Literature summary for 2.7.7.48 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.

Search for more literature for 2.7.7.48

Inhibitors

Inhibitors	Comment	Organism	Structure
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
CTP	reaction at the A-incorporation site is inhibited with inhibition constants of 2.7 mM	Qubevirus durum
UTP	reaction at the A-incorporation site is inhibited with inhibition constants of 3.2 mM	Qubevirus durum

Organism

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

Purification (Commentary)

Purification (Comment)	Organism
-	Qubevirus durum

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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	-	?

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)