AMP nucleosidase (AMN)

AMP nucleosidase (AMN) is an enzyme found exclusively in prokaryotes, such as Escherichia coli, where it catalyzes the hydrolysis of adenosine monophosphate (AMP) into adenine and ribose 5-phosphate[1][3][4][6]. This reaction plays a key role in the purine nucleoside salvage pathway and in regulating intracellular AMP concentrations. AMN is structurally a homohexamer, with each monomer containing a catalytic domain and a putative regulatory domain. Its activity is allosterically regulated: activated by ATP and inhibited by inorganic phosphate. AMN’s structure reveals similarity to nucleoside phosphorylases, placing it within that enzyme family, but with a unique regulatory domain. The enzyme is not present in higher eukaryotes and has no direct link to human diseases or existing drugs[1][2][4][6].

Other names

adenosine monophosphate nucleosidaseAMN