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Literature summary for 2.4.2.48 extracted from

  • Sabina, J.; Soell, D.
    The RNA-binding PUA domain of archaeal tRNA-guanine transglycosylase is not required for archaeosine formation (2006), J. Biol. Chem., 281, 6993-7001.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
truncated forms of TGT expressed in Escherichia coli Pyrococcus furiosus

Protein Variants

Protein Variants Comment Organism
additional information the C-terminal extension of the enzyme is not required for the selection of G15 as the site of base exchange. Truncated forms of Pyrococcus furiosus TGT retain their specificity for guanine exchange at position 15. Deletion of the PUA domain causes a 4fold drop in the observed kcat and results in a 75fold increased Km for tRNAAsp compared with full-length TGT Pyrococcus furiosus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
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additional information
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Pyrococcus furiosus

Organism

Organism UniProt Comment Textmining
Pyrococcus furiosus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
tRNAguanine + 7-cyano-7-deazaguanine archaeal TGT substitutes 7-cyano-7-deazaguanine for the G in position 15 of tRNA as the first step in archaeosine formation Pyrococcus furiosus ?
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