Nuclease from Serratia marcescens (Sm nuclease) is a well-characterized extracellular endonuclease with unique properties originally isolated from the bacterium Serratia marcescens. It catalyzes the hydrolysis of both single-stranded and double-stranded DNA and RNA molecules, generating 5’-phosphate and 3’-hydroxyl termini. Metal ions, typically magnesium or manganese, coordinate within the active site and play a crucial role in catalysis by stabilizing the transition state during phosphodiester bond cleavage. Unlike some nucleases that require specific sequence motifs for substrate recognition, Sm nuclease exhibits non-specific endonuclease activity cleaving nucleic acids at random sites along the phosphate backbone. Its robust enzymatic activity and versatility, makes it particularly useful for various biotechnological applications, such as DNA and RNA purification, removal of nucleic acid contaminants from protein samples, generation of cohesive ends for cloning, and site-directed mutagenesis. Furthermore, Sm nuclease is beneficial in various nucleic acid manipulation techniques, including restriction enzyme digest, DNA footprinting, and next-generation sequencing library preparation. This nuclease is also known as Benzonase® (Benzonase is a trademark of Merck KGaA, Darmstadt, Germany).
