Crystallization and preliminary crystallographic analysis of porcine acylaminoacyl peptidase

Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Helena WrightVilmos Fülöp

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 A 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 A and four molecules in the asymmetric unit.

References

Oct 5, 1993·Journal of Molecular Biology·M FeeseS J Remington
Mar 29, 2002·Proteomics·Paul Richards, John Lees
Dec 17, 2002·Nature Structural Biology·Hanne B RasmussenNicolai Wagtmann
Mar 21, 2003·Biochemical and Biophysical Research Communications·Hajime HiramatsuRyo Shimizu
Apr 12, 2003·Proceedings of the National Academy of Sciences of the United States of America·Michael EngelHans Brandstetter

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Citations

Nov 10, 2018·The Journal of Biological Chemistry·Pooja YadavRavindra D Makde
Sep 26, 2019·Current Protein & Peptide Science·Anna J Kiss-SzemánDóra K Menyhárd

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