Literature DB >> 16511202

Crystallization and preliminary crystallographic analysis of porcine acylaminoacyl peptidase.

Helena Wright1, András L Kiss, Zoltán Szeltner, László Polgár, Vilmos 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.

Entities:  

Mesh：

Substances：

Year:  2005        PMID： 16511202      PMCID： PMC1991319          DOI： 10.1107/S1744309105029222

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN： 1744-3091


  21 in total

1.  Functional proteomics using microchannel plate detectors.

Authors:  Paul Richards; John Lees
Journal:  Proteomics       Date:  2002-03       Impact factor: 3.984

2.  Structural relationship between lipases and peptidases of the prolyl oligopeptidase family.

Authors:  L Polgár
Journal:  FEBS Lett       Date:  1992-10-26       Impact factor: 4.124

3.  Purification and properties of acylamino acid-releasing enzyme from rat liver.

Authors:  S Tsunasawa; K Narita; K Ogata
Journal:  J Biochem       Date:  1975-01-01       Impact factor: 3.387

4.  Crystal structure of human dipeptidyl peptidase IV/CD26 in complex with a substrate analog.

Authors:  Hanne B Rasmussen; Sven Branner; Finn C Wiberg; Nicolai Wagtmann
Journal:  Nat Struct Biol       Date:  2003-01

5.  Identification of acylpeptide hydrolase as a sensitive site for reaction with organophosphorus compounds and a potential target for cognitive enhancing drugs.

Authors:  P G Richards; M K Johnson; D E Ray
Journal:  Mol Pharmacol       Date:  2000-09       Impact factor: 4.436

6.  The structure and function of human dipeptidyl peptidase IV, possessing a unique eight-bladed beta-propeller fold.

Authors:  Hajime Hiramatsu; Kiyoshi Kyono; Yutaka Higashiyama; Chiaki Fukushima; Hideaki Shima; Shigeru Sugiyama; Koji Inaka; Atsushi Yamamoto; Ryo Shimizu
Journal:  Biochem Biophys Res Commun       Date:  2003-03-21       Impact factor: 3.575

7.  Evidence for nonacetylcholinesterase targets of organophosphorus nerve agent: supersensitivity of acetylcholinesterase knockout mouse to VX lethality.

Authors:  E G Duysen; B Li; W Xie; L M Schopfer; R S Anderson; C A Broomfield; O Lockridge
Journal:  J Pharmacol Exp Ther       Date:  2001-11       Impact factor: 4.030

8.  High-resolution structure of human apo dipeptidyl peptidase IV/CD26 and its complex with 1-[([2-[(5-iodopyridin-2-yl)amino]-ethyl]amino)-acetyl]-2-cyano-(S)-pyrrolidine.

Authors:  Christian Oefner; Allan D'Arcy; Aengus Mac Sweeney; Sabine Pierau; Rana Gardiner; Glenn E Dale
Journal:  Acta Crystallogr D Biol Crystallogr       Date:  2003-06-27

9.  The crystal structure of dipeptidyl peptidase IV (CD26) reveals its functional regulation and enzymatic mechanism.

Authors:  Michael Engel; Torsten Hoffmann; Leona Wagner; Michael Wermann; Ulrich Heiser; Reiner Kiefersauer; Robert Huber; Wolfram Bode; Hans-Ulrich Demuth; Hans Brandstetter
Journal:  Proc Natl Acad Sci U S A       Date:  2003-04-10       Impact factor: 11.205

10.  Structural basis of proline-specific exopeptidase activity as observed in human dipeptidyl peptidase-IV.

Authors:  Ralf Thoma; Bernd Löffler; Martine Stihle; Walter Huber; Armin Ruf; Michael Hennig
Journal:  Structure       Date:  2003-08       Impact factor: 5.006
View more
  2 in total

1.  Carboxypeptidase in prolyl oligopeptidase family: Unique enzyme activation and substrate-screening mechanisms.

Authors:  Pooja Yadav; Venuka Durani Goyal; Neeraj Kailash Gaur; Ashwani Kumar; Sadashiv M Gokhale; Sahayog N Jamdar; Ravindra D Makde
Journal:  J Biol Chem       Date:  2018-11-08       Impact factor: 5.157

2.  Cryo-EM structure of acylpeptide hydrolase reveals substrate selection by multimerization and a multi-state serine-protease triad.

Authors:  Anna J Kiss-Szemán; Pál Stráner; Imre Jákli; Naoki Hosogi; Veronika Harmat; Dóra K Menyhárd; András Perczel
Journal:  Chem Sci       Date:  2022-05-18       Impact factor: 9.969
  2 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.