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Curr. Med. Chem. Cent. Nerv. Syst. Agents
- Publisher
- Wiley
- Copyright
- Copyright © 2005 Wiley Subscription Services, Inc., A Wiley Company
- ISSN
- 1744-3091
- eISSN
- 1744-3091
- DOI
- 10.1107/S1744309105029222
- pmid
- 16511202
- Publisher site
- See Article on Publisher Site
Abstract
Acylaminoacyl peptidase (also known as acylamino‐acid‐releasing enzyme or acylpeptide hydrolase; EC 3.4.19.1) is an unusual member of the prolyl oligopeptidase family catalysing the hydrolysis of an N‐acylated peptide to an acylamino acid and a peptide with a free N‐terminus. Acylaminoacyl peptidase purified from porcine liver has been crystallized in mother liquor containing 0.1 M Tris–HCl pH 7.0, 10%(w/v) polyethylene glycol 8000, 50 mM MgCl2 and 1%(w/v) CHAPS using the hanging‐drop vapour‐diffusion technique. A full data set to 3.4 Å resolution was collected at ESRF beamline ID14‐4 and space group C222 was assigned, with unit‐cell parameters a = 84.8, b = 421.1, c = 212.0 Å and four molecules in the asymmetric unit.
Journal
Acta Crystallographica Section F – Wiley
Published: Oct 1, 2005