Wright_2005_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_61_942

Reference

Title : Crystallization and preliminary crystallographic analysis of porcine acylaminoacyl peptidase - Wright_2005_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_61_942
Author(s) : Wright H , Kiss AL , Szeltner Z , Polgar L , Fulop V
Ref : Acta Crystallographica Sect F Struct Biol Cryst Commun , 61 :942 , 2005
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.

PubMedSearch : Wright_2005_Acta.Crystallogr.Sect.F.Struct.Biol.Cryst.Commun_61_942
PubMedID: 16511202
Gene_locus related to this paper: aerpe-APE1547

Related information

Inhibitor Gly-Phe-OH    Ac-Phe-OH
Substrate Gly-Phe-OH    Ac-Phe-OH    Abz-Gly-Phe-OH
Gene_locus Gly-Phe-OH    Ac-Phe-OH    Abz-Gly-Phe-OH    aerpe-APE1547
Structure Gly-Phe-OH    Ac-Phe-OH    Abz-Gly-Phe-OH    aerpe-APE1547    2HU8    2HU5    2HU7

Citations formats

Wright H, Kiss AL, Szeltner Z, Polgar L, Fulop V (2005)
Crystallization and preliminary crystallographic analysis of porcine acylaminoacyl peptidase
Acta Crystallographica Sect F Struct Biol Cryst Commun 61 :942

Wright H, Kiss AL, Szeltner Z, Polgar L, Fulop V (2005)
Acta Crystallographica Sect F Struct Biol Cryst Commun 61 :942