Secretory expression in Bacillus subtilis and biochemical characterization of a highly thermostable polyethylene terephthalate hydrolase from bacterium HR29

2021 ◽  
Vol 143 ◽  
pp. 109715
Author(s):  
Xingxiang Xi ◽  
Kefeng Ni ◽  
Helong Hao ◽  
Yuepeng Shang ◽  
Bo Zhao ◽  
...  
2017 ◽  
Vol 74 (12) ◽  
pp. 2319-2332 ◽  
Author(s):  
Meriem El Ghachi ◽  
Nicole Howe ◽  
Rodolphe Auger ◽  
Alexandre Lambion ◽  
Annick Guiseppi ◽  
...  

2018 ◽  
Vol 204 (1) ◽  
pp. 1-8 ◽  
Author(s):  
N. Zeytuni ◽  
K.A. Flanagan ◽  
L.J. Worrall ◽  
S.C. Massoni ◽  
A.H. Camp ◽  
...  

2010 ◽  
Vol 192 (11) ◽  
pp. 2900-2907 ◽  
Author(s):  
Maarten Groeneveld ◽  
Ruud G. J. Detert Oude Weme ◽  
Ria H. Duurkens ◽  
Dirk Jan Slotboom

ABSTRACT Bacterial secondary transporters of the DctA family mediate ion-coupled uptake of C4-dicarboxylates. Here, we have expressed the DctA homologue from Bacillus subtilis in the Gram-positive bacterium Lactococcus lactis. Transport of dicarboxylates in vitro in isolated membrane vesicles was assayed. We determined the substrate specificity, the type of cotransported ions, the electrogenic nature of transport, and the pH and temperature dependence patterns. DctA was found to catalyze proton-coupled symport of the four C4-dicarboxylates from the Krebs cycle (succinate, fumurate, malate, and oxaloacetate) but not of other mono- and dicarboxylates. Because (i) succinate-proton symport was electrogenic (stimulated by an internal negative membrane potential) and (ii) the divalent anionic form of succinate was recognized by DctA, at least three protons must be cotransported with succinate. The results were interpreted in the light of the crystal structure of the homologous aspartate transporter GltPh from Pyrococcus horikoshii.


2014 ◽  
Vol 109 ◽  
pp. 184-190 ◽  
Author(s):  
Wenbo Hao ◽  
Fangling Ji ◽  
Jingyun Wang ◽  
Yue Zhang ◽  
Tianqi Wang ◽  
...  

2010 ◽  
Vol 7 (6) ◽  
pp. 1563-1572 ◽  
Author(s):  
Tohru Kamei ◽  
Daisuke Yamashiro ◽  
Terumi Horiuchii ◽  
Yutaka Minouchi ◽  
Makoto Ashiuchi

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