Czernecki, Dariusz; Legrand, Pierre; Tekpinar, Mustafa; Rosario, Sandrine; Kaminski, Pierre-Alexandre; Delarue, Marc published the artcile< How cyanophage S-2L rejects adenine and incorporates 2-aminoadenine to saturate hydrogen bonding in its DNA>, Recommanded Product: 7H-Purin-2-amine, the main research area is .
Abstract: Bacteriophages have long been known to use modified bases in their DNA to prevent cleavage by the host′s restriction endonucleases. Among them, cyanophage S-2L is unique because its genome has all its adenines (A) systematically replaced by 2-aminoadenines (Z). Here, we identify a member of the PrimPol family as the sole possible polymerase of S-2L and we find it can incorporate both A and Z in front of a T. Its crystal structure at 1.5 Å resolution confirms that there is no structural element in the active site that could lead to the rejection of A in front of T. To resolve this contradiction, we show that a nearby gene is a triphosphohydolase specific of dATP (DatZ), that leaves intact all other dNTPs, including dZTP. This explains the absence of A in S-2L genome. Crystal structures of DatZ with various ligands, including one at sub-angstrom resolution, allow to describe its mechanism as a typical two-metal-ion mechanism and to set the stage for its engineering.
Nature Communications published new progress about 452-06-2. 452-06-2 belongs to class imidazoles-derivatives, and the molecular formula is C5H5N5, Recommanded Product: 7H-Purin-2-amine.
Referemce:
Imidazole – Wikipedia,
Imidazole | C3H4N2 – PubChem