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Frontiers of Chemical Science and Engineering

ISSN 2095-0179

ISSN 2095-0187(Online)

CN 11-5981/TQ

邮发代号 80-969

2019 Impact Factor: 3.552

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Frontiers of Chemical Science and Engineering  2016, Vol. 10 Issue (2): 238-244   https://doi.org/10.1007/s11705-016-1566-2
  本期目录
Functional characterization of a thermostable methionine adenosyltransferase from Thermus thermophilus HB27
Yanhui Liu,Biqiang Chen,Zheng Wang,Luo Liu(),Tianwei Tan()
Beijing Key Laboratory of Bioprocess, Beijing University of Chemical Technology, Beijing 100029, China
 全文: PDF(398 KB)   HTML
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Abstract：

MATTt (a thermostable methionine adenosyltransferase from Thermus thermophilus HB27) was overexpressed in Escherchia coli and purified using Ni-NTA affinity column. The enzymatic activity of MATTt was investigated in a temperature range from 30 °C to 90 °C, showing that MATTt exhibited a high enzymatic activity and good thermostability at 80 °C. Circular dichroism spectra reveals that MATTt contains high portion of β-sheet structures contributing to the thermostability of MATTt. The kinetic parameter, Km is 4.19 mmol/L and 1.2 mmol/L for ATP and methionine, respectively. MATTt exhibits the highest enzymatic activity at pH 8. Cobalt (Co2+) and zinc ion (Zn2+) enhances remarkably the activity of MATTt compared to the magnesium ion (Mg2+). All these results indicated that the thermostable MATTt has great potential for industry applications.
Key words： ion-preference    methionine adenosyltransferase    secondary structure    thermostability    Thermus thermophilus
收稿日期: 2015-10-27      出版日期: 2016-05-19
Corresponding Author(s): Luo Liu,Tianwei Tan   
 引用本文:   
. [J]. Frontiers of Chemical Science and Engineering, 2016, 10(2): 238-244.
Yanhui Liu,Biqiang Chen,Zheng Wang,Luo Liu,Tianwei Tan. Functional characterization of a thermostable methionine adenosyltransferase from Thermus thermophilus HB27. Front. Chem. Sci. Eng., 2016, 10(2): 238-244.
 链接本文:  
https://academic.hep.com.cn/fcse/CN/10.1007/s11705-016-1566-2
https://academic.hep.com.cn/fcse/CN/Y2016/V10/I2/238
Fig.1  
Fig.2  
Fig.3  
Organism Vmax /(µmol·min–1·mg–1) Km (ATP) /(mmol/L) Km (methionine) /(mmol/L) Temperature /°C Ref.
T. thermophilus 0.84 4.19 1.2 70 This study
M. jannaschiia 3.0 0.25 0.14 70 [25]
E. coli 1.2 0.11 0.08 25 [26]
H. sapiens 0.2 0.03 0.003 37 [27]
B. subtilis 0.36 0.92 0.26 37 [14]
Tab.1  
Fig.4  
Fig.5  
Program Secondary structure Temperature /°C
25 70 80 90
K2D2 α-helix/% 15.97 12.52 3.44 3.69
β-sheet/% 30.83 35.2 47.08 44.51
SELCON3 α-helix/% 81.1 81.1 46.6 43.9
β-sheet/% 0.8 0.6 12.0 28.7
β-turns/% 7.1 6.7 24.2 21.7
Random coils/% 16.1 15.7 33.4 33.1
Tab.2  
Fig.6  
Fig.7  
Fig.8  
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