Literature summary for 2.7.7.6 extracted from

Woody, A.Y.M.; Osumi-Davis, P.A.; Hiremath, M.M.; Woody, R.W.
Pre-steady-state and steady-state kinetic studies on transcription initiation catalyzed by T7 RNA polymerase and its active-site mutants K631R and Y639F (1998), Biochemistry, 37, 15958-15964.

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Protein Variants

Protein Variants	Comment	Organism
K631R	the fraction of catalytically active E form is 38% compared to 100% for the wild-type enzyme. The synthesis of long transcripts is markedly diminished for the mutant due to decreasing processivity	Escherichia phage T7
Y639F	the fraction of catalytically active E form is 32% compared to 100% for the wild-type enzyme	Escherichia phage T7

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	-	Escherichia phage T7

Organism

Organism	UniProt	Comment	Textmining
Escherichia phage T7	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
nucleoside triphosphate + RNAn	the enzyme requires DNA as template	Escherichia phage T7	diphosphate + RNAn+1	-	?

Subunits

Subunits	Comment	Organism
More	existence of two possible conformers: E and E that are in rapid equilibrium. Both forms can form the quarternary complex, but only the E form is capable of catalyzing phosphodiester bond formation	Escherichia phage T7

Turnover Number [1/s]

Turnover Number Minimum [1/s]	Turnover Number Maximum [1/s]	Substrate	Comment	Organism	Structure
additional information	-	additional information	-	Escherichia phage T7

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Release 2023.1 (January 2023)