Secondary Structure of Holo-Enzyme and Apo-Enzyme of Aminoacylase Using CD and FTIR Spectroscopy  

作　　者：张艳 陈培榕 何飚 周海梦 

机构地区：[1]Department of Chemistry,Tsinghua University,Beijing 100084,PRC [2]Department of Biological Science & Biotechnology,Tsinghua University,Beijing 100084,PRC State Key Laboratory of Biomacromolecules,Institute of Biophysics,Academia Sinica,PRC

出　　处：《Science China Chemistry》1994年第12期1471-1478,共8页中国科学（化学英文版）

摘　　要：Aminoacylase is a dimeric metal enzyme containing one Zn^(2+)-ion per subunit of active site. It is essential for the activity of enzyme.Fourier transform-infrared spectroscopy has been used for the study on the secondary structure of holo-enzyme and ago-enzyme of aminoaeylase from pig kidney.Resolution en- hancement of the amide I secondary structure-sensitive overlapped component bands has been achieved by means of the Fourier self-deconvolution and the Fourier derivation.The effect of Zn^(2+)-ion on the secondary structure of aminoacylase was observed clearly.After the removal of Zn^(2+)in aminoacylase,the extent of the ordered structure was decreased markedly.It suggests that the conformation st or near the active site of aminoacylase contains more ordered structures,and the presence of Zn^(2+)helps to keep the conformation of the active site required for the catalysis of the enzyme.Aminoacylase is a dimeric metal enzyme containing one Zn²⁺-ion per subunit of active site.It is essential for the activity of enzyme.Fourier transform-infrared spectroscopy has been used for the studyon the secondary structure of holo-enzyme and ago-enzyme of aminoaeylase from pig kidney.Resolution en-hancement of the amide I secondary structure-sensitive overlapped component bands has been achieved bymeans of the Fourier self-deconvolution and the Fourier derivation.The effect of Zn²⁺-ion on the secondarystructure of aminoacylase was observed clearly.After the removal of Zn²⁺in aminoacylase,the extent of theordered structure was decreased markedly.It suggests that the conformation st or near the active site ofaminoacylase contains more ordered structures,and the presence of Zn²⁺helps to keep the conformation ofthe active site required for the catalysis of the enzyme.

关 键 词：AMINOACYLASE FTIR SPECTRUM SECONDARY structure. 

分 类 号：O629.8[理学—有机化学]