[HTML][HTML] Structure of human cytosolic X-prolyl aminopeptidase: a double Mn (II)-dependent dimeric enzyme with a novel three-domain subunit
X Li, Z Lou, X Li, W Zhou, M Ma, Y Cao, Y Geng… - Journal of biological …, 2008 - ASBMB
X-prolyl aminopeptidases catalyze the removal of a penultimate prolyl residue from the N
termini of peptides. Mammalian X-prolyl aminopeptidases are shown to be 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
(XPN-PEP1) was solved at a resolution of 1.6 Å. The structure reveals a dimer with a
unique three-domain organization in each subunit, rather than the two domains common to …
termini of peptides. Mammalian X-prolyl aminopeptidases are shown to be 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
(XPN-PEP1) was solved at a resolution of 1.6 Å. The structure reveals a dimer with a
unique three-domain organization in each subunit, rather than the two domains common to …