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Literature summary extracted from

  • Nakaishi, T.; Iio, K.; Yamamoto, K.; Urabe, I.; Yomo, T.
    Kinetic properties of Qb replicase, an RNA dependent RNA polymerase (2002), J. Biosci. Bioeng., 93, 322-327.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.7.48 ATP reaction at the U-incorporation site is inhibited with inhibition constant 1.09 mM, reaction at the G-incorporation site is inhibited with inhibition constant 1.25 mM, reaction at the C-incorporation site is inhibited with inhibition constant 1.48 mM Qubevirus durum
2.7.7.48 CTP reaction at the A-incorporation site is inhibited with inhibition constants of 2.7 mM Qubevirus durum
2.7.7.48 UTP reaction at the A-incorporation site is inhibited with inhibition constants of 3.2 mM Qubevirus durum

Organism

EC Number Organism UniProt Comment Textmining
2.7.7.48 Qubevirus durum
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 Escherichia coli infected with
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Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.48
-
 Qubevirus durum

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.7.48 nucleoside triphosphate + RNAn when the nucleotide concentrations are low, C is incorporated at the fastest rate and G at the slowest. G-incorporation step largely limits the overall reaction rate Qubevirus durum diphosphate + RNAn+1
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