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Article

Structure of human cytosolic X-prolyl aminopeptidase: a double Mn(II)-dependent dimeric enzyme with a novel three-domain subunit.

The Journal of biological chemistry - 15 Aug 2008

Li Xin, Lou Zhiyong, Li Xuemei, Zhou Weihong, Ma Ming, Cao Youjia, Geng Yunqi, Bartlam Mark, Zhang Xuejun C, Rao Zihe

Abstract excerpt

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...

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Identifiers

PMID: 18515364
DOI: 10.1074/jbc.M710274200

Genes

XPNPEP1

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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