isozymes. Among the Cys residues tested, only Cys119 mutants showed a significant reduction in the ADP-ribosylation. These results suggest a possibility that the Cys119 residue has an important role in the regulation of hGDH isozymes by ADP-ribosylation. << Less
FEBS Lett. 579:4125-4130(2005) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.