scholarly journals Characterization of GDP-mannose pyrophosphorylase from Escherichia coli O157:H7 EDL933 and its broad substrate specificity

2005 ◽  
Vol 37 (1-6) ◽  
pp. 1-8 ◽  
Author(s):  
Yung-Hun Yang ◽  
Young-Bok Kang ◽  
Kwang-Won Lee ◽  
Tek-Hyung Lee ◽  
Sung-Soo Park ◽  
...  
2010 ◽  
Vol 76 (12) ◽  
pp. 4096-4098 ◽  
Author(s):  
Tatiana N. Stekhanova ◽  
Andrey V. Mardanov ◽  
Ekaterina Y. Bezsudnova ◽  
Vadim M. Gumerov ◽  
Nikolai V. Ravin ◽  
...  

ABSTRACT Short-chain alcohol dehydrogenase, encoded by the gene Tsib_0319 from the hyperthermophilic archaeon Thermococcus sibiricus, was expressed in Escherichia coli, purified and characterized as an NADPH-dependent enantioselective oxidoreductase with broad substrate specificity. The enzyme exhibits extremely high thermophilicity, thermostability, and tolerance to organic solvents and salts.


2014 ◽  
Vol 59 (3) ◽  
pp. 1755-1758 ◽  
Author(s):  
Luisa Borgianni ◽  
Filomena De Luca ◽  
Maria Cristina Thaller ◽  
Yunsop Chong ◽  
Gian Maria Rossolini ◽  
...  

ABSTRACTThe POM-1 metallo-β-lactamase is a subclass B3 resident enzyme produced byPseudomonas otitidis, a pathogen causing otic infections. The enzyme was overproduced inEscherichia coliBL21(DE3), purified by chromatography, and subjected to structural and functional analysis. The purified POM-1 is a tetrameric enzyme of broad substrate specificity with higher catalytic activities with penicillins and carbapenems than with cephalosporins.


2018 ◽  
Vol 18 (1) ◽  
Author(s):  
Mahdia Rahman ◽  
Ashikun Nabi ◽  
Md Asadulghani ◽  
Shah M. Faruque ◽  
Mohammad Aminul Islam

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