Literature summary for 2.7.7.7 extracted from

Hogg, M.; Cooper, W.; Reha-Krantz, L.; Wallace, S.S.
Kinetics of error generation in homologous B-family DNA polymerases (2006), Nucleic Acids Res., 34, 2528-2535.

Search for more literature for 2.7.7.7

Organism

Organism	UniProt	Comment	Textmining
Escherichia phage RB69	P04415	-	-
Tequatrovirus T4	P04415	-	-

Purification (Commentary)

Purification (Comment)	Organism
-	Tequatrovirus T4
-	Escherichia phage RB69

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
deoxynucleoside triphosphate + DNAn	bacteriohage T4 and bacteriophage RB69 replicative DNA polymerases exhibit differing abilities to form various base pairs. Formation of Watson-Crick base pairs occurs at similar rates between the two proteins but the incoming nucleotides are bound less tightly by RB69 DNA polymerase. Incorporation of an A opposite furan by T4 DNA polymerase is more rapid than for RB69 DNA polymerase with the two proteins having similar binding constants for the incoming dATP. An A:C mismatch is formed almost equally well by both proteins, while a significant difference exists when a T:T mismatch is formed	Tequatrovirus T4	diphosphate + DNAn+1	-	?
deoxynucleoside triphosphate + DNAn	bacteriohage T4 and bacteriophage RB69 replicative DNA polymerases exhibit differing abilities to form various base pairs. Formation of Watson-Crick base pairs occurs at similar rates between the two proteins but the incoming nucleotides are bound less tightly by RB69 DNA polymerase. Incorporation of an A opposite furan by T4 DNA polymerase is more rapid than for RB69 DNA polymerase with the two proteins having similar binding constants for the incoming dATP. An A:C mismatch is formed almost equally well by both proteins, while a significant difference exists when a T:T mismatch is formed	Escherichia phage RB69	diphosphate + DNAn+1	-	?

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Release 2023.1 (January 2023)