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Literature summary 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

EC Number Organic Solvent Comment Organism
2.7.7.48 urea denaturation Qubevirus durum

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.7.48
-
 Qubevirus durum

Renatured (Commentary)

EC Number Renatured (Comment) Organism
2.7.7.48 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

EC Number Storage Stability Organism
2.7.7.48 -20°C, enzyme concentration greater than 1 mg/ml, stable for more than 1 year Qubevirus durum

Substrates and Products (Substrate)

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

Subunits

EC Number Subunits Comment Organism
2.7.7.48 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