Reaction participants Show >> << Hide
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Namehelp_outline
guanosine34 in tRNAAsp
Identifier
RHEA-COMP:19056
Reactive part
help_outline
- Name help_outline GMP residue Identifier CHEBI:74269 Charge -1 Formula C10H11N5O7P Positionhelp_outline 34 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 queuine Identifier CHEBI:17433 (CAS: 72496-59-4) help_outline Charge 0 Formula C12H15N5O3 InChIKeyhelp_outline WYROLENTHWJFLR-ACLDMZEESA-N SMILEShelp_outline Nc1nc2[nH]cc(CN[C@H]3C=C[C@H](O)[C@@H]3O)c2c(=O)[nH]1 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 guanine Identifier CHEBI:16235 (Beilstein: 147911; 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
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Namehelp_outline
queuosine34 in tRNAAsp
Identifier
RHEA-COMP:18572
Reactive part
help_outline
- Name help_outline queuosine 5'-phosphate residue Identifier CHEBI:194431 Charge -1 Formula C17H21N5O9P Positionhelp_outline 34 SMILEShelp_outline C1(=O)NC(=NC2=C1C(=CN2[C@@H]3O[C@H](COP(*)([O-])=O)[C@@H](O*)[C@H]3O)CN[C@H]4C=C[C@@H]([C@@H]4O)O)N 2D coordinates Mol file for the small molecule Search links Involved in 6 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:78303 | RHEA:78304 | RHEA:78305 | RHEA:78306 | |
|---|---|---|---|---|
| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
| UniProtKB help_outline |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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tRNA-guanine transglycosylase from bovine liver. Purification of the enzyme to homogeneity and biochemical characterization.
Slany R.K., Muller S.O.
The eucaryotic tRNA-modifying enzyme tRNA-guanine transglycosylase (Tgt) exchanges a guanine residue in the anticodon of tRNAs specific for aspartic acid, asparagine, histidine and tyrosine with the nutritionally derived deazaguanine base queuine (q), and with queuine precursors and guanine. In hi ... >> More
The eucaryotic tRNA-modifying enzyme tRNA-guanine transglycosylase (Tgt) exchanges a guanine residue in the anticodon of tRNAs specific for aspartic acid, asparagine, histidine and tyrosine with the nutritionally derived deazaguanine base queuine (q), and with queuine precursors and guanine. In higher eucaryotes, the amount of the resulting queuosine nucleoside (Q) is dependent on the developmental state of the respective cells. Neoplastically transformed and fast-proliferating cells usually are almost Q-deficient. The Tgt enzyme from bovine liver was purified 14,000-fold by DEAE cellulose chromatography, ammonium sulfate precipitation, and two subsequent affinity chromatography steps on heparin and tRNA agarose. The purest preparations contained two major proteins of 66 kDa and 32 kDa as revealed by SDS/PAGE and silver staining. The Km of the Tgt enzyme for guanine was 1.4 microM and the value for a purified Q-specific tRNA(Tyr), was 0.08 microM. The enzyme was active over a broad pH range; the activity was independent of metal ions and was strongly inhibited by salt concentrations higher than 50 mM. The determination and comparison of the N-terminal amino acid sequences from endoproteinase Lys-C cleavage products of the two subunits revealed no significant similarity to any known proteins. << Less
Eur J Biochem 230:221-228(1995) [PubMed] [EuropePMC]
This publication is cited by 1 other entry.