» Articles » PMID: 1361094

Proline-specific Aminopeptidases: Potential Role in Bradykinin Degradation

Overview
Specialty Pharmacology
Date 1992 Jan 1
PMID 1361094
Citations 3
Authors
Affiliations
Soon will be listed here.
Abstract

The N-terminus of bradykinin is shown to be sequentially degraded by the human proline-specific aminopeptidases aminopeptidase P (EC 3.4.11.9) and dipeptidyl peptidase IV (EC 3.4.14.5). Additional evidence is provided for the hypothesis that these proline-specific aminopeptidases play an essential role in the degradation of peptides containing an N-terminal Xaa-Pro sequence.

Citing Articles

Proteome profiling of clear cell renal cell carcinoma in von Hippel-Lindau patients highlights upregulation of Xaa-Pro aminopeptidase-1, an anti-proliferative and anti-migratory exoprotease.

Drendel V, Heckelmann B, Chen C, Weisser J, Espadas G, Schell C Oncotarget. 2017; 8(59):100066-100078.

PMID: 29245961 PMC: 5725003. DOI: 10.18632/oncotarget.21929.


Crystal structure of X-prolyl aminopeptidase from Caenorhabditis elegans: A cytosolic enzyme with a di-nuclear active site.

Iyer S, La-Borde P, Payne K, Parsons M, Turner A, Isaac R FEBS Open Bio. 2015; 5:292-302.

PMID: 25905034 PMC: 4404410. DOI: 10.1016/j.fob.2015.03.013.


Dipeptidyl-peptidase IV secreted by Aspergillus fumigatus, a fungus pathogenic to humans.

Beauvais A, Monod M, Wyniger J, Debeaupuis J, Grouzmann E, Brakch N Infect Immun. 1997; 65(8):3042-7.

PMID: 9234752 PMC: 175429. DOI: 10.1128/iai.65.8.3042-3047.1997.