Effects of mercuric ion on the conformation and activity of Penaeus Vannamei beta-N-acetyl-d-glucosaminidase.
beta-N-acetyl-d-glucosaminidase (NAGase, EC.3.2.1.52), a composition of the chitinases, catalyzes the cleavage of N-acetylglucosamine polymers into N-acetylglucosamine. In this paper, the effects of mercuric ion on the activity of NAGase from Penaeus vannamei for the hydrolysis of pNP-NAG have been studied. The results show that HgCl2 can lead to irreversible inactivation to this enzyme. The inactivation process follows a first-order reaction and the inactivation rate constants have been determined. The relationship between the inactivation rate constants and HgCl2 concentration has been studied and the result shows that only one molecule of HgCl2 binds to the enzyme molecule to lead the enzyme lose its activity. Moreover, the conformational changes of the enzyme inactivated by HgCl2 were studied by following changes in the intrinsic fluorescence emission and ultraviolet absorption spectra.
Lin
Jian-Cheng
JC
The Key Laboratory of Ministry of Education for Cell Biology and Tumor Cell Engineering, Department of Biochemistry and Biotechnology, School of Life Sciences, Xiamen University, Xiamen 361005, China.
Xie
Xiao-Lan
XL
Gong
Min
M
Wang
Qin
Q
Chen
Qing-Xi
QX
D000118:Acetylglucosaminidase / Q000737:chemistry*; D002942:Circular Dichroism; D004305:Dose-Response Relationship, Drug; D007477:Ions / Q000737:chemistry*; D007700:Kinetics; D008627:Mercuric Chloride / Q000494:pharmacology; D008628:Mercury / Q000737:chemistry* / Q000378:metabolism; D008968:Molecular Conformation; D033561:Penaeidae / Q000201:enzymology*; D011487:Protein Conformation; D011489:Protein Denaturation; D017510:Protein Folding; D013050:Spectrometry, Fluorescence; D013053:Spectrophotometry; D014466:Ultraviolet Rays
D007477:Ions; D008627:Mercuric Chloride; D000118:Acetylglucosaminidase; D008628:Mercury