Information on EC 3.1.21.6 - CC-preferring endodeoxyribonuclease

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY hide
3.1.21.6
-
RECOMMENDED NAME
GeneOntology No.
CC-preferring endodeoxyribonuclease
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Endonucleolytic cleavage to give 5'-phosphooligonucleotide end-products, with a preference for cleavage within the sequence CC
show the reaction diagram
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-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
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-
-
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CAS REGISTRY NUMBER
COMMENTARY hide
37211-67-9
not distinguished from EC 3.1.21.2
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
mc26 culture
-
-
Manually annotated by BRENDA team
Virus NYs-1
dsDNA-containing virus
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-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
28S rDNA + H2O
?
show the reaction diagram
-
R1Bm EN cleaves both strands of the 28S rDNA sequence at the target site, 5'-A(G/C)(A/T)!(A/G)T-3' is the consensus sequence, thus cleavage site
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-
?
covalently closed circular DNA pUC18 + H2O
?
show the reaction diagram
-
-
-
-
?
double-stranded DNA
?
show the reaction diagram
Lambda DNA
Double-stranded fragments between 7 and 24 bases with 5' and/or 3'-protruding single-stranded tails
show the reaction diagram
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-
-
-
lambda DNA + H2O
?
show the reaction diagram
-
-
-
-
?
pBR322 DNA + H2O
DNA fragments carrying phosphate groups at 5' ends and hydroxyl group at the 3' ends, respectively
show the reaction diagram
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-
-
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?
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
can replace Mg2+ showing better activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
-
chelates Mg2+, increasing Mg2+ concentrations can restore the activity of the enzyme
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
18
-
crude extract
9444
-
521fold purified enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
additional information
Virus NYs-1
-
Chlorella sp. strain NC64A cell infected with the dsDNA-containing virus NYs-1
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22000
-
gel filtration
43000
-
gel filtration
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by hanging drop vapor diffusion method, to 2.0 A resolution, belongs to space group P321 with unit cell parameters a = b = 141.3 A, c = 37.5 A, alpha = beta = 90°, gamma = 120°, has a beta-hairpin region (residues 176-183) at the edge of the DNA binding surface
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
0°C, Tris-HCl buffer, pH 7.4, 10 mM EDTA, 10% glycerol, stable for at least 15 days
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by nickel chelation chromatography and by gel filtration
-
to near homogeneity, 521fold by gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
plasmid pR1EN and its mutant derivatives were transformed into Escherichia coli BL21(DE3)/pLysS strain
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D19A
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relative activity of bottom-strand cleavage is less than half that of top-strand cleavage, whereas activity of top-strand cleavage is more than 80% that of the wild-type
E147A
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does not exhibit a significant reduction in nicking activity, compared with that of the wild-type
E18A
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relative activity of bottom-strand cleavage is less than half that of top-strand cleavage, whereas activity of top-strand cleavage is more than 80% that of the wild-type
H130A
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moderately decreased nicking activity
H140A
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shows less than 20% of the wild-type activity for the cleavage of both strands, amounts of cleavage products are less than 1% of the total substrates
H209A
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exhibits no detectable cleavage activity on the top or bottom strand of the oligonucleotide substrate
H54A
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relative activity of bottom-strand cleavage is less than half that of top-strand cleavage, whereas activity of top-strand cleavage is more than 80% that of the wild-type
H78A
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shows less than 20% of the wild-type activity for the cleavage of both strands, amounts of cleavage products are less than 1% of the total substrates
K56A
-
moderately decreased nicking activity
N180A
-
altered cleavage patterns, shows less than 20% of the wild-type activity for the cleavage of both strands, amounts of cleavage products are less than 1% of the total substrates
Q97A
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shows less than 20% of the wild-type activity for the cleavage of both strands, amounts of cleavage products are less than 1% of the total substrates
R139A
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shows less than 20% of the wild-type activity for the cleavage of both strands, amounts of cleavage products are less than 1% of the total substrates
R144A
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shows less than 20% of the wild-type activity for the cleavage of both strands, amounts of cleavage products are less than 1% of the total substrates
S206A
-
relative activity of bottom-strand cleavage is less than half that of top-strand cleavage, whereas activity of top-strand cleavage is more than 80% that of the wild-type
S43A
-
does not exhibit a significant reduction in nicking activity, compared with that of the wild-type
S99A
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does not exhibit a significant reduction in nicking activity, compared with that of the wild-type
T178A
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shows less than 20% of the wild-type activity for the cleavage of both strands, amounts of cleavage products are less than 1% of the total substrates
Y42A
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shows less than 20% of the wild-type activity for the cleavage of both strands, amounts of cleavage products are less than 1% of the total substrates
Y98A
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altered cleavage patterns, shows less than 20% of the wild-type activity for the cleavage of both strands, amounts of cleavage products are less than 1% of the total substrates
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information