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Benzonase equivalent isa genetically engineered endonuclease from Serratia marcescens. The three-dimensional crystal structure of Serratia marcescens (Sm) nuclease has been refined at 1.7 Å resolution to the R-factor of 17.3% and R-free of 22.2%. The final model consists of 3678 non-hydrogen atoms and 443 water molecules. The analysis of the secondary and the tertiary structures of the Sm nuclease suggests a topology which reveals essential inner symmetry in all the three layers forming the monomer.
Exonuclease I cleaves single-stranded DNA in the 3′→ 5′ direction, releasing 5′ -mono/di-nucleotides and leaving double-stranded DNA molecules and the 5'-terminus intact.
Exonuclease III is a 3′→ 5′ exonuclease which acts by digesting one strand of a dsDNA duplex at a time or digesting the RNA strand of an RNA-DNA heteroduplex (1).
Modified Enzyme. catalyzes the hydrolysis of inorganic pyrophosphate to form orthophosphate.
T7 Exonuclease is similar to Lambda Exonuclease in that it catalyzes the stepwise hydrolysis of duplex DNA from the 5' termini liberating 5' mononucleotides. However, unlike Lambda Exonuclease, the enzyme has low processivity and it will remove both 5-hydroxyl and 5-phosphcryl termini.
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