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Literature summary for 2.7.7.50 extracted from

  • Ho, C.K.; Schwer, B.; Shuman, S.
    Genetic, physical, and functional interactions between the triphosphatase and guanylyltransferase components of the yeast mRNA capping apparatus (1998), Mol. Cell. Biol., 18, 5189-5198.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.7.7.50

Activating Compound

Activating Compound Comment Organism Structure
RNA 5'-triphosphatase binding in the capping enzyme complex stimulates the mRNA guanylyltransferase by 10fold, icreases affinity for GTP Saccharomyces cerevisiae

Cloned(Commentary)

Cloned (Comment) Organism
expression of wild-type from plasmid in deficient mutant ceg1-25 Saccharomyces cerevisiae

Protein Variants

Protein Variants Comment Organism
additional information RNA 5'-triphosphatase, CET1 or CES5, expressed from high copy number plasmid in Saccharomyces cerevisiae, can compensate the growth defect caused by mutation ceg1-25 of the RNA guanylyltransferase Saccharomyces cerevisiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
GTP + pp(5')RNA Saccharomyces cerevisiae interaction of RNA 5'-triphosphatase and mRNA guanylyltransferase of the capping enzyme complex is essential for function and viability in vivo G(5')ppp(5')RNA + diphosphate
-
 ?
GTP + pp(5')RNA Saccharomyces cerevisiae mouse guanylyltransferase domain can substitute the deficient enzyme in Saccharomyces cerevisiae mutant in vivo G(5')ppp(5')RNA + diphosphate
-
 ?

Organism

Organism UniProt Comment Textmining
Saccharomyces cerevisiae
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 temperature-sensitive growth defect mutant ceg1-25
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Saccharomyces cerevisiae
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 gene CEG1
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
GTP + pp(5')RNA
-
 Saccharomyces cerevisiae G(5')ppp(5')RNA + diphosphate guanosine residue linked 5' through three phosphates to the 5' position of the terminal residue ?
GTP + pp(5')RNA interaction of RNA 5'-triphosphatase and mRNA guanylyltransferase of the capping enzyme complex is essential for function and viability in vivo Saccharomyces cerevisiae G(5')ppp(5')RNA + diphosphate
-
 ?
GTP + pp(5')RNA mouse guanylyltransferase domain can substitute the deficient enzyme in Saccharomyces cerevisiae mutant in vivo Saccharomyces cerevisiae G(5')ppp(5')RNA + diphosphate
-
 ?

Synonyms

Synonyms Comment Organism
More RNA 5'-triphosphatase and a RNA guanylyltransferase form a heterodimeric complex Saccharomyces cerevisiae
More enzyme is part of the bifunctional capping enzyme, which consists of autonomous and non-overlapping RNA 5'-triphosphatase and a RNA guanylyltransferase domain and activity Saccharomyces cerevisiae