Crystal structures of human prostatic acid phosphatase in complex with a phosphate ion and alpha-benzylaminobenzylphosphonic acid update the mechanistic picture and offer new insights into inhibitor design

Human prostatic acid phosphatase crystal structures in complex with a phosphate ion and alpha-benzylaminobenzylphosphonic acid reveal the identity of the final intemediate in the catalytic mechanism and determinants of binding ligands within the active site, respectively. The latter explains the enzyme's preference to aromatic substrates.