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Literature summary extracted from
- Characterization of the endonuclease SSO2001 from Sulfolobus solfataricus P2 (2009), FEBS Lett., 583, 771-776.
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.1.99.B5 | expressed in Escherichia coli as a stable and soluble fusion protein with esterase. The fusion protein shows increased stability | Saccharolobus solfataricus |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.1.99.B5 | D63A | activity is nearly completely abolished | Saccharolobus solfataricus |
| 3.1.99.B5 | D63A/E92A | nuclease activity is completely inhibited | Saccharolobus solfataricus |
| 3.1.99.B5 | E92A | activity of the mutant is diminished, some residual activity remains | Saccharolobus solfataricus |
| 3.1.99.B5 | H62A/H91A | slightly decreased nuclease activity | Saccharolobus solfataricus |
| 3.1.99.B5 | S95 | mutation does not disturb the nuclease activity | Saccharolobus solfataricus |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.99.B5 | EDTA | inhibits the nuclease activity by chelating Mg2+ | Saccharolobus solfataricus |  |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.1.99.B5 | Mg2+ | cleavage of double-stranded substrates by nuclease-esterase fusion protein is observed in the presence of 10 mM MgCl2, but not in presence of Ca2+, Mn2+, Ni2+, or Zn2+ ions | Saccharolobus solfataricus | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.1.99.B5 | Saccharolobus solfataricus | Q97WW0 | - |
- |
| 3.1.99.B5 | Saccharolobus solfataricus P2 | Q97WW0 | - |
- |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.1.99.B5 | double-stranded DNA + H2O | the enzyme preferentially cleaves the dsDNA at G:C pairs. No structure specificity of the enzyme activity is observed. No obvious preference for dsDNA versus dsRNA is found when digestion under different nucleic acid concentrations is followed. Cleavage stopps at approximately 4 base pairs from the 5'-end implying that dsDNA strands shorter than 4 base pairs are not optimal substrates for nuclease activity | Saccharolobus solfataricus | ? | - |
? | |
| 3.1.99.B5 | double-stranded DNA + H2O | the enzyme preferentially cleaves the dsDNA at G:C pairs. No structure specificity of the enzyme activity is observed. No obvious preference for dsDNA versus dsRNA is found when digestion under different nucleic acid concentrations is followed. Cleavage stopps at approximately 4 base pairs from the 5'-end implying that dsDNA strands shorter than 4 base pairs are not optimal substrates for nuclease activity | Saccharolobus solfataricus P2 | ? | - |
? | |
| 3.1.99.B5 | double-stranded RNA + H2O | no obvious preference for dsDNA versus dsRNA is found when digestion under different nucleic acid concentrations is followed. Cleavage stopps at approximately 4 base pairs from the 5'-end implying that dsDNA strands shorter than 4 base pairs are not optimal substrates for nuclease activity | Saccharolobus solfataricus | ? | - |
? | |
| 3.1.99.B5 | double-stranded RNA + H2O | no obvious preference for dsDNA versus dsRNA is found when digestion under different nucleic acid concentrations is followed. Cleavage stopps at approximately 4 base pairs from the 5'-end implying that dsDNA strands shorter than 4 base pairs are not optimal substrates for nuclease activity | Saccharolobus solfataricus P2 | ? | - |
? | |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.1.99.B5 | SSO2001 | locus name | Saccharolobus solfataricus |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.99.B5 | 50 | - |
nuclease-esterase fusion protein | Saccharolobus solfataricus |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.1.99.B5 | 35 | 65 | 35°C: about 55% of maximal activity, 65°C: about 30% of maximal activity | Saccharolobus solfataricus |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.99.B5 | 3 | - |
optimal pH of the nuclease activity of nuclease-esterase fusion protein is in the range of neutral pH (78). An approximately 10% lower activity is found at pH 3 | Saccharolobus solfataricus |
| 3.1.99.B5 | 7 | 8 | optimal pH of the nuclease activity of nuclease-esterase fusion protein is in the range of neutral pH (78). An approximately 10% lower activity is found at pH 3 | Saccharolobus solfataricus |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.1.99.B5 | 3 | 8 | optimal pH of the nuclease activity of nuclease-esterase fusion protein is in the range of neutral pH (78). An approximately 10% lower activity is found at pH 3. pH 2.0: about 15% of maximal activity, pH 9: about 30% of maximal activity | Saccharolobus solfataricus |
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