Information on EC 3.1.11.6 - exodeoxyribonuclease VII

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.11.6
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RECOMMENDED NAME
GeneOntology No.
exodeoxyribonuclease VII
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Exonucleolytic cleavage in either 5'- to 3'- or 3'- to 5'-direction to yield nucleoside 5'-phosphates
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
52933-20-7
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain AB1157
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Manually annotated by BRENDA team
strain BW25113
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Manually annotated by BRENDA team
strain ZK126
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Manually annotated by BRENDA team
strain ZK126
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Manually annotated by BRENDA team
xseB
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Manually annotated by BRENDA team
strain RM118
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Manually annotated by BRENDA team
strain RM118
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Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
duplex DNA containing single-stranded termini + H2O
hydrolyzed single-stranded DNA
show the reaction diagram
polydeoxyribonucleotides + H2O
hydrolyzed single-stranded DNA
show the reaction diagram
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-
-
?
single-stranded DNA + H2O
?
show the reaction diagram
single-stranded DNA + H2O
hydrolyzed single-stranded DNA
show the reaction diagram
thymine dimers + H2O
hydrolyzed single-stranded DNA
show the reaction diagram
additional information
?
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
single-stranded DNA + H2O
hydrolyzed single-stranded DNA
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KCl
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ExoVII activity is maximal at low salt concentrations (lower than 250 mM)
additional information
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manganese, nickel, cobalt and zinc have no effect
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
N-ethylmaleimide
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47% inhibition in absence of mercaptoethanol
phosphate
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inhibits nuclease activity at 80C; strongly inhibits, almost complete inhibition by 50 mM
sulfate
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strongly inhibits, almost complete inhibition by 50 mM
additional information
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is not active in standard Escherichia coli ExoVII buffer. Acetate has no effect
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
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required for 100% activity
phosphate
sulfate
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stimulates
additional information
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8 - 7.9
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
80
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XseA/B homologs TM1768 and TM1769 show robust and maximal nuclease activity
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
51820
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large subunit, amino acid sequence
54000
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heterodimer, 1 * 54000, 4 * 105000, large subunit: xseA gene, small subunit: xseB gene, SDS-PAGE
88000
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gel fltration
105000
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heterodimer, 1 * 54000, 4 * 105000, large subunit: xseA gene, small subunit: xseB gene, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pentamer
additional information
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stoichiometry of small to large subunits regulates ExoVII activity
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
structural analysis using bioinformatics. Large subunit XseA consists of four domains: an N-terminal OB-fold domain, a middle putatively catalytic domain, a coiled-coil domain and a short C-terminal segment. The OB-fold domain is responsible for DNA binding, the coiled-coil domain is involved in binding multiple copies of the XseB subunit and residues D155, R205, H238 and D241 of the middle domain are important for the catalytic activity but not for DNA binding
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3 - 7.8
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50% loss of activity compared to pH 7.8
134037
7.8 - 8.6
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50% loss of activity compared to pH 7.8
134037
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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half-life: 90 min
45
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half-life: 45 min
60
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half-life: 7 min
80
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XseA/B homologs TM1768 and TM1769 show robust nuclease activity
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
freezing and thawing causes loss of activity
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20C, 20 mM Tris-HCl, pH 8, 10 mM mercaptoethanol, 0.1 mM EDTA, 0.2 M NaCl, 50% glycerol, 18 months, 10% loss of activity
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
7500fold to 87% homogeneity
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wild-type and mutant ExoVII (XseA/B homologs TM1768 and TM1769) purified by gel filtration and on nickel-NTA column; wild-type and mutant ExoVII (XseA/B homologs TM1768 and TM1769) purified on nickel-NTA column
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
large subunit
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strain deficient in enzymic activity plus deficiency in RecJ, ExoI and ExoX exonuclease activities as well as a strain deficient in RecJ, ExoVII and ExoI exonucleases grow poorly in presence of 2-aminopurine. Exposure to 2-aminopurine results in filament formation. The quadruple mutant is cold-sensitive with a severe growth defect at 30C
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strain deficient in enzymic activity plus deficiency in RecJ, ExoI and ExoX exonuclease activities displays a 7fold increase in mutation rate, the availabilty of any one of thr nucleases is enough to support full mismatch correction
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wild-type and mutant ExoVII (XseA/B homologs TM1768 and TM1769) coexpressed in Escherichia coli BL21(DE3) cells
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D155A
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mutant of large subunit XseA, complete loss of catalytic activity
D241A
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mutant of large subunit XseA, complete loss of catalytic activity
DELTA397-456
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deletion mutant of large subunit XseA, complete loss of catalytic activity
F63A
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mutant of large subunit XseA, decrease in DNA-binding activity
H238A
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mutant of large subunit XseA, complete loss of catalytic activity
Q96A
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mutant of large subunit XseA, shows only mild effects
R205A
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mutant of large subunit XseA, complete loss of catalytic activity
R64E/R68E/R69E
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mutant of large subunit XseA, decrease in DNA-binding activity
D235A/D240A
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is completely inactive, even in the presence of magnesium
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
additional information
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