Comparison between conformational change and inactivation rates of aminoacylase during denaturation in urea solutions.
The kinetic method of the substrate reaction in the presence of inactivator previously described by Tsou has been applied to the determination of inactivation rates of aminoacylase during denaturation in urea solutions. The protective effect of substrate on the inactivation of aminoacylase by urea has been investigated. Simultaneously, the comparison between conformational change and inactivation rates of enzyme in the urea solutions of different concentrations has been studied. Results obtained show that the inactivation rate constants of the enzyme are larger than the rate constants of conformational changes. The present results show that the active site of metal enzyme-aminoacylase is also located in a limited and flexible region of the molecule that is more sensitive to denaturants than the enzyme as a whole.
Wang
H
H
Department of Biological Science and Biotechnology, Tsinghua University, Beijing, China.
Wang
X
X
Zhang
T
T
Zhou
H
H
D000581:Amidohydrolases / Q000737:chemistry* / Q000378:metabolism; D008968:Molecular Conformation; D011489:Protein Denaturation; D013329:Structure-Activity Relationship; D014508:Urea
D014508:Urea; D000581:Amidohydrolases; C019672:aminoacylase I