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Polymerase: Phi29

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Polymerase Reference Property Result Context
Phi29 The bacteriophage phi 29 DNA polymerase, a proofreading enzyme. Molecular Weight 6.652E+04 Dalton
Phi29 The bacteriophage phi 29 DNA polymerase, a proofreading enzyme. 3-5' Exonuclease (proofreading) Yes
Phi29 The bacteriophage phi 29 DNA polymerase, a proofreading enzyme. Full length or truncated Full length
Phi29 Highly efficient DNA synthesis by the phage phi 29 DNA polymerase. Symmetrical mode of DNA replication. Molecular Weight 6.6E+04 Dalton
Phi29 Highly efficient DNA synthesis by the phage phi 29 DNA polymerase. Symmetrical mode of DNA replication. Full length or truncated Full length
Phi29 Highly efficient DNA synthesis by the phage phi 29 DNA polymerase. Symmetrical mode of DNA replication. Processivity 70kb
Phi29 Terminal protein-primed DNA amplification. Maximum Product Length 1.928E+04bp Experimental conditions: Temp (30°C)
Phi29 Characterization and purification of a phage phi 29-encoded DNA polymerase required for the initiation of replication. Molecular Weight 6.8E+04 Dalton Technique: SDS-PAGE
Phi29 Characterization and purification of a phage phi 29-encoded DNA polymerase required for the initiation of replication. Cloned or native Cloned in E. coli
Phi29 Characterization and purification of a phage phi 29-encoded DNA polymerase required for the initiation of replication. Tagged No
Phi29 Characterization and purification of a phage phi 29-encoded DNA polymerase required for the initiation of replication. Full length or truncated Full length
Phi29 Characterization and purification of a phage phi 29-encoded DNA polymerase required for the initiation of replication. Other accessory protein(s) p3 terminal protein (TP)
Phi29 Initiation of phage phi 29 DNA replication in vitro: formation of a covalent complex between the terminal protein, p3, and 5'-dAMP. Cloned or native Cloned in E. coli
Phi29 Initiation of phage phi 29 DNA replication in vitro: formation of a covalent complex between the terminal protein, p3, and 5'-dAMP. Tagged No
Phi29 Initiation of phage phi 29 DNA replication in vitro: formation of a covalent complex between the terminal protein, p3, and 5'-dAMP. Other accessory protein(s) p3 terminal protein (TP)
Phi29 Insights into strand displacement and processivity from the crystal structure of the protein-primed DNA polymerase of bacteriophage phi29. Processivity 70kb
Phi29 Functional characterization of highly processive protein-primed DNA polymerases from phages Nf and GA-1, endowed with a potent strand displacement capacity. 3-5' Exonuclease (proofreading) Yes
Phi29 Functional characterization of highly processive protein-primed DNA polymerases from phages Nf and GA-1, endowed with a potent strand displacement capacity. Cloned or native Cloned in E. coli
Phi29 Functional characterization of highly processive protein-primed DNA polymerases from phages Nf and GA-1, endowed with a potent strand displacement capacity. Full length or truncated Full length
Phi29 Functional characterization of highly processive protein-primed DNA polymerases from phages Nf and GA-1, endowed with a potent strand displacement capacity. Vmax 2280 /minute Reaction: Nucleotide incorporation; Substrate: dNTPs
Phi29 A specific subdomain in phi29 DNA polymerase confers both processivity and strand-displacement capacity. 3-5' Exonuclease (proofreading) Yes
Phi29 A specific subdomain in phi29 DNA polymerase confers both processivity and strand-displacement capacity. Full length or truncated Full length
Phi29 A specific subdomain in phi29 DNA polymerase confers both processivity and strand-displacement capacity. Processivity 7E+04bp
Phi29 TempliPhi, phi29 DNA polymerase based rolling circle amplification of templates for DNA sequencing. 3-5' Exonuclease (proofreading) Yes
Phi29 TempliPhi, phi29 DNA polymerase based rolling circle amplification of templates for DNA sequencing. Cloned or native Native organism
Phi29 TempliPhi, phi29 DNA polymerase based rolling circle amplification of templates for DNA sequencing. Tagged No
Phi29 TempliPhi, phi29 DNA polymerase based rolling circle amplification of templates for DNA sequencing. Overall Error Rate 3E-06 errors/bp
Phi29 TempliPhi, phi29 DNA polymerase based rolling circle amplification of templates for DNA sequencing. Full length or truncated Full length
Phi29 TempliPhi, phi29 DNA polymerase based rolling circle amplification of templates for DNA sequencing. Maximum Product Length 800kb
Phi29 TempliPhi, phi29 DNA polymerase based rolling circle amplification of templates for DNA sequencing. Processivity 70kb
Phi29 TempliPhi, phi29 DNA polymerase based rolling circle amplification of templates for DNA sequencing. Vmax 50 /second Reaction: Nucleotide incorporation; Substrate: dNTPs
Phi29 Functional importance of bacteriophage phi29 DNA polymerase residue Tyr148 in primer-terminus stabilisation at the 3'-5' exonuclease active site. 3-5' Exonuclease (proofreading) Yes
Phi29 Functional importance of bacteriophage phi29 DNA polymerase residue Tyr148 in primer-terminus stabilisation at the 3'-5' exonuclease active site. 5-3' Exonuclease Unspecified
Phi29 Duality of polynucleotide substrates for Phi29 DNA polymerase: 3'-->5' RNase activity of the enzyme. RNase H Yes
Phi29 Phi29 DNA polymerase residues Tyr59, His61 and Phe69 of the highly conserved ExoII motif are essential for interaction with the terminal protein. 3-5' Exonuclease (proofreading) Yes
Phi29 Phi29 DNA polymerase residues Tyr59, His61 and Phe69 of the highly conserved ExoII motif are essential for interaction with the terminal protein. 5-3' Exonuclease Unspecified
Phi29 Processive proofreading and the spatial relationship between polymerase and exonuclease active sites of bacteriophage phi29 DNA polymerase. 3-5' Exonuclease (proofreading) Yes
Phi29 Processive proofreading and the spatial relationship between polymerase and exonuclease active sites of bacteriophage phi29 DNA polymerase. Cloned or native Cloned in E. coli
Phi29 Processive proofreading and the spatial relationship between polymerase and exonuclease active sites of bacteriophage phi29 DNA polymerase. 5-3' Exonuclease Unspecified
Phi29 Processive proofreading and the spatial relationship between polymerase and exonuclease active sites of bacteriophage phi29 DNA polymerase. Full length or truncated Full length
Phi29 Processive proofreading and the spatial relationship between polymerase and exonuclease active sites of bacteriophage phi29 DNA polymerase. Vmax 500 /second Reaction: 3-5' Exonuclease; Substrate: DNA template
Phi29 Involvement of the "linker" region between the exonuclease and polymerization domains of phi29 DNA polymerase in DNA and TP binding. 3-5' Exonuclease (proofreading) Yes
Phi29 Involvement of the "linker" region between the exonuclease and polymerization domains of phi29 DNA polymerase in DNA and TP binding. 5-3' Exonuclease Unspecified

Version:20241218

Using Polbase tables:

Sorting:

Tables may be sorted by clicking on any of the column titles. A second click reverses the sort order. <Ctrl> + click on the column titles to sort by more than one column (e.g. family then name).

Filtering:

It is also possible to filter the table by typing into the search box above the table. This will instantly hide lines from the table that do not contain your search text.