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Literature summary for 2.7.7.48 extracted from

  • Blumenthal, T.
    Qbeta RNA replicase and protein synthesis elongation factors EF-Tu and EF-Ts (1979), Methods Enzymol., 60, 628-638.
    View publication on PubMed

Organic Solvent Stability

Organic Solvent Comment Organism
urea denaturation Qubevirus durum

Organism

Organism UniProt Comment Textmining
Qubevirus durum
-
Escherichia coli infected with
-
Qubevirus durum
-
QbetaamB86
-
Qubevirus durum QbetaamB86
-
QbetaamB86
-

Purification (Commentary)

Purification (Comment) Organism
-
Qubevirus durum

Renatured (Commentary)

Renatured (Comment) Organism
when the enzyme is denatured in 8 M urea, a maximum of about 40% of the poly(G) polymerase activity can be regained Qubevirus durum

Storage Stability

Storage Stability Organism
-20°C, enzyme concentration greater than 1 mg/ml, stable for more than 1 year Qubevirus durum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
nucleoside triphosphate + RNAn GTP and polyC Qubevirus durum diphosphate + RNAn+1
-
?
nucleoside triphosphate + RNAn GTP and polyC Qubevirus durum QbetaamB86 diphosphate + RNAn+1
-
?

Subunits

Subunits Comment Organism
tetramer the enzyme contains four nonidentical polypeptide chains, only one of which is a product of the phage genome. The other three subunits, present in uninfected cells are ribosomal protein S1 and protein synthesis elongation factors EF-Tu and EF-TS Qubevirus durum