Effect of Specific Hydrogen Bond on Activity and Thermostability of Hyperthermophilic Esterase APE1547

Chem. J. Chinese Universities

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Effect of Specific Hydrogen Bond on Activity and Thermostability of Hyperthermophilic Esterase APE1547

BI Yun-Feng¹, XIE Gui-Qiu^1,2, GAO Ren-Jun¹, LU Jing³, CAO Shu-Gui¹*

1. Key Laboratory for Molecular Enzymology and Engineering, Ministry of Education,
2. School of Pharmaceutical Sciences, Jilin University, Changchun 130021, China;
3. College of Bioengineering, Inner Mogolia Agricultural University, Hohhot 010018, China

Received:2006-12-25 Revised:1900-01-01 Online:2007-10-10 Published:2007-10-10
Contact: CAO Shu-Gui

Abstract

Abstract: Thermophilic esterase APE1547 from Aeropyrum pernix K1 contained a β-propeller with seven blades. There are three hydrogen bonding interactions(Thr127-Gly154,Leu182- Arg145-Glu122) between blades 3 and 4 in the β-propeller domain of the APE1547. To examine the role of these hydrogen bonds, we eliminated these three hydrogen bonds between blades 3 and 4, by site-directed mutagenesis. The analysis results of kinetics, thermostability and differential scanning calorimetry(DSC) of the mutants show that K_cat/K_m value of each mutation increased, and stability decreased dramatically than wild-type protein. These results strongly suggest that the three specific hydrogen bonds played an important role on maintaining the stability and activity of the esterase APE1547.

Key words: Esterase APE1547, Hydrogen bond, Mutation, Activity, Stability

CLC Number:

O629
Q814

TrendMD:

BI Yun-Feng¹, XIE Gui-Qiu^1,2, GAO Ren-Jun¹, LU Jing³, CAO Shu-Gui¹*. Effect of Specific Hydrogen Bond on Activity and Thermostability of Hyperthermophilic Esterase APE1547[J]. Chem. J. Chinese Universities, doi: .

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Effect of Specific Hydrogen Bond on Activity and Thermostability of Hyperthermophilic Esterase APE1547

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