3.1.11.5: exodeoxyribonuclease V
This is an abbreviated version!
For detailed information about exodeoxyribonuclease V, go to the full flat file.
Word Map on EC 3.1.11.5
Reaction
Exonucleolytic cleavage (in the presence of ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'-phosphooligonucleotides =
Synonyms
AddAB enzyme, E. coli ATP-dependent DNase, E. coli exonuclease V, Escherichia coli exonuclease V, Escherichia coli RecBCD, Exodeoxyribonuclease V 125 kDa polypeptide, Exodeoxyribonuclease V 135 KDA polypeptide, Exodeoxyribonuclease V 67 kDa polypeptide, exonuclease V, ExoV, gene recBC DNase, gene RecBC endoenzyme, nuclease, exodeoxyribo V, PAB2263, RecB, RecB helicase-nuclease, REcB30 protein, recBC deoxyribonuclease, recBC DNase, recBC nuclease, RecBCD, RecBCD DNase, recBCD enzyme, RecBCD exonuclease, RecBCD-type helicase-nuclease, RecD, UPF0286 protein PYRAB01260
ECTree
3.1.11.5 exodeoxyribonuclease VAdvanced search results
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results (Engineering
Engineering on EC 3.1.11.5 - exodeoxyribonuclease V
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D1067A
D1080A
K1082A
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chi is not a hot-spot for recombination in the mutant, the mutant is sligthtly defective for recombinational repair
K1082Q
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The mutation in the carboxyl-terminal nuclease domain of the RecB subunit abolishes nuclease activity on both single- and double-stranded DNA but the mutant enzyme is active as helicase. The mutant is unable to produce chi-specific fragments from either strand of a chi-containing double-stranded DNA substrate.
Y1081A
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The mutation in the carboxyl-terminal nuclease domain of the RecB subunit exhibits substantial nuclease activity.
Y1081F
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The mutation in the carboxyl-terminal nuclease domain of the RecB subunit exhibits essentially wild-type levels of activity.
Y1114A
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The mutation in the carboxyl-terminal nuclease domain of the RecB subunit exhibits substantial nuclease activity.
Y1114F
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The mutation in the carboxyl-terminal nuclease domain of the RecB subunit exhibits essentially wild-type levels of activity.
D1118A
-
site-directed mutagenesis, inactivation in the nuclease center of RecB
K229Q
-
site-directed mutagenesis, inactivation of the ATPase active site of RecD
K29Q
-
site-directed mutagenesis, inactivation of the ATPase active site of RecB
D1118A
-
site-directed mutagenesis, inactivation in the nuclease center of RecB
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K229Q
-
site-directed mutagenesis, inactivation of the ATPase active site of RecD
-
K29Q
-
site-directed mutagenesis, inactivation of the ATPase active site of RecB
-
additional information
D1067A
-
chi is not a hot-spot for recombination in the mutant, the mutant is sligthtly defective for recombinational repair
D1067A
-
The mutation in the carboxyl-terminal nuclease domain of the RecB subunit abolishes nuclease activity on both single- and double-stranded DNA but the mutant enzyme is active as helicase. The mutant is unable to produce chi-specific fragments from either strand of a chi-containing double-stranded DNA substrate.
D1080A
-
chi is not a hot-spot for recombination in the mutant, the mutant is sligthtly defective for recombinational repair
D1080A
-
Comparison: recB(D1080A)CD is recombinant-deficient, and sensitive to DNA damaging agents, and the purified enzyme failed to load RecA during DNA winding. recB(D1080A)C is recombinant-proficient and resistant to DNA damaging agents, and the mutant is active RecA loading assay.
additional information
-
in mutants carrying either recB2109 or recD1903, which do not exhibit significant nuclease activities, the prophage progressively loses its capacity for both site-specific and general recombination
additional information
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RecB mutants that cannot bind or hydrolyze ATP are completely defective for DNA recombination
additional information
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recBC1010D, recBC1041D and recBCD1013 mutants have less than 0.2% of the exonuclease activity of wild-type enzyme. recBC1010D and recBC1041D produce RecD but fail to assemble it into holoenzyme
additional information
the mutant RecB2109CD degrades the double-stranded DNA primarily in the 5 to 3 direction, producing processed double-stranded DNA with a 3-terminal overhang, the mutant is unable to coordinate the loading of RecA protein onto the single-stranded DNA produced, this inability can be responsible for recB2109 recombination defect observed in vivo
additional information
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the recombination deficiency of the RecBC1004D-chi interaction can be overcome by the enhanced ability of RecA730 to assemble on single-stranded DNA in vitro and in vivo
additional information
deletion of amino acids 881-899 (DELTA19) of RecB, the entire tether. The resulting mutant DELTA19 is recombination-deficient and has no detectable Chi activity. The mutant retained nuclease activity, demonstrating that it is not a null mutant. Additional construction of RecB mutants lacking one or another part of the tether. Inserting two foreign tethers, to make the tether 57 amino acids long, both reduce Chi activity and recombination proficiency to about the same level as that of RecBCD with the 38-amino-acid tethers. None of the mutants reported increases Chi hotspot activity. RecBCD enzymatic activities coincide with the genetic activities of the tether mutants
additional information
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deletion of amino acids 881-899 (DELTA19) of RecB, the entire tether. The resulting mutant DELTA19 is recombination-deficient and has no detectable Chi activity. The mutant retained nuclease activity, demonstrating that it is not a null mutant. Additional construction of RecB mutants lacking one or another part of the tether. Inserting two foreign tethers, to make the tether 57 amino acids long, both reduce Chi activity and recombination proficiency to about the same level as that of RecBCD with the 38-amino-acid tethers. None of the mutants reported increases Chi hotspot activity. RecBCD enzymatic activities coincide with the genetic activities of the tether mutants
additional information
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disruption of genes in the recCBD operon and creation of DELTArecC, DELTArecB, DELTArecD, and DELTArecCBD strains of Pseudomonas syringae Lz4W
additional information
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disruption of genes in the recCBD operon and creation of DELTArecC, DELTArecB, DELTArecD, and DELTArecCBD strains of Pseudomonas syringae Lz4W
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