EC Number | Cloned (Comment) | Organism |
---|---|---|
3.1.11.1 | overexpression in Escherichia coli | Saccharolobus solfataricus |
EC Number | Inhibitors | Comment | Organism | Structure |
---|---|---|---|---|
3.1.11.1 | NTP | the strong 3'-5' exonuclease activity of polB1 is inhibited by 50% in the presence of 0.002 mM dNTPs, but remains measurable at up to 0.6 mM dNTPs | Saccharolobus solfataricus |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.1.11.1 | Saccharolobus solfataricus | P26811 | - |
- |
3.1.11.1 | Saccharolobus solfataricus P2 | P26811 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
3.1.11.1 | - |
Saccharolobus solfataricus |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.1.11.1 | dsDNA + H2O | the enzyme degrades both single-stranded (ss) and double-stranded (ds) DNA at similar rates in vitro at temperatures of physiological relevance. No difference is found in the cleavage of 3'-recessive, 3'-protruding and blunt-ended DNA duplexes at these temperatures. A single-stranded nick in duplex DNA is less readily employed by the enzyme to initiate cleavage than a free 3' end. At lower temperatures, Sso polB1 cleavs ssDNA more efficiently than dsDNA | Saccharolobus solfataricus | ? | - |
? | |
3.1.11.1 | dsDNA + H2O | the enzyme degrades both single-stranded (ss) and double-stranded (ds) DNA at similar rates in vitro at temperatures of physiological relevance. No difference is found in the cleavage of 3'-recessive, 3'-protruding and blunt-ended DNA duplexes at these temperatures. A single-stranded nick in duplex DNA is less readily employed by the enzyme to initiate cleavage than a free 3' end. At lower temperatures, Sso polB1 cleavs ssDNA more efficiently than dsDNA | Saccharolobus solfataricus P2 | ? | - |
? | |
3.1.11.1 | ssDNA + H2O | the enzyme degrades both single-stranded (ss) and double-stranded (ds) DNA at similar rates in vitro at temperatures of physiological relevance. No difference is found in the cleavage of 3'-recessive, 3'-protruding and blunt-ended DNA duplexes at these temperatures. A single-stranded nick in duplex DNA is less readily employed by the enzyme to initiate cleavage than a free 3' end. At lower temperatures, Sso polB1 cleavs ssDNA more efficiently than dsDNA | Saccharolobus solfataricus | ? | - |
? | |
3.1.11.1 | ssDNA + H2O | the enzyme degrades both single-stranded (ss) and double-stranded (ds) DNA at similar rates in vitro at temperatures of physiological relevance. No difference is found in the cleavage of 3'-recessive, 3'-protruding and blunt-ended DNA duplexes at these temperatures. A single-stranded nick in duplex DNA is less readily employed by the enzyme to initiate cleavage than a free 3' end. At lower temperatures, Sso polB1 cleavs ssDNA more efficiently than dsDNA | Saccharolobus solfataricus P2 | ? | - |
? |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
3.1.11.1 | Sso polB1 | - |
Saccharolobus solfataricus |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.1.11.1 | 65 | - |
assay at | Saccharolobus solfataricus |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
3.1.11.1 | 8 | - |
assay at | Saccharolobus solfataricus |
EC Number | General Information | Comment | Organism |
---|---|---|---|
3.1.11.1 | physiological function | in view of the strong exonuclease activity of Sso polB1 on matched dsDNA, its is suggested that Sulfolobus solfataricus may have evolved mechanisms to regulate the exonuclease/polymerase ratio of the enzyme, thereby reducing the cost of proofreading at high temperature | Saccharolobus solfataricus |