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Namehelp_outline
a 5'-end adenosine-5'-diphospho-5'-ribonucleotide-tRNAHis
Identifier
RHEA-COMP:13932
Reactive part
help_outline
- Name help_outline adenosine-5'-diphospho-5'-(ribonucleotide) residue Identifier CHEBI:138280 Charge -2 Formula C15H19N5O13P2R SMILEShelp_outline *[C@@H]1O[C@H](COP(=O)(OP(=O)(OC[C@H]2O[C@@H](N3C=4N=CN=C(N)C4N=C3)[C@@H]([C@@H]2O)O)[O-])[O-])[C@@H](O*)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline GTP Identifier CHEBI:37565 (Beilstein: 5211792) help_outline Charge -4 Formula C10H12N5O14P3 InChIKeyhelp_outline XKMLYUALXHKNFT-UUOKFMHZSA-J SMILEShelp_outline Nc1nc2n(cnc2c(=O)[nH]1)[C@@H]1O[C@H](COP([O-])(=O)OP([O-])(=O)OP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 100 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
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Namehelp_outline
a 5'-end triphospho-guanosine-ribonucleotide-tRNAHis
Identifier
RHEA-COMP:13931
Reactive part
help_outline
- Name help_outline 5'-triphospho-guanosine-ribonucleotide residue Identifier CHEBI:138278 Charge -5 Formula C15H18N5O20P4R SMILEShelp_outline [C@@H]1(O[C@H]([C@@H]([C@@H]1O*)O)*)COP(O[C@@H]2[C@H](O[C@@H](N3C=4N=C(NC(=O)C4N=C3)N)[C@@H]2O)COP(=O)(OP(=O)(OP(=O)([O-])[O-])[O-])[O-])(=O)[O-] 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline AMP Identifier CHEBI:456215 Charge -2 Formula C10H12N5O7P InChIKeyhelp_outline UDMBCSSLTHHNCD-KQYNXXCUSA-L SMILEShelp_outline Nc1ncnc2n(cnc12)[C@@H]1O[C@H](COP([O-])([O-])=O)[C@@H](O)[C@H]1O 2D coordinates Mol file for the small molecule Search links Involved in 545 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 10,232 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:54560 | RHEA:54561 | RHEA:54562 | RHEA:54563 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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| MetaCyc help_outline |
Related reactions help_outline
More general form(s) of this reaction
Publications
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tRNA(His) guanylyltransferase (THG1), a unique 3'-5' nucleotidyl transferase, shares unexpected structural homology with canonical 5'-3' DNA polymerases.
Hyde S.J., Eckenroth B.E., Smith B.A., Eberley W.A., Heintz N.H., Jackman J.E., Doublie S.
All known DNA and RNA polymerases catalyze the formation of phosphodiester bonds in a 5' to 3' direction, suggesting this property is a fundamental feature of maintaining and dispersing genetic information. The tRNA(His) guanylyltransferase (Thg1) is a member of a unique enzyme family whose member ... >> More
All known DNA and RNA polymerases catalyze the formation of phosphodiester bonds in a 5' to 3' direction, suggesting this property is a fundamental feature of maintaining and dispersing genetic information. The tRNA(His) guanylyltransferase (Thg1) is a member of a unique enzyme family whose members catalyze an unprecedented reaction in biology: 3'-5' addition of nucleotides to nucleic acid substrates. The 2.3-Å crystal structure of human THG1 (hTHG1) reported here shows that, despite the lack of sequence similarity, hTHG1 shares unexpected structural homology with canonical 5'-3' DNA polymerases and adenylyl/guanylyl cyclases, two enzyme families known to use a two-metal-ion mechanism for catalysis. The ability of the same structural architecture to catalyze both 5'-3' and 3'-5' reactions raises important questions concerning selection of the 5'-3' mechanism during the evolution of nucleotide polymerases. << Less
Proc. Natl. Acad. Sci. U.S.A. 107:20305-20310(2010) [PubMed] [EuropePMC]
This publication is cited by 3 other entries.
Comments
RHEA:54560 part of RHEA:54564