摘要
Aminoacylase is a dimeric metal enzyme containing one Zn<sup>2+</sup>-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 Zn<sup>2+</sup>-ion on the secondarystructure of aminoacylase was observed clearly.After the removal of Zn<sup>2+</sup>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 Zn<sup>2+</sup>helps to keep the conformation ofthe active site required for the catalysis of the enzyme.
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.
