Journal
JOURNAL OF BIOSCIENCE AND BIOENGINEERING
Volume 121, Issue 5, Pages 491-496Publisher
SOC BIOSCIENCE BIOENGINEERING JAPAN
DOI: 10.1016/j.jbiosc.2015.09.008
Keywords
L-2-Haloacid dehalogenase; Circular dichroism; Environmental effects; Conformation
Funding
- Chinese Academy of Sciences Hundred Talent Program [A1097]
- National Natural Science Foundation of China [31100092]
Ask authors/readers for more resources
2-Haloacid dehalogenases have been highly studied due to their potential applications in chemical industries and bioremediation. Although biochemical and structural characterizations of the enzyme have been detailed, no information was available regarding environmental effects on the structure function relationship. Here, circular dichroism spectroscopy (CD) was used to investigate the correlation between changes on the conformation and the function of L-2-haloacid dehalogenase (HadL AJ1) from the Pseudomonas putida induced by the environmental factors. Decreased alpha-helix and increased beta-sheet contents were observed in the structure of HadL AJ1 along with activity losses caused by pH, temperature and inhibitors. Regardless of which factor above-mentioned existed, more than 65.0% of HadL AJ1 activity could be remained if its alpha-helix content was over 12.0%. The maintenance of alpha-helical structure in HadL All was indispensable to its catalysis, while beta-sheet increase restricts its activity. This study revealed the variation of enzymatic activity due to environmental conditions resulting in structural changes monitored by CD, which contributed to rational modification and was instructive for predicting changes of the enzymatic activity during application. (C) 2015, The Society for Biotechnology, Japan. All rights reserved.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available