Enzymes
| UniProtKB help_outline | 1,034 proteins |
Reaction participants Show >> << Hide
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Namehelp_outline
an N2-(1-hydroxy-2-oxoethyl)-guanosine in RNA
Identifier
RHEA-COMP:14859
Reactive part
help_outline
- Name help_outline N2-(1-hydroxy-2-oxoethyl)-GMP residue Identifier CHEBI:141581 Charge -1 Formula C12H13N5O9P SMILEShelp_outline C1(=O)NC(=NC2=C1N=CN2[C@@H]3O[C@H](COP(=O)(*)[O-])[C@@H](O*)[C@H]3O)NC(C([H])=O)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 (Beilstein: 3587155; 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 6,048 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
a guanosine in RNA
Identifier
RHEA-COMP:14855
Reactive part
help_outline
- Name help_outline GMP residue Identifier CHEBI:74269 Charge -1 Formula C10H11N5O7P SMILEShelp_outline C1(=O)NC(=NC2=C1N=CN2[C@@H]3O[C@H](COP(=O)(*)[O-])[C@@H](O*)[C@H]3O)N 2D coordinates Mol file for the small molecule Search links Involved in 42 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline glycolate Identifier CHEBI:29805 (CAS: 666-14-8) help_outline Charge -1 Formula C2H3O3 InChIKeyhelp_outline AEMRFAOFKBGASW-UHFFFAOYSA-M SMILEShelp_outline OCC([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 23 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 9,176 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:57292 | RHEA:57293 | RHEA:57294 | RHEA:57295 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Publications
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Metabolite damage and its repair or pre-emption.
Linster C.L., Van Schaftingen E., Hanson A.D.
It is increasingly evident that metabolites suffer various kinds of damage, that such damage happens in all organisms and that cells have dedicated systems for damage repair and containment. First, chemical biology is demonstrating that diverse metabolites are damaged by side reactions of 'promisc ... >> More
It is increasingly evident that metabolites suffer various kinds of damage, that such damage happens in all organisms and that cells have dedicated systems for damage repair and containment. First, chemical biology is demonstrating that diverse metabolites are damaged by side reactions of 'promiscuous' enzymes or by spontaneous chemical reactions, that the products are useless or toxic and that the unchecked buildup of these products can be devastating. Second, genetic and genomic evidence from prokaryotes and eukaryotes is implicating a network of new, conserved enzymes that repair damaged metabolites or somehow pre-empt damage. Metabolite (that is, small-molecule) repair is analogous to macromolecule (DNA and protein) repair and seems from comparative genomic evidence to be equally widespread. Comparative genomics also implies that metabolite repair could be the function of many conserved protein families lacking known activities. How--and how well--cells deal with metabolite damage affects fields ranging from medical genetics to metabolic engineering. << Less
Nat Chem Biol 9:72-80(2013) [PubMed] [EuropePMC]
This publication is cited by 44 other entries.
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Guanine glycation repair by DJ-1/Park7 and its bacterial homologs.
Richarme G., Liu C., Mihoub M., Abdallah J., Leger T., Joly N., Liebart J.C., Jurkunas U.V., Nadal M., Bouloc P., Dairou J., Lamouri A.
DNA damage induced by reactive carbonyls (mainly methylglyoxal and glyoxal), called DNA glycation, is quantitatively as important as oxidative damage. DNA glycation is associated with increased mutation frequency, DNA strand breaks, and cytotoxicity. However, in contrast to guanine oxidation repai ... >> More
DNA damage induced by reactive carbonyls (mainly methylglyoxal and glyoxal), called DNA glycation, is quantitatively as important as oxidative damage. DNA glycation is associated with increased mutation frequency, DNA strand breaks, and cytotoxicity. However, in contrast to guanine oxidation repair, how glycated DNA is repaired remains undetermined. Here, we found that the parkinsonism-associated protein DJ-1 and its bacterial homologs Hsp31, YhbO, and YajL could repair methylglyoxal- and glyoxal-glycated nucleotides and nucleic acids. DJ-1-depleted cells displayed increased levels of glycated DNA, DNA strand breaks, and phosphorylated p53. Deglycase-deficient bacterial mutants displayed increased levels of glycated DNA and RNA and exhibited strong mutator phenotypes. Thus, DJ-1 and its prokaryotic homologs constitute a major nucleotide repair system that we name guanine glycation repair. << Less
Science 357:208-211(2017) [PubMed] [EuropePMC]
This publication is cited by 23 other entries.