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Literature summary for 2.7.7.79 extracted from

  • Jahn, D.; Pande, S.
    Histidine tRNA guanylyltransferase from Saccharomyces cerevisiae. II. Catalytic mechanism (1991), J. Biol. Chem., 266, 22832-22836.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
ADP 20 mM (7fold excess over ATP), 94% inhibition Saccharomyces cerevisiae
AMP 20 mM (7fold excess over ATP), complete inhibition Saccharomyces cerevisiae

Localization

Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
p-tRNAHis + ATP + GTP Saccharomyces cerevisiae the extra nucleotide in position -1 of mitochondrial and eukaryotic cytoplasmic tRNAHis molecules is added posttranscriptionally to the 5' end of the tRNA by a histidine-tRNA specific guanylyltransferase pppG-p-tRNAHis + AMP + diphosphate
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Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae P53215
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Reaction

Reaction Comment Organism Reaction ID
App-tRNAHis + GTP = pppGp-tRNAHis + AMP (1b) Saccharomyces cerevisiae
p-tRNAHis + ATP + GTP + H2O = pGp-tRNAHis + AMP + 2 diphosphate overall reaction Saccharomyces cerevisiae
p-tRNAHis + ATP = App-tRNAHis + diphosphate (1a) Saccharomyces cerevisiae

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
p-tRNAHis + ATP + dGTP dGTP is almost as efficient as GTP for the guanylylation process. While GDP still serves for the enzymatic reaction, GMP is accepted very poorly by the enzyme Saccharomyces cerevisiae ?
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p-tRNAHis + ATP + GDP dGTP is almost as efficient as GTP for the guanylylation process. While GDP still serves for the enzymatic reaction, GMP is accepted very poorly by the enzyme Saccharomyces cerevisiae ?
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?
p-tRNAHis + ATP + GTP the extra nucleotide in position -1 of mitochondrial and eukaryotic cytoplasmic tRNAHis molecules is added posttranscriptionally to the 5' end of the tRNA by a histidine-tRNA specific guanylyltransferase Saccharomyces cerevisiae pppG-p-tRNAHis + AMP + diphosphate
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?
p-tRNAHis + ATP + GTP during the first step ATP is cleaved to AMP and diphosphate creating adenylylated enzyme. In a second step the activated enzyme forms a stable complex with its cognate tRNA substrate. The 5'-phosphate of the tRNA is adenylylated by nucleotide transfer from the adenylylated guanylyltransferase to form A(5')pp(5') at the 5'-end of the tRNA. Finally, the 3'-hydroxyl of GTP adds to the activated 5' terminus of the tRNA with the release of AMP. dGTP is almost as efficient as GTP for the guanylylation process. While GDP still serves for the enzymatic reaction, GMP is accepted very poorly by the enzyme Saccharomyces cerevisiae pppGp-tRNAHis + AMP + diphosphate
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p-tRNAHis + dATP + GTP 30% of the activity compared to ATP Saccharomyces cerevisiae pppGp-tRNAHis + dAMP + diphosphate
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Synonyms

Synonyms Comment Organism
histidine tRNA guanylyltransferase
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Saccharomyces cerevisiae
TGT
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Saccharomyces cerevisiae