Structural basis of substrate specificity of <i>Helix pomatia</i> AMP deaminase and a chimeric ADGF adenosine deaminase.

ABSTRACT: HPAMPD, an enzyme enriched in the foot muscle of the mollusk Helix pomatia, exhibits deaminase activity on adenosine-5'-monophosphate (AMP). HPAMPD is the first member of the adenosine deaminase-related growth factor (ADGF) family to prefer the nucleotide, AMP, over the nucleoside, adenosine. To investigate the substrate selectivity of HPAMPD, we determined its structure in the apo form and in complex with the adenosine analogs pentostatin (2'-deoxycoformycin) and pentostatin-5'-monophosphate. Structurally, HPAMPD adopts a fold similar to human ADA2, an ADGF family member. HPAMPD has acquired the ability to interact with the 5'-monophosphate group of AMP through polar and charged residues located in three key structural elements: (1) the loop immediately following strand β1, (2) the

SUBMITTER: Kaur G 

PROVIDER: S-EPMC11974800 | biostudies-literature | 2025 Mar

REPOSITORIES: biostudies-literature