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Polymerase: Bst LF

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Polymerase Reference Property Result Context
Bst LF Thermostable Bst DNA polymerase I lacks a 3'-->5' proofreading exonuclease activity. Molecular Weight 67kD Technique: SDS-PAGE (Cleaved from MBP tag)
Bst LF Thermostable Bst DNA polymerase I lacks a 3'-->5' proofreading exonuclease activity. 3-5' Exonuclease (proofreading) No
Bst LF Thermostable Bst DNA polymerase I lacks a 3'-->5' proofreading exonuclease activity. Cloned or native Cloned in E. coli
Bst LF Thermostable Bst DNA polymerase I lacks a 3'-->5' proofreading exonuclease activity. 5-3' Exonuclease No
Bst LF Thermostable Bst DNA polymerase I lacks a 3'-->5' proofreading exonuclease activity. Tagged Yes
Bst LF Thermostable Bst DNA polymerase I lacks a 3'-->5' proofreading exonuclease activity. Tag Name MBP
Bst LF Thermostable Bst DNA polymerase I lacks a 3'-->5' proofreading exonuclease activity. Full length or truncated Truncated
Bst LF Thermostable Bst DNA polymerase I lacks a 3'-->5' proofreading exonuclease activity. Specific Activity 1E+05 units/mg
Bst LF Thermostable Bst DNA polymerase I lacks a 3'-->5' proofreading exonuclease activity. Describe truncation Lacks 5'->3' exonuclease domain det by subtilisin digestion - deletion up to nt 867
Bst LF Use of the restriction enzyme AvaI and exo- Bst polymerase in strand displacement amplification. Application name SDA
Bst LF Crystal structure of a thermostable Bacillus DNA polymerase I large fragment at 2.1 A resolution. KM 13uM Reaction: Nucleotide incorporation; Substrate: dNTPs; Technique: Filter binding ; Experimental conditions: Temp (65°C)
Bst LF Crystal structure of a thermostable Bacillus DNA polymerase I large fragment at 2.1 A resolution. KM 3.4nM Reaction: Polymerase-DNA interaction; Substrate: DNA template; Technique: Filter binding ; Experimental conditions: Temp (65°C)
Bst LF Crystal structure of a thermostable Bacillus DNA polymerase I large fragment at 2.1 A resolution. kcat 191.2 /second Reaction: Nucleotide incorporation; Substrate: dNTPs; Technique: Filter binding (16.5 nM primed M13); Experimental conditions: Temp (65°C)
Bst LF Crystal structure of a thermostable Bacillus DNA polymerase I large fragment at 2.1 A resolution. Describe truncation Contains C-terminal 592 aas (of 876)
Bst LF Processive DNA synthesis observed in a polymerase crystal suggests a mechanism for the prevention of frameshift mutations. Cloned or native Cloned in E. coli
Bst LF Processive DNA synthesis observed in a polymerase crystal suggests a mechanism for the prevention of frameshift mutations. Tagged No
Bst LF Processive DNA synthesis observed in a polymerase crystal suggests a mechanism for the prevention of frameshift mutations. Full length or truncated Truncated
Bst LF Processive DNA synthesis observed in a polymerase crystal suggests a mechanism for the prevention of frameshift mutations. Describe truncation C-term 592 aa's from C-term of full-length
Bst LF Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. Polymerase Catalytic Residue Amino Acids Asp653,Asp830,Glu831
Bst LF Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. 3-5' Exonuclease (proofreading) No
Bst LF Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. Cloned or native Cloned in E. coli
Bst LF Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. 5-3' Exonuclease Yes
Bst LF Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. Full length or truncated Truncated
Bst LF Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. Amino Acids Contacting Template Tyr714
Bst LF Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. Processivity 111bp
Bst LF Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. Specific Activity 1.5E+05 units/mg Technique: Polymerase Assay (calf thymus DNA)
Bst LF Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. Specific Activity 4.9E+05 units/mg Technique: Polymerase Assay (M13 DNA)
Bst LF Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. KM 13uM Reaction: Nucleotide incorporation; Substrate: dNTPs
Bst LF Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. KM 3.4nM Reaction: Polymerase-DNA interaction; Substrate: DNA template
Bst LF Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. kcat 191.2 /second Reaction: Nucleotide incorporation; Substrate: dNTPs
Bst LF Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal. Describe truncation contains aa 297-876
Bst LF DNA polymerases from hyperthermophiles. Reverse Transcriptase Activity Yes
Bst LF DNA polymerases from hyperthermophiles. 3-5' Exonuclease (proofreading) No
Bst LF DNA polymerases from hyperthermophiles. 5-3' Exonuclease No
Bst LF DNA polymerases from hyperthermophiles. Processivity 111bp
Bst LF DNA polymerases from hyperthermophiles. Specific Activity 15 units/mg Technique: Polymerase Assay (calf thymus DNA)
Bst LF DNA polymerases from hyperthermophiles. Specific Activity 49 units/mg Technique: Polymerase Assay (M13 DNA)
Bst LF DNA polymerases from hyperthermophiles. KM 13uM Reaction: Nucleotide incorporation; Substrate: dNTPs
Bst LF DNA polymerases from hyperthermophiles. KM 4.2nM Reaction: Polymerase-DNA interaction; Substrate: DNA template
Bst LF DNA polymerases from hyperthermophiles. Strand Displacement Yes
Bst LF DNA polymerases from hyperthermophiles. kcat 1.15E+04 /minute Reaction: Nucleotide incorporation; Substrate: dNTPs

Version:20240423

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.