Well ordered crystals of a short-chain alcohol dehydrogenase from Drosophila lebanonensis: re-evaluation of the crystallographic data and rotation-function analysis

1995 ◽  
Vol 51 (1) ◽  
pp. 69-72 ◽  
Author(s):  
R. Ladenstein ◽  
G. Tibbelin ◽  
A. Karshikoff ◽  
S. Atrian ◽  
R. Gonzàlez-Duarte
2001 ◽  
Vol 268 (10) ◽  
pp. 3062-3068 ◽  
Author(s):  
John van der Oost ◽  
Wilfried G. B. Voorhorst ◽  
Servé W. M. Kengen ◽  
Ans C. M. Geerling ◽  
Vincent Wittenhorst ◽  
...  

1995 ◽  
Vol 232 (2) ◽  
pp. 473-477 ◽  
Author(s):  
Franco Gabrielli ◽  
Giulia Donadel ◽  
Giuliano Bensi ◽  
Adriana Heguy ◽  
Marialuisa Melli

2002 ◽  
Vol 14 (8) ◽  
pp. 1833-1846 ◽  
Author(s):  
Miguel González-Guzmán ◽  
Nadezda Apostolova ◽  
José M. Bellés ◽  
José M. Barrero ◽  
Pedro Piqueras ◽  
...  

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.


2003 ◽  
Vol 44 (1) ◽  
pp. 85-92 ◽  
Author(s):  
Joonyul Kim ◽  
Hong-Gyu Kang ◽  
Sung-Hoon Jun ◽  
Jinwon Lee ◽  
Jieun Yim ◽  
...  

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