being a type ii restriction enzyme, "bgl"ii does not require atp (adenosine triphosphate) for its enzymatic function, but only requires association with a divalent metal cation, most likely mg. unlike other restriction enzymes of its class, "bgl"ii has been shown to possess some unique structural characteristics, such as a β-sandwich subdomain, and appears to undergo a unique conformational change upon dimerization, but its overall structure and mechanism of catalysis remain consistent with other type ii restriction enzymes.