Information on EC 3.1.11.3 - exodeoxyribonuclease (lambda-induced)

phosphorylated double-stranded DNA + H2O

Substrates: -
Products: -

phosphorylated double-stranded DNA + H2O

single-stranded DNA + ?

774045

Substrates: -
Products: -

PO4-TAT(-FAM)CCACAGACACATACTCCA-BHQ1 + H2O

Substrates: a probe sequence
Products: -

PO4-TCTCCACAYT(-FAM)CACATACTCCA-BHQ1 + H2O

Substrates: a probe sequence, Y = tetrahydrofuran abasic site
Products: -

PO4-TUT(-FAM)ACACAGACACATACTCCA-BHQ1 + H2O

Substrates: a probe sequence
Products: -

PO4-TUT(-FAM)TCACAGACACATACTCCA-BHQ1 + H2O

Substrates: a probe sequence
Products: -

PO4-TXT(-FAM)TCACAGACACATACTCCA-BHQ1 + H2O

Substrates: a probe sequence, X = natural abasic site generated by UDG
Products: -

PO4-TYT(-FAM)ACACAGACACATACTCCA-BHQ1 + H2O

Substrates: a probe sequence, Y = tetrahydrofuran abasic site
Products: -

PO4-TYT(-FAM)CCACAGACACATACTCCA-BHQ1 + H2O

Substrates: a probe sequence, Y = tetrahydrofuran abasic site
Products: -

PO4-TYT(-FAM)TCACAGACACATACTCCA-BHQ1 + H2O

Substrates: a probe sequence, Y = tetrahydrofuran abasic site
Products: -

PO4-TYTCCACAGACACAT(-FAM)ACTCCATAATTTAA-BHQ1 + H2O

Substrates: a probe sequence, Y = tetrahydrofuran abasic site
Products: -

single-stranded DNA + H2O

5'-phosphomononucleotides

14 entries

TATGTGTCTGTGVAGACGAGAGTAAG + H2O

Substrates: a target sequence
Products: -

TGTGTCTGTGVAGACGAGAGTAAG + H2O

Substrates: a target sequence
Products: -

additional information

9 entries

DNA + H2O

Substrates: -
Products: -

DNA + H2O

Substrates: -
Products: -

double-stranded DNA + H2O

Substrates: the enzyme binds to double-stranded DNA ends, resecting one strand in the 5' to 3' direction to expose a 3' single-stranded DNA overhang
Products: -

double-stranded DNA + H2O

Substrates: -
Products: -

double-stranded DNA + H2O

770512

Substrates: 5' phosphorothiolate at the 5' ends of the reverse transcription-loop-mediated isothermal amplification product effectively prevents enzyme end-degradation. Addition of the enzyme with Rep-X and ATP leads to appreciable degradation of reverse transcription-loop-mediated isothermal amplification product
Products: -

double-stranded DNA + H2O

Substrates: the enzyme shows selective hydrolysis of phosphate modified strands, with either 5' recessed end or blunt end double-stranded DNA as its substrate
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

133979, 133984, 133985, 133986, 133988, 133992

Substrates: -
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

Substrates: exonucleolytic cleavage in the 5'- to 3'-direction to yield 5'-phosphomononucleotides
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

Substrates: degradation also at single-stranded breaks within DNA-duplex
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

Substrates: possess "red" recombination system
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

Substrates: high processivity
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

133987

Substrates: no activity on denatured DNA or RNA
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

133980, 133983, 133987

Substrates: degrades native DNA 100 times faster than long single-stranded DNA or oligonucleotides
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

Substrates: shows strong preference for termini bearing 5'-phosphoryl groups
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

133978, 133980, 133989

Substrates: no attack at single-stranded breaks within DNA-duplex
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

133978, 133980, 133981

Substrates: degrades double-stranded native DNA
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

Substrates: preference for a 5'-phosphoryl group over a 5'-hydroxyl group
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

133978, 133980, 133981, 133983, 133987, 133989

Substrates: -
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

695543, 695561

Substrates: lambda exonuclease is unable to initiate DNA digestion at nicks or gaps
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

Substrates: degradation also at single-stranded breaks within DNA-duplex
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

Substrates: degrades double-stranded native DNA
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

Substrates: -
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

133979, 133984, 133985, 133986, 133988, 133992

Substrates: -
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

Substrates: exonucleolytic cleavage in the 5'- to 3'-direction to yield 5'-phosphomononucleotides
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

Substrates: possess "red" recombination system
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

Substrates: high processivity
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

133987

Substrates: no activity on denatured DNA or RNA
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

133980, 133983, 133987

Substrates: degrades native DNA 100 times faster than long single-stranded DNA or oligonucleotides
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

Substrates: shows strong preference for termini bearing 5'-phosphoryl groups
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

133978, 133980, 133989

Substrates: no attack at single-stranded breaks within DNA-duplex
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

Substrates: degrades double-stranded native DNA
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

Substrates: preference for a 5'-phosphoryl group over a 5'-hydroxyl group
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

133978, 133980, 133983, 133987, 133989

Substrates: -
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

Lambdavirus lambda phage 80

Substrates: -
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

Substrates: no activity on denatured DNA or RNA
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

Substrates: degrades double-stranded native DNA
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

Substrates: -
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

Substrates: activity depends on lenght of double-stranded DNA
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

Substrates: high processivity
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

Substrates: degrades double-stranded native DNA
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

Substrates: -
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

708359

Substrates: sequence-dependent rate and pausing of individual lambda exonuclease enzymes during the digestion of a DNA sequence containing 120 CGG repeats. GC-rich repetitive sequences provide a significant barrier to lambda exonuclease activity by increasing the probability of pausing in addition to reducing the average digestion rate
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

710025

Substrates: lambda exonuclease selectively digests the phosphorylated undesired strand of double-stranded DNA and produces single-stranded DNA in high yield and purity
Products: -

oligonucleotides + H2O

5'-phosphomononucleotides

Substrates: strong preference for relatively short chain oligonucleotides
Products: -

oligonucleotides + H2O

5'-phosphomononucleotides

Substrates: low rate
Products: -

oligonucleotides + H2O

5'-phosphomononucleotides

Substrates: strong preference for relatively short chain oligonucleotides
Products: -

oligonucleotides + H2O

5'-phosphomononucleotides

Substrates: low rate
Products: -

single-stranded DNA + H2O

5'-phosphomononucleotides

Substrates: -
Products: -

single-stranded DNA + H2O

5'-phosphomononucleotides

Substrates: mechanism for stimulation of recombination
Products: -

single-stranded DNA + H2O

5'-phosphomononucleotides

Substrates: degrades the 5'-terminated strand at a single-stranded branch
Products: -

single-stranded DNA + H2O

5'-phosphomononucleotides

Substrates: rate of digestion and binding is inversely related to the chain lenght
Products: -

single-stranded DNA + H2O

5'-phosphomononucleotides

Substrates: digestion not processively
Products: -

single-stranded DNA + H2O

5'-phosphomononucleotides

Substrates: at single-stranded DNA branches
Products: -

single-stranded DNA + H2O

5'-phosphomononucleotides

Substrates: -
Products: -

single-stranded DNA + H2O

5'-phosphomononucleotides

Substrates: mechanism for stimulation of recombination
Products: -

single-stranded DNA + H2O

5'-phosphomononucleotides

Substrates: degrades the 5'-terminated strand at a single-stranded branch
Products: -

single-stranded DNA + H2O

5'-phosphomononucleotides

Substrates: rate of digestion and binding is inversely related to the chain lenght
Products: -

single-stranded DNA + H2O

5'-phosphomononucleotides

Substrates: digestion not processively
Products: -

single-stranded DNA + H2O

5'-phosphomononucleotides

Substrates: binds to circular or linear single-stranded DNA
Products: -

single-stranded DNA + H2O

5'-phosphomononucleotides

Substrates: at single-stranded DNA branches
Products: -

single-stranded DNA + H2O

5'-phosphomononucleotides

Substrates: degrades ssDNA at higher enzyme concentrations
Products: -

additional information

713754

Substrates: for enzyme digestion of single DNA molecules, individual lambda-DNA molecules labeled with the fluorescent dye, YOYO-1, are stretched in a laminar flow stream and immobilized on a bare fused-silica prism surface based on hydrophobic and electrostatic interactions. Enzyme digestion is initiated by the influx of lambda-exonuclease enzyme via capillary force, method evaluation, overview. Progression of single-DNA digestion by lambda-exonuclease enzyme based on the decrease in the length of the DNA molecule at a dye:bp ratio of 1:5
Products: -

additional information

Substrates: the enzyme unwinds the DNA prior to cleavage, such that two nucleotides of the 5'-ended strand insert into the active site of one subunit of the trimer, while the 3'-ended strand passes through the central channel to emerge out the back of the trimer. Unwinding of the DNA is facilitated by several apolar residues, including Leu78, that wedge into the base pairs at the single/double-strand junction to form favorable hydrophobic interactions. The terminal 5' phosphate of the DNA binds to a positively charged pocket buried at the end of the active site, while the scissile phosphate bridges two active site Mg2+ ions, mechanism of progressivity, structure-activity analysis, overview
Products: -

additional information

Substrates: G-quadruplexes are resistant to lambda-exo digestion
Products: -

additional information

Substrates: analysis of the ability of enzyme lambda-exo to efficiently digest G4 structures by digesting a plasmid derived from the human MYC locus (from MCF-7 breast cancer cells) that contains a well-characterized G4 motif, overview. Genome-wide biases of lambda-exo are profiled by sequencing the DNA remaining after lambda-exo digestion of sonicated genomic DNA (gDNA) from nonreplicating G0 MCF7 cells (LexoG0). The enzyme does not efficiently digest G-quadruplex (G4) structures in a plasmid. And enzyme lambda-exo digestion of nonreplicating genomic DNA (LexoG0) enriches GC-rich DNA and G4 motifs genome-wide
Products: -

additional information

750114

Substrates: an ultrasensitive electrochemical biosensor for polynucleotide kinase assay based on gold nanoparticle-mediated lambda exonuclease cleavage-induced signal amplification is constructed. The presence of polynucleotide kinase (PNK) induces the phosphorylation of the strand 2-strand 1 hybrid and the subsequent cleavage of double-stranded DNA (dsDNA) by lambda exonuclease, resulting in the release of AuNP-strand 2 conjugates and [Ru(NH3)6]3+ from the gold electrode surface and consequently the decrease of electrochemical signal
Products: -

additional information

Substrates: sensitive discrimination of stable mismatched base pairs by an abasic site modified fluorescent probe and lambda exonuclease, substrate is target ssDNA with diverse DNA sequences, overview. Substrate specificity for base positions, discrimination factors of C:C type mismatched probe/target duplex, discrimination factors (DF) for duplexes containing different types of mismatched base pairs at position +I by using the abasic site modified probe in the absence and presence of different blocker strands, tested blocker sequences for the targets and type of mismatched base pair, overview
Products: -

additional information

Substrates: the enzyme has low activity towards non-phosphorylated DNA and single-stranded DNA
Products: -

additional information

Substrates: the enzyme degrades double-stranded DNA up to 350 times faster than single-stranded DNA and shows barely detectable rates of hydrolysis of RNA
Products: -

additional information

Substrates: the enzyme is ATP-independent
Products: -

show all columns Go to Natural Substrate Search

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NATURAL SUBSTRATE

NATURAL PRODUCT

REACTION DIAGRAM

ORGANISM

UNIPROT

LITERATURE

COMMENTARY

REVERSIBILITY
r=reversible
ir=irreversible
?=not specified

double-stranded DNA + H2O

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

6 entries

phosphorylated double-stranded DNA + H2O

Substrates: -
Products: -

single-stranded DNA + H2O

5'-phosphomononucleotides

additional information

Substrates: G-quadruplexes are resistant to lambda-exo digestion
Products: -

double-stranded DNA + H2O

Substrates: the enzyme binds to double-stranded DNA ends, resecting one strand in the 5' to 3' direction to expose a 3' single-stranded DNA overhang
Products: -

double-stranded DNA + H2O

Substrates: -
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

133984, 133985, 133986, 133988, 133978, 133980, 133981, 133983, 133987, 133989

Substrates: -
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

Substrates: -
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

133984, 133985, 133986, 133988, 133978, 133980, 133983, 133987, 133989

Substrates: -
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

Lambdavirus lambda phage 80

Substrates: -
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

Substrates: -
Products: -

double-stranded DNA + H2O

single-stranded DNA + 5'-phospho-2'-deoxynucleotides

Substrates: -
Products: -

single-stranded DNA + H2O

5'-phosphomononucleotides

Substrates: -
Products: -

single-stranded DNA + H2O

5'-phosphomononucleotides

Substrates: at single-stranded DNA branches
Products: -

single-stranded DNA + H2O

5'-phosphomononucleotides

Substrates: -
Products: -

single-stranded DNA + H2O

5'-phosphomononucleotides

Substrates: at single-stranded DNA branches
Products: -

show all columns Go to Cofactor Search

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COFACTOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

ATP

show all columns Go to Metals and Ions Search

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METALS and IONS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

Mg2+

Mn2+

Mg2+

required

Mg2+

optimal concentration 5 mM

Mg2+

required

Mg2+

optimal concentration 5 mM

Mg2+

required

Mg2+

activates

Mg2+

dependent on

Mg2+

required

Mg2+

highly dependent on Mg2+. The optimum concentration is 1.0-2.5 mM

Mg2+

required

Mg2+

Mg2+

required

Mg2+

required

Mg2+

initiates DNA digestion

708359

Mn2+

divalent cation: Mn2+ or Mg2+ required

133981, 133986

Mn2+

optimal concentration 1 mM

Mn2+

divalent cation: Mn2+ or Mg2+ required

Mn2+

optimal concentration 1 mM

Mn2+

divalent cation: Mn2+ or Mg2+ required

Mn2+

divalent cation: Mn2+ or Mg2+ required

show all columns Go to Inhibitor Search

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INHIBITOR

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

high pressure

KCl

Na+

NaCl

p-chloromercuribenzoate

3 entries

high pressure

hydrostatic pressure controles activity

high pressure

hydrostatic pressure controles activity

KCl

31% inhibition at 50 mM

KCl

31% inhibition at 50 mM

KCl

KCl

NaCl

82% inhibition at 50 mM

NaCl

82% inhibition at 50 mM

NaCl

NaCl

inhibition at concentrations over 70 mM

p-chloromercuribenzoate

p-chloromercuribenzoate

p-chloromercuribenzoate

show all columns Go to Activating Compound Search

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ACTIVATING COMPOUND

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

2-mercaptoethanol

dithiothreitol

KCl

NaCl

Show Disease (435 entries)

82% stimulation up to 70 mM

dithiothreitol

required

dithiothreitol

required

KCl

stimulates at 20 mM

KCl

stimulates at 20 mM

show all columns Go to KM Value Search

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KM VALUE [mM]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

0.0000018

DNA

0.0000018

DNA

5'-OH blunt end double-stranded DNA

0.0000018

DNA

5'-OH blunt end double-stranded DNA

show all columns Go to Turnover Number Search

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TURNOVER NUMBER [1/s]

SUBSTRATE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

IMAGE

6 - 11.7

Double-stranded DNA

Double-stranded DNA

at 20°C and pH 7.5

Double-stranded DNA

at 20°C and pH 7.5

11.7

Double-stranded DNA

at 37°C and pH 7.5

11.7

Double-stranded DNA

at 37°C and pH 7.5

show all columns Go to pH Optimum Search

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pH OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

7.7

8 - 8.5

9.2 - 9.5

9.4

9.5

9.2 - 9.5

9.2 - 9.5

9.4

assay at

9.4

assay at

750704, 750114, 750293

show all columns Go to pH Range Search

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pH RANGE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

7 - 10.2

7.5

9.2 - 9.5

highly active between pH 9.2 and 9.5

9.6

7 - 10.2

pH 7.0: 16%, 8.0: 35%, pH 10.0: 35%, 10.2: 8% of maximal activity

7 - 10.2

pH 7.0: 16%, 8.0: 35%, pH 10.0: 35%, 10.2: 8% of maximal activity

7.5

no activity at DNA nicks

7.5

no activity at DNA nicks

9.6

no activity at DNA nicks

9.6

no activity at DNA nicks

show all columns Go to Temperature Optimum Search

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TEMPERATURE OPTIMUM

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

show all columns Go to Organism Search

assay at

750704, 750114, 750293

assay at

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks include all textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks + FRENDAco-occurrence of enzyme names and organism names (less precise)

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ORGANISM

COMMENTARY

LITERATURE

UNIPROT

SEQUENCE DB

SOURCE

brenda

Lambdavirus lambda phage 80

phage 80

brenda

brenda

yeast

brenda

brenda

brenda

Escherichia coli infected with phage lambda only

133972, 133978, 133979, 133980, 133981, 133983, 133984, 133985, 133986, 133987, 133988, 133989, 133992, 133993

brenda

recB gene

brenda

133972, 133978, 133979, 133983, 133984, 133986, 133987, 133989, 133992, 133993

brenda

682074

UniProt

brenda

713754, 716778, 728851, 728953

brenda

750114, 750293, 750704

UniProt

brenda

768545, 770512, 772444, 774045, 774735, 775746, 776012

brenda

defective lambda mutant T11

brenda

multiple mutant phage strain SG5519

brenda

mutants with increased thermostability

brenda

phage 80

brenda

redA and redB mutants

133980, 133985

brenda

show all columns Go to Source Tissue Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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SOURCE TISSUE

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

SOURCE

commercial preparation

695543, 695561

brenda

lung

brenda

show all columns Go to Localization Search

only manually annotated data include textmining data from AMENDAenzyme occurrence in organism, localization and source tissue with reliability ranks

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LOCALIZATION

ORGANISM

UNIPROT

COMMENTARY

GeneOntology No.

LITERATURE

SOURCE

nucleus

5634

brenda

top hide

Highest Expressing Human Cell Lines

Filter by:

Cell Line Links

Gene Links

show all columns Go to General Information Search

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GENERAL INFORMATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

physiological function

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

physiological function

analysis of intrinsic biases of lambda exonuclease in nascent strand sequencing reveals phasing between nucleosomes and G-quadruplex motifs around a subset of human replication origins

Go to AA Sequence and Transmembrane Helices SearchGo to Localization Prediction

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UNIPROT

ENTRY NAME

ORGANISM

NO. OF AA

NO. OF TRANSM. HELICES

MOLECULAR WEIGHT[Da]

SOURCE

SEQUENCE

LOCALIZATION PREDICTION

The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).

E8PLM2 pBLAST

OLD_THESS

Thermus scotoductus (strain ATCC 700910 / SA-01)

528

59748

Swiss-Prot

P03697 pBLAST

EXO_LAMBD

Escherichia phage lambda

226

25909

Swiss-Prot

P13520 pBLAST

VOLD_BPP2

Escherichia phage P2

586

65381

Swiss-Prot

P20321 pBLAST

EXRN_BPT3

Enterobacteria phage T3

302

34627

Swiss-Prot

Escherichia phage CICC 80001

A0A088F7W3 pBLAST

A0A088F7W3_9CAUD

300

34560

TrEMBL

Escherichia phage 64795_ec1

A0A192Y7A3 pBLAST

A0A192Y7A3_9CAUD

300

34473

TrEMBL

A0A2H4P6D1 pBLAST

A0A2H4P6D1_9CAUD

Escherichia phage EG1

300

34531

TrEMBL

A0A2K9VJU9 pBLAST

A0A2K9VJU9_9CAUD

Escherichia phage HZ2R8

300

34488

TrEMBL

A0A2Z5HA74 pBLAST

A0A2Z5HA74_9CAUD

Salmonella phage 3A_8767

300

34474

TrEMBL

Enterobacteria phage vB_EcoP_IME390

A0A386KC14 pBLAST

A0A386KC14_9CAUD

300

34488

TrEMBL

A0A386K657 pBLAST

A0A386K657_9CAUD

Escherichia phage N30

300

34503

TrEMBL

A0A386K899 pBLAST

A0A386K899_9CAUD

Escherichia phage C5

300

34503

TrEMBL

A0A481S227 pBLAST

A0A481S227_9CAUD

Escherichia phage NC-A

300

34518

TrEMBL

A0A481V878 pBLAST

A0A481V878_9CAUD

Escherichia phage HZP2

300

34580

TrEMBL

A0A5J6T7Y3 pBLAST

A0A5J6T7Y3_9CAUD

Serratia phage Pila

300

34503

TrEMBL

A0A649WKI6 pBLAST

A0A649WKI6_9CAUD

Salmonella phage C2

300

34545

TrEMBL

Escherichia phage vB_EcoP_PHB20

A0A6B9RH14 pBLAST

A0A6B9RH14_9CAUD

300

34488

TrEMBL

Escherichia phage vB_EcoP_PHB19

A0A6B9RKL5 pBLAST

A0A6B9RKL5_9CAUD

300

34517

TrEMBL

A0A6M5CA54 pBLAST

A0A6M5CA54_9CAUD

Enterococcus phage EFA-2

300

34475

TrEMBL

Secretory Pathway (Reliability: 4)

A0A7S6R7E8 pBLAST

A0A7S6R7E8_9CAUD

Escherichia phage JB01

300

34573

TrEMBL

A0A9E7NLW7 pBLAST

A0A9E7NLW7_9CAUD

Cedecea phage Yanou

300

34547

TrEMBL

other Location (Reliability: 3)

A0A9X9JM84 pBLAST

A0A9X9JM84_9CAUD

Escherichia phage 04922B

300

34518

TrEMBL

A0AA51R3U1 pBLAST

A0AA51R3U1_9CAUD

Escherichia phage pO111

300

34531

TrEMBL

Chloroplast (Reliability: 3)

A0AA51VJJ7 pBLAST

A0AA51VJJ7_9CAUD

Yersinia phage vB_YpYeO9

300

34503

TrEMBL

Escherichia phage Sekstaphage-1

A0AA96PPI1 pBLAST

A0AA96PPI1_9CAUD

302

34627

TrEMBL

Serratia phage vB_SmaP-UFV01

A0AAE7FJ81 pBLAST

A0AAE7FJ81_9CAUD

300

34545

TrEMBL

A0AAE7VK68 pBLAST

A0AAE7VK68_9CAUD

Edwardsiella phage PVN09

300

34460

TrEMBL

Escherichia phage JeanTinguely

A0AAE7VU32 pBLAST

A0AAE7VU32_9CAUD

300

34499

TrEMBL

Escherichia phage JacobBurckhardt

A0AAE7VTP5 pBLAST

A0AAE7VTP5_9CAUD

300

34531

TrEMBL

Yersinia phage vB_YenP_WX2

A0AAT9S9I8 pBLAST

A0AAT9S9I8_9CAUD

300

34559

TrEMBL

Yersinia phage vB_YenP_WX1

A0AAT9SCB1 pBLAST

A0AAT9SCB1_9CAUD

300

34531

TrEMBL

Yersinia phage vB_YenP_WW2

A0AAT9S9X8 pBLAST

A0AAT9S9X8_9CAUD

300

34517

TrEMBL

B3VD58 pBLAST

B3VD58_9CAUD

Escherichia phage 13a

300

34591

TrEMBL

E1XUA5 pBLAST

E1XUA5_9CAUD

Salmonella phage Vi06

300

34588

TrEMBL

I6Q9P1 pBLAST

I6Q9P1_9CAUD

Yersinia phage YpP-Y

300

34522

TrEMBL

Secretory Pathway (Reliability: 1)

I6Q8W1 pBLAST

I6Q8W1_9CAUD

Yersinia phage YpsP-G

300

34489

TrEMBL

I6Q8U2 pBLAST

I6Q8U2_9CAUD

Yersinia phage YpP-R

300

34522

TrEMBL

Q6WYD9 pBLAST

Q6WYD9_BPT7

300

34600

TrEMBL

Q6WYP0 pBLAST

Q6WYP0_BPT7

300

34502

TrEMBL

Q6WY33 pBLAST

Q6WY33_BPT7

300

34706

TrEMBL

Q778K3 pBLAST

Q778K3_BPT3

Enterobacteria phage T3

302

34627

TrEMBL

Q858L5 pBLAST

Q858L5_9CAUD

Yersinia phage phiA1122

300

34522

TrEMBL

T1PVL1 pBLAST

T1PVL1_9CAUD

Enterobacteria phage T7M

302

34627

TrEMBL

P06229 pBLAST

FEN_BPT5

Escherichia phage T5

291

33448

Swiss-Prot

Entries 1 - 20 of 44

Show complete table

Go to PDB and Structure Links Search

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PDB

SCOP

CATH

UNIPROT

ORGANISM

show all columns Go to Molecular Weight Search

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MOLECULAR WEIGHT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

24000

28000

3 entries

42000

sedimentation, gel filtration

70000

gel fitration, SDS-PAGE

24000

gel fitration, SDS-PAGE

24000

gel fitration, SDS-PAGE

24000

gene sequence

24000

gene sequence

28000

28000

alpha,beta, 1 * 24000 + 1 * 28000, exonuclease and beta protein as subunits, SDS-PAGE at the presence of urea

28000

alpha,beta, 1 * 24000 + 1 * 28000, exonuclease and beta protein as subunits, SDS-PAGE at the presence of urea

show all columns Go to Subunit Search

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SUBUNIT

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

x * 25900, calculated from amino acid sequence

dimer

trimer

dimer

alpha,beta, 1 * 24000 + 1 * 28000, exonuclease and beta protein as subunits, SDS-PAGE at the presence of urea

dimer

Go to Crystallization (commentary) Search

alpha,beta, 1 * 24000 + 1 * 28000, exonuclease and beta protein as subunits, SDS-PAGE at the presence of urea

trimer

crystal structure

trimer

crystal structure

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CRYSTALLIZATION (Commentary)

ORGANISM

UNIPROT

LITERATURE

133993

by ammonium sulfate precepitation

by ammonium sulfate precepitation

show all columns Go to Protein Variants Search

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PROTEIN VARIANTS

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

D119A

site-directed mutagenesis, inactive mutant

E85A

site-directed mutagenesis, almost inactive mutant

K131A

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

K131A

show all columns Go to Temperature Stability Search

site-directed mutagenesis, inactive mutant

K131A

inactive

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TEMPERATURE STABILITY

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

30 min, pH 9.4, inactivation

complete inactivation after 5 min without substrate

complete inactivation after 5 min without substrate

Go to General Stability Search

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GENERAL STABILITY

ORGANISM

UNIPROT

LITERATURE

repeated freezing and thawing causes loss of activity

stability enhanced by dithiothreitol

repeated freezing and thawing causes loss of activity

repeated freezing and thawing causes loss of activity

stability enhanced by dithiothreitol

stability enhanced by dithiothreitol

Go to Storage Stability Search

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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

-20�C, 40% glycerol, 1mg/ml bovine serum albumin, 6 months, 0% loss of activity

-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

-20�C, in solution, 1 year, 10% loss of activity

0�C, in solution, 2 months, little loss of activity

0�C, in solution, 2 months, little loss of activity

Go to Purification (commentary) Search

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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

133985, 133987, 133988, 133989

133985, 133987, 133989

lambda mutant T11 overexpress the enzyme

lambda mutant T11 overexpress the enzyme

multiple mutant phage strain SG5519 as source of the enzyme

multiple mutant phage strain SG5519 as source of the enzyme

partial

partial

partial

partial

subfractions upon gradient chromatography: IVa, IVb, phage-lambda induced enzyme

show all columns Go to Application Search

subfractions upon gradient chromatography: IVa, IVb, phage-lambda induced enzyme

to homogeneity

to homogeneity

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APPLICATION

ORGANISM

UNIPROT

COMMENTARY

LITERATURE

analysis

medicine

molecular biology

nascent strand sequencing (NS-seq) is used to discover DNA replication origins genome-wide, allowing identification of features for their specification. NS-seq depends on the ability of lambda exonuclease (lambda-exo) to efficiently digest parental DNA while leaving RNA-primer protected nascent strands intact. LexoG0 data to control for nascent strand-independent lambda-exo biases in NSseq and validated this approach at the rDNA locus. Possible increase of both sensitivity and specificity of NS-seq, overview

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

728953

additional information

analysis

use as reagent restriction mapping and substrate preparation

analysis

use as reagent restriction mapping and substrate preparation

analysis

for studies of genetic recombination

133980, 133985, 133988

analysis

for studies of genetic recombination

133980, 133985, 133988

analysis

use as reagent for determination of secondary structures at DNA termini

analysis

use as reagent for determination of secondary structures at DNA termini

analysis

use as reagent restriction mapping and substrate preparation

133972

analysis

use as reagent restriction mapping and substrate preparation

133972

analysis

ultiplexed single-molecule assay for enzymatic activity on flow-stretched DNA can be applied to lambda exonuclease

682074

analysis

a novel method for real-time monitoring of the activity and kinetics of T4 polynucleotide kinase (PNK) by use of a singly fluorophore-labeled DNA-hairpin smart probe (SP) coupled with lambda exonuclease (lambda exo) cleavage.

695561

analysis

simple and homogeneous microRNA assay by integration of ligase chain reaction and lambda exonuclease-assisted cationic conjugated polymer biosensing. Ligase chain reaction is utilized for exponential amplification of microRNA, and lambda exonuclease is introduced to degrade excess fluorescein-labeled probes in ligase chain reaction for eliminating background signal. The method is sensitive enough to detect 0.1 fM target microRNA and specific to discriminate one-base difference of microRNAs

728851

analysis

an ultrasensitive electrochemical biosensor for polynucleotide kinase assay based on gold nanoparticle-mediated lambda exonuclease cleavage-induced signal amplification is constructed. The presence of polynucleotide kinase (PNK) induces the phosphorylation of the strand 2-strand 1 hybrid and the subsequent cleavage of double-stranded DNA (dsDNA) by lambda exonuclease, resulting in the release of AuNP-strand 2 conjugates and [Ru(NH3)6]3+ from the gold electrode surface and consequently the decrease of electrochemical signal. The PNK activity can be simply monitored by the measurement of [Ru(NH3)6]3+ peak current signal. This assay is very sensitive with a very low detection limit and exhibits a large dynamic range from 0.001 to 10 U/ml. The method can be used to screen the PNK inhibitors, and it shows excellent performance in real sample analysis, thus holding great potential for further applications in biological researches and clinic diagnosis

750114

analysis

Lambdavirus lambda phage 80

for studies of genetic recombination

medicine

the enzyme can be used in a biosensor to detect the tumor marker Pax-5a. The enzyme can cleave the blunt end formed by the hairpin probe and the Pax-5a gene, which exposes the nucleic acid sequence that can initiate the hybridization chain reaction

medicine

the enzyme assists a ligase chain reaction-based electrochemical biosensor for highly sensitive CYP2C19*2 allele genotyping with zero-background in human whole blood samples

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

710025

additional information

top print hide References Search

the enzyme induces DNAzyme amplification for fluorescent detection of brown spot of tobacco caused by Alternaria alternata

775746

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REF.

AUTHORS

TITLE

JOURNAL

VOL.

PAGES

YEAR

ORGANISM (UNIPROT)

PUBMED ID

SOURCE

133972

Pierce, J.R.; Nazimiec, M.; Tang, M.s.

Comparison of sequence preference of tomaymycin- and anthramycin-DNA bonding by exonuclease III and lambda exonuclease digestion and UvrABC nuclease incision analysis

Biochemistry

7069-7078

1993

Escherichia coli, Lambdavirus lambda

8343501

brenda

133978

Lehman, I.R.

Bacterial deoxyribonucleases

The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )

251-270

1971

Escherichia coli, Lambdavirus lambda

brenda

Mitsis, P.G.; Kwagh, J.G.

Characterization of the interaction of lambda exonuclease with the ends of DNA

Nucleic Acids Res.

3057-3063

1999

Escherichia coli, Lambdavirus lambda

10454600

brenda

Little, J.W.

Lambda exonuclease

Gene Amplif. Anal.

135-145

1981

Escherichia coli, Lambdavirus lambda

6242844

brenda

Kerr, C.; Sadowski, P.D.

Gene 6 exonuclease of bacteriophage T7. I. Purification and properties of the enzyme

J. Biol. Chem.

247

305-310

1972

Escherichia coli, Escherichia phage T7

4336366

brenda

Lindahl, T.

An exonuclease specific for double-stranded DNA: deoxyribonuclease from rabbit tissues

Methods Enzymol.

148-153

1971

Oryctolagus cuniculus

brenda

Sriprakash, K.S.; Lundh, N.; Huh, M.M.O.; Radding, C.M.

The specificity of lambda exonuclease. Interactions with single-atranded DNA

J. Biol. Chem.

250

5438-5445

1975

Escherichia coli, Lambdavirus lambda

1141237

brenda

Cassuto, E.; Radding, C.M.

Mechanism for the action of lambda exonuclease in genetic recombination

Nature New Biol.

229

13-16

1971

Escherichia coli, Lambdavirus lambda

5276049

brenda

133985

Radding, C.M.

The role of exonuclease and beta protein of bacteriophage lambda in genetic recombination. I. Effects of red mutants on protein structure

J. Mol. Biol.

491-499

1970

Escherichia coli, Lambdavirus lambda

4992641

brenda

Little, J.W.; Lehman, I.R.; Kaiser, A.D.

An exonuclease induced by bacteriophage lambda. I. Preparation of the crystalline enzyme

J. Biol. Chem.

242

672-678

1967

Escherichia coli, Lambdavirus lambda

6017736

brenda

133987

Little, J.W.

An exonuclease induced by bacteriophage lambda. II. Nature of the enzymatic reaction

J. Biol. Chem.

242

679-686

1967

Escherichia coli, Lambdavirus lambda

6017737

brenda

Radding, C.M.; Szpirer, J.; Thomas, R.

The structural gene for lambda exonuclease

Proc. Natl. Acad. Sci. USA

277-283

1967

Escherichia coli, Lambdavirus lambda, Lambdavirus lambda phage 80

16591465

brenda

Carter, D.M.; Radding, C.M.

The role of exonuclease and beta protein of phage lambda in genetic recombination. II. Substrate specificity and the mode of action of lambda exonuclease

J. Biol. Chem.

246

2502-2512

1971

Escherichia coli, Lambdavirus lambda

4928646

brenda

Dolberg, M.; Baur, C.P.; Knippers, R.

Purification and characterization of a novel 5' exodeoxyribonuclease from the yeast Saccharomyces cerevisiae

Eur. J. Biochem.

198

783-787

1991

Saccharomyces cerevisiae

2050153

brenda

Rudd, E.A.

Reversible inhibition of lambda exonuclease with high pressure

Biochem. Biophys. Res. Commun.

230

140-142

1997

Escherichia coli, Lambdavirus lambda

9020031

brenda

133993

Kovall, R.A.; Matthews, B.W.

Structural, functional, and evolutionary relationships between lambda-exonuclease and the type II restriction endonucleases

Proc. Natl. Acad. Sci. USA

7893-7897

1998

Escherichia coli, Lambdavirus lambda

9653111

brenda

682074

Kim, S.; Blainey, P.C.; Schroeder, C.M.; Xie, X.S.

Multiplexed single-molecule assay for enzymatic activity on flow-stretched DNA

Nat. Methods

397-399

2007

Lambdavirus lambda (P03697)

17435763

brenda

695543

Balagurumoorthy, P.; Adelstein, S.J.; Kassis, A.I.

Method to eliminate linear DNA from mixture containing nicked circular, supercoiled, and linear plasmid DNA

Anal. Biochem.

381

172-174

2008

Escherichia coli

18638445

brenda

695561

Song, C.; Zhao, M.

Real-time monitoring of the activity and kinetics of T4 polynucleotide kinase by a singly labeled DNA-hairpin smart probe coupled with lambda exonuclease cleavage

Anal. Chem.

1383-1388

2009

Escherichia coli

19170527

brenda

708359

Conroy, R.S.; Koretsky, A.P.; Moreland, J.

Lambda exonuclease digestion of CGG trinucleotide repeats

Eur. Biophys. J.

337-343

2010

synthetic construct

19562332

brenda

710025

Avci-Adali, M.; Paul, A.; Wilhelm, N.; Ziemer, G.; Wendel, H.P.

Upgrading SELEX technology by using lambda exonuclease digestion for single-stranded DNA generation

Molecules

1-11

2010

synthetic construct

20110867

brenda

713754

Kang, S.H.; Lee, S.; Yeung, E.S.

Digestion of individual DNA molecules by lambda-exonuclease at liquid-solid interface

Analyst

135

1759-1764

2010

Lambdavirus lambda

20436973

brenda

Zhang, J.; McCabe, K.A.; Bell, C.E.

Crystal structures of lambda exonuclease in complex with DNA suggest an electrostatic ratchet mechanism for processivity

Proc. Natl. Acad. Sci. USA

108

11872-11877

2011

Lambdavirus lambda

21730170

brenda

728851

Yuan, Z.; Zhou, Y.; Gao, S.; Cheng, Y.; Li, Z.

Homogeneous and sensitive detection of microRNA with ligase chain reaction and lambda exonuclease-assisted cationic conjugated polymer biosensing

ACS Appl. Mater. Interfaces

6181-6185

2014

Lambdavirus lambda

24773186

brenda

728953

Oliver-Calixte, N.J.; Uba, F.I.; Battle, K.N.; Weerakoon-Ratnayake, K.M.; Soper, S.A.

Immobilization of lambda exonuclease onto polymer micropillar arrays for the solid-phase digestion of dsDNAs

Anal. Chem.

4447-4454

2014

Lambdavirus lambda

24628008

brenda

750114

Cui, L.; Li, Y.; Lu, M.; Tang, B.; Zhang, C.Y.

An ultrasensitive electrochemical biosensor for polynucleotide kinase assay based on gold nanoparticle-mediated lambda exonuclease cleavage-induced signal amplification

Biosens. Bioelectron.

1-7

2018

Lambdavirus lambda (P03697)

28732343

brenda

Wu, T.; Xiao, X.; Gu, F.; Zhao, M.

Sensitive discrimination of stable mismatched base pairs by an abasic site modified fluorescent probe and lambda exonuclease

Chem. Commun. (Camb.)

17402-17405

2015

Lambdavirus lambda (P03697)

26465212

brenda

Foulk, M.; Urban, J.; Casella, C.; Gerbi, S.

Characterizing and controlling intrinsic biases of lambda exonuclease in nascent strand sequencing reveals phasing between nucleosomes and G-quadruplex motifs around a subset of human replication origins

Genome Res.

725-735

2015

Lambdavirus lambda (P03697)

brenda

Xu, L.; Zhao, W.; Pu, J.; Wang, S.; Liu, S.; Li, H.; Yu, R.

A Pax-5a gene analysis approach enabled by selective digestion with lambda exonuclease

Anal. Methods

2415-2422

2022

Lambdavirus lambda

35670541

brenda

770512

Zou, R.; Gavrilov, M.; Liu, Y.; Rasoloson, D.; Conte, M.; Hardick, J.; Shen, L.; Chen, S.; Pekosz, A.; Seydoux, G.; Manabe, Y.; Ha, T.

Improving the specificity of nucleic acid detection with endonuclease-actuated degradation

Commun. Biol.

290

2022

Lambdavirus lambda

35361863

brenda

Brewster, J.L.; Tolun, G.

Half a century of bacteriophage lambda recombinase In vitro studies of lambda exonuclease and Red-beta annealase

IUBMB Life

1622-1633

2020

Lambdavirus lambda

32621393

brenda

774045

Le Dortz, L.L.; Rouxel, C.; Leroy, Q.; Brosseau, N.; Boulouis, H.J.; Haddad, N.; Lagree, A.C.; Deshuillers, P.L.

Optimized lambda exonuclease digestion or purification using streptavidin-coated beads which one is best for successful DNA aptamer selection?

Methods Protoc.

2022

Lambdavirus lambda

36412811

brenda

Guo, Z.; Zhang, X.; Zhou, S.

Sequential logic circuit built on lambda exonuclease for cross inhibition

New J. Chem.

8925-8932

2023

Lambdavirus lambda

brenda

775746

Lian, K.; Chen, G.; Wang, X.; Zhang, W.; Hu, X.; Wang, H.; Li, Y.; Xi, D.; Wang, Y.

Fluorescent detection of brown spot of tobacco caused by Alternaria alternata based on lambda exonuclease-induced DNAzyme amplification

RSC Adv.

1587-1593

2023

Lambdavirus lambda

36688064

brenda