PMID: 2318199Feb 22, 1990Paper

Nuclear magnetic relaxation studies of the role of the metal ion in Mn2(+)-substituted aminoacylase I

European Journal of Biochemistry
D HeeseK H Röhm

Abstract

Substitution of the essential Zn2+ ions of porcine kidney aminoacylase I (EC 3.5.1.14) by Mn2+ did not markedly affect the kinetic properties of the enzyme. Using Mn2+ as a paramagnetic probe, we were able to study the conformations of bound ligands by measuring the enhancement of ligand proton relaxation in 1H NMR. In addition, the effects of inhibitors on the paramagnetic enhancement of water proton relaxation rates were examined. The results of both approaches, in agreement with kinetic evidence, suggest that the metal center of aminoacylase I is too distant from the ligand binding site to allow direct participation of the metal in substrate binding or catalysis. We, therefore, propose that the metal ion of aminoacylase I plays a purely structural role.

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Citations

Nov 1, 1995·Journal of Protein Chemistry·Y X ZhangH M Zhou
Mar 16, 2001·Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology·A Biagini, A Puigserver
Sep 30, 2000·European Journal of Biochemistry·T GiardinaA Puigserver
May 26, 2010·Proceedings of the National Academy of Sciences of the United States of America·Christopher L DupontGustavo Caetano-Anollés
Jan 12, 2001·Biological Chemistry·H LindnerK H Röhm
Apr 14, 2009·Biochimica Et Biophysica Acta·Kirill TsirulnikovAlexander Pushkin
Jul 16, 2004·Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology·Josette PerrierAntoine Puigserver
Aug 23, 2003·The Journal of Biological Chemistry·Holger A LindnerRobert Ménard
Jan 17, 2020·Critical Reviews in Toxicology·Patrick E Hanna, M W Anders
Jul 11, 2006·International Journal of Biological Macromolecules·Sung-Hye KimYong-Bin Yan

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