Literature summary for 2.7.7.7 extracted from

Ong, J.L.; Loakes, D.; Jaroslawski, S.; Too, K.; Holliger, P.
Directed evolution of DNA polymerase, RNA polymerase and reverse transcriptase activity in a single polypeptide (2006), J. Mol. Biol., 361, 537-550.

Search for more literature for 2.7.7.7

Application

Application	Comment	Organism
biotechnology	short-patch compartmentalized self-replication will be a powerful strategy for the generation of polymerases with altered substrate specificity for applications in nano- and biotechnology and in the enzymatic synthesis of antisense and RNAi probes	Thermus aquaticus

Protein Variants

Protein Variants	Comment	Organism
E602V/A608V/I614M/E615G	the mutant enzyme is able to incorporate both NTPs and dNTPs with the same catalytic efficiency as the wild-type enzyme incorporates dNTPs. The mutant enzyme allowed the generation of mixed RNADNA amplification products in PCR demonstrating DNA polymerase, RNA polymerase as well as reverse transcriptase activity within the same polypeptide. The mutant displays an expanded substrate spectrum towards other 2'-substituted nucleotides and is able to synthesize nucleic acid polymers in which each base bear a different 2'-substituent	Thermus aquaticus

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	-	Thermus aquaticus

Organism

Organism	UniProt	Comment	Textmining
Thermus aquaticus	P19821	-	-

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Release 2023.1 (January 2023)