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Information on EC 3.1.99.B5 - endonuclease SSO2001 and Organism(s) Saccharolobus solfataricus and UniProt Accession Q97WW0

for references in articles please use BRENDA:EC3.1.99.B5
preliminary BRENDA-supplied EC number
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EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
            
                3.1.99.B5 endonuclease SSO2001
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This record set is specific for:
Saccharolobus solfataricus
UNIPROT: Q97WW0
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The taxonomic range for the selected organisms is: Saccharolobus solfataricus
The expected taxonomic range for this enzyme is: Saccharolobus solfataricus
Reaction Schemes
endonuclease specifically digesting double-stranded oligonucleotides and preferably cleaving at G:C pairs
Synonyms
sso2001, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
double-stranded DNA + H2O
?
show the reaction diagram
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
-
-
?
double-stranded RNA + H2O
?
show the reaction diagram
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
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
inhibits the nuclease activity by chelating Mg2+
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3
optimal pH of the nuclease activity of nuclease-esterase fusion protein is in the range of neutral pH (7–8). An approximately 10% lower activity is found at pH 3
7 - 8
optimal pH of the nuclease activity of nuclease-esterase fusion protein is in the range of neutral pH (7–8). An approximately 10% lower activity is found at pH 3
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3 - 8
optimal pH of the nuclease activity of nuclease-esterase fusion protein is in the range of neutral pH (7–8). 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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
nuclease-esterase fusion protein
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35 - 65
35°C: about 55% of maximal activity, 65°C: about 30% of maximal activity
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D63A
activity is nearly completely abolished
D63A/E92A
nuclease activity is completely inhibited
E92A
activity of the mutant is diminished, some residual activity remains
H62A/H91A
slightly decreased nuclease activity
S95
mutation does not disturb the nuclease activity
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a stable and soluble fusion protein with esterase. The fusion protein shows increased stability
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Han, D.; Krauss, G.
Characterization of the endonuclease SSO2001 from Sulfolobus solfataricus P2
FEBS Lett.
583
771-776
2009
Saccharolobus solfataricus (Q97WW0), Saccharolobus solfataricus, Saccharolobus solfataricus P2 (Q97WW0), Saccharolobus solfataricus P2
Manually annotated by BRENDA team