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Literature summary for 5.4.99.25 extracted from

  • Muller, S.; Fourmann, J.B.; Loegler, C.; Charpentier, B.; Branlant, C.
    Identification of determinants in the protein partners aCBF5 and aNOP10 necessary for the tRNA:Psi55-synthase and RNA-guided RNA:PSI-synthase activities (2007), Nucleic Acids Res., 35, 5610-5624.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
protein aNOP10 interaction with the pseudouridine synthase aCBF5 is required for the RNA-guided RNA:pseudouridine-synthase activity. The stable anchoring of aCBF5 to tRNAs relies on its PUA domain and the tRNA CCA sequence. Nonetheless, interaction of aNOP10 with aCBF5 can counterbalance the absence of the PUA domain or the CCA sequence and more generally helps the aCBF5 tRNA:pseudouridine55-synthase activity. Substitution of the aNOP10 residue Y14 by an alanine disturbs this activity, it only impairs mildly the RNA-guided activity. The opposite effect is observed for the aNOP10 variant H31A Pyrococcus abyssi

Protein Variants

Protein Variants Comment Organism
K53A substitution K53A or R202A in aCBF5 impairs both the tRNA:pseudouridine55-synthase and the RNA-guided RNA:pseudouridine-synthase activities Pyrococcus abyssi
R202A substitution K53A or R202A in aCBF5 impairs both the tRNA:pseudouridine55-synthase and the RNA-guided RNA:pseudouridine-synthase activities Pyrococcus abyssi

Organism

Organism UniProt Comment Textmining
Pyrococcus abyssi Q9V1A5
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
tRNA uridine55 the stable anchoring of aCBF5 to tRNAs relies on its PUA domain and the tRNA CCA sequence Pyrococcus abyssi tRNA pseudouridine55
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Synonyms

Synonyms Comment Organism
aCBF5
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Pyrococcus abyssi
tRNA:PSI55-synthase
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Pyrococcus abyssi