Enzymes
| UniProtKB help_outline | 1 proteins |
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- Name help_outline guanine Identifier CHEBI:16235 (CAS: 73-40-5) help_outline Charge 0 Formula C5H5N5O InChIKeyhelp_outline UYTPUPDQBNUYGX-UHFFFAOYSA-N SMILEShelp_outline C12=C(N=C(NC1=O)N)NC=N2 2D coordinates Mol file for the small molecule Search links Involved in 16 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
- Name help_outline N2-(ADP-D-ribosyl)-guanine Identifier CHEBI:142716 Charge -2 Formula C20H24N10O14P2 InChIKeyhelp_outline REISTPJDYOQJMJ-MCTWQFKWSA-L SMILEShelp_outline C1=NC2=C(N1)N=C(NC2=O)NC3O[C@H](COP(OP(OC[C@H]4O[C@@H](N5C6=C(C(=NC=N6)N)N=C5)[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 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 (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
- 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 9,932 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:71903 | RHEA:71904 | RHEA:71905 | RHEA:71906 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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ADP-ribosylation of guanosine by SCO5461 protein secreted from Streptomyces coelicolor.
Nakano T., Matsushima-Hibiya Y., Yamamoto M., Takahashi-Nakaguchi A., Fukuda H., Ono M., Takamura-Enya T., Kinashi H., Totsuka Y.
The Streptomyces coelicolor A3(2) genome encodes a possible secretion protein, SCO5461, that shares a 30% homology with the activity domains of two toxic ADP-ribosyltransferases, pierisins and mosquitocidal toxin. We found ADP-ribosylating activity for the SCO5461 protein product through its co-in ... >> More
The Streptomyces coelicolor A3(2) genome encodes a possible secretion protein, SCO5461, that shares a 30% homology with the activity domains of two toxic ADP-ribosyltransferases, pierisins and mosquitocidal toxin. We found ADP-ribosylating activity for the SCO5461 protein product through its co-incubation with guanosine and NAD(+), which resulted in the formation of N(2)-(ADP-ribos-1-yl)-guanosine ((ar2)Guo), with a K(m) value of 110 μM. SCO5461 was further found to ADP-ribosylate deoxyguanosine, GMP, dGMP, GTP, dGTP, and cyclic GMP with k(cat) values of 150-370 s(-1). Oligo(dG), oligo(G), and yeast tRNA were also ADP-ribosylated by this protein, although with much lower k(cat) values of 0.2 s(-1) or less. SCO5461 showed maximum ADP-ribosylation activity towards guanosine at 30 °C, and maintained 20% of these maximum activity levels even at 0 °C. This is the first report of the ADP-ribosylation of guanosine and guanine mononucleotides among the family members of various ADP-ribosylating enzymes. We additionally observed secretion of the putative gene product, SCO5461, in liquid cultures of S. coelicolor. We thus designated the SCO5461 protein product as S. coelicolor ADP-ribosylating protein, ScARP. Our current results could offer new insights into not only the ADP-ribosylation of small molecules but also signal transduction events via enzymatic nucleoside modification by toxin-related enzymes. << Less
Toxicon 63:55-63(2013) [PubMed] [EuropePMC]
This publication is cited by 8 other entries.