Information on EC 3.1.99.B5 - endonuclease SSO2001

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The expected taxonomic range for this enzyme is: Sulfolobus solfataricus

EC NUMBER
COMMENTARY hide
3.1.99.B5
preliminary BRENDA-supplied EC number
RECOMMENDED NAME
GeneOntology No.
endonuclease SSO2001
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
endonuclease specifically digesting double-stranded oligonucleotides and preferably cleaving at G:C pairs
show the reaction diagram
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
double-stranded RNA + H2O
?
show the reaction diagram
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
INHIBITORS
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
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as a stable and soluble fusion protein with esterase. The fusion protein shows increased stability
ENGINEERING
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
D63A
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activity is nearly completely abolished
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D63A/E92A
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nuclease activity is completely inhibited
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E92A
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activity of the mutant is diminished, some residual activity remains
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H62A/H91A
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slightly decreased nuclease activity
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S95
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mutation does not disturb the nuclease activity
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