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Literature summary for 3.1.11.5 extracted from

  • Wang, J.; Chen, R.; Julin, D.A.
    A single nuclease active site of the Escherichia coli RecBCD enzyme catalyzes single-stranded DNA degradation in both directions (2000), J. Biol. Chem., 275, 507-513.
    View publication on PubMed
Search for more literature for 3.1.11.5

Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Protein Variants

Protein Variants Comment Organism
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. Escherichia coli
K1082Q 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. Escherichia coli
Y1081A The mutation in the carboxyl-terminal nuclease domain of the RecB subunit exhibits substantial nuclease activity. Escherichia coli
Y1081F The mutation in the carboxyl-terminal nuclease domain of the RecB subunit exhibits essentially wild-type levels of activity. Escherichia coli
Y1114A The mutation in the carboxyl-terminal nuclease domain of the RecB subunit exhibits substantial nuclease activity. Escherichia coli
Y1114F The mutation in the carboxyl-terminal nuclease domain of the RecB subunit exhibits essentially wild-type levels of activity. Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

Purification (Comment) Organism
wild-type and mutant enzymes of RecB subunit: D1067A and K1082Q Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
Exonucleolytic cleavage (in the presence of ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'-phosphooligonucleotides mechanism, The enzyme is an ATP-dependent DNA exonuclease and a helicase, its exonuclease activity is subject to regulation by an octameric nucleotide sequence called chi. Escherichia coli
a

Subunits

Subunits Comment Organism
heterotrimer RecB, RecC and RecD subunits, The nuclease active site on the RecB 30000 Da domain is the universal nuclease active site of enzyme that is responsible for single-stranded DNA degradation in both directions. Escherichia coli