Abstract
Abstract X‐prolyl aminopeptidases catalyze the removal of a penultimate prolyl residue from the N‐termini of peptides. Mammalian X‐prolyl aminopeptidases are responsible for the degradation of bradykinin, a blood pressure regulator peptide, and have been linked to myocardial infarction. The X‐ray crystal structure of human cytosolic X‐prolyl aminopeptidase (XPNPEP1) reveals a dimer with a unique three‐domain organization in each subunit, rather than the two domains common to all other known structures of X‐prolyl aminopeptidases and prolidases. The C‐terminal catalytic domain of XPNPEP1 coordinates two metal ions and shares a similar fold with other prolyl aminopeptidases. Metal content analysis and activity assays confirm that the enzyme is double Mn(II) dependent for its activity, which contrasts with the previous notion that each XPNPEP1 subunit contains only one Mn(II) ion.
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