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Literature summary for 3.1.11.3 extracted from

  • Zhang, J.; McCabe, K.A.; Bell, C.E.
    Crystal structures of lambda exonuclease in complex with DNA suggest an electrostatic ratchet mechanism for processivity (2011), Proc. Natl. Acad. Sci. USA, 108, 11872-11877.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.1.11.3

Protein Variants

Protein Variants Comment Organism
D119A site-directed mutagenesis, inactive mutant Lambdavirus lambda
E85A site-directed mutagenesis, almost inactive mutant Lambdavirus lambda
K131A site-directed mutagenesis, inactive mutant Lambdavirus lambda
K49A site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme Lambdavirus lambda
K76A site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme Lambdavirus lambda
L78A site-directed mutagenesis, the mutant shows a significantly diminished level of activity compared to the wild-type enzyme Lambdavirus lambda
M53A site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme Lambdavirus lambda
R137A site-directed mutagenesis, inactive mutant Lambdavirus lambda
R28A site-directed mutagenesis, mutation of a residue that contact the 5' phosphate of the DNA, inactive mutant Lambdavirus lambda
R45A site-directed mutagenesis, inactive mutant Lambdavirus lambda
W24A site-directed mutagenesis, mutation of a residue that contact the 5' phosphate of the DNA, almost inactive mutant Lambdavirus lambda

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ dependent on Lambdavirus lambda

Organism

Organism UniProt Comment Textmining
Lambdavirus lambda
-
-
-

Reaction

Reaction Comment Organism Reaction ID
exonucleolytic cleavage in the 5'- to 3'-direction to yield nucleoside 5'-phosphates lambda exonuclease uses a classic two-metal mechanism Lambdavirus lambda
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information 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 Lambdavirus lambda ?
-
 ?

Synonyms

Synonyms Comment Organism
lambda exonuclease
-
 Lambdavirus lambda

General Information

General Information Comment Organism
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 Lambdavirus lambda