Information on EC 3.1.11.3 - exodeoxyribonuclease (lambda-induced)

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
3.1.11.3
-
RECOMMENDED NAME
GeneOntology No.
exodeoxyribonuclease (lambda-induced)
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 5'-phosphates
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY hide
37288-28-1
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
yeast
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
lambda exonuclease is an ATP-independent, but Mg2+-dependent enzyme that binds to dsDNA ends and processively digests the 5'-ended strand to form 5' mononucleotides and a long 3'-ended ssDNA tail
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
single-stranded DNA + 5'-phospho-2'-deoxynucleotides
show the reaction diagram
oligonucleotides + H2O
5'-phosphomononucleotides
show the reaction diagram
single-stranded DNA + H2O
5'-phosphomononucleotides
show the reaction diagram
additional information
?
-
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
double-stranded DNA + H2O
single-stranded DNA + 5'-phospho-2'-deoxynucleotides
show the reaction diagram
single-stranded DNA + H2O
5'-phosphomononucleotides
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
high pressure
-
p-chloromercuribenzoate
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-mercaptoethanol
-
-
dithiothreitol
NaCl
-
82% stimulation up to 70 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0000018
DNA
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
6 - 11.7
Double-stranded DNA
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9.2 - 9.5
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7 - 10.2
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia phage lambda
Escherichia phage lambda
Escherichia phage lambda
Escherichia phage lambda
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
42000
-
sedimentation, gel filtration
70000
-
gel fitration, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
by ammonium sulfate precepitation
-
by ammonium sulfate precepitation
-
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
repeated freezing and thawing causes loss of activity
stability enhanced by dithiothreitol
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, 40% glycerol, 1mg/ml bovine serum albumin, 6 months, 0% loss of activity
-20°C, in solution, 1 year, 10% loss of activity
0°C, in solution, 2 months, little loss of activity
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crosses of phage 80 and lambda
-
lambda mutant T11 overexpress the enzyme; multiple mutant phage strain SG5519 as source of the enzyme
partial
subfractions upon gradient chromatography: IVa, IVb, phage-lambda induced enzyme; to homogeneity
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D119A
-
site-directed mutagenesis, inactive mutant
E85A
-
site-directed mutagenesis, almost inactive mutant
K131A
-
site-directed mutagenesis, inactive mutant
K49A
-
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
K76A
-
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
L78A
-
site-directed mutagenesis, the mutant shows a significantly diminished level of activity compared to the wild-type enzyme
M53A
-
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
R137A
-
site-directed mutagenesis, inactive mutant
R28A
-
site-directed mutagenesis, mutation of a residue that contact the 5' phosphate of the DNA, inactive mutant
R45A
-
site-directed mutagenesis, inactive mutant
W24A
-
site-directed mutagenesis, mutation of a residue that contact the 5' phosphate of the DNA, almost inactive mutant
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
synthesis
-
solid-phase digestion of dsDNAs using immobilization of lambda exonuclease onto poly(methylmethacrylate) micropillars populated within a microfluidic device for the on-chip digestion. The efficiency for the catalysis of dsDNA digestion using lamba-exonuclease, including its processivity and reaction rate, are higher when the enzyme is attached to a solid support compared to the free solution digestion. A clipping rate of 1000 nucleotides per s can be obtained for the digestion of lambda-DNA (48.5 kbp) by lambda-exonuclease
additional information
-
preparation of single-stranded DNA is an essential and important step in the combinatorial chemistry technique SELEX (Systematic Evolution of Ligands by EXponential enrichment) for in vitro selection of single-stranded DNA aptamers and numerous other molecular biology procedures, whereby single-stranded DNA generation by lambda exonuclease digestion is superior to other techniques. Important role for complete lambda exonuclease digestion of phosphorylated DNA strand plays the manufacturing of phosphorylated primer
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