scholarly journals From Alcohol Dehydrogenase to a “One-way” Carbonyl Reductase by Active-site Redesign

2010 ◽  
Vol 285 (40) ◽  
pp. 30644-30653 ◽  
Author(s):  
Mario Klimacek ◽  
Bernd Nidetzky
1991 ◽  
Vol 88 (18) ◽  
pp. 8149-8153 ◽  
Author(s):  
T. D. Hurley ◽  
W. F. Bosron ◽  
J. A. Hamilton ◽  
L. M. Amzel

2003 ◽  
Vol 22 (5) ◽  
pp. 457-461 ◽  
Author(s):  
Sander R. Piersma ◽  
Annika Norin ◽  
Simon de Vries ◽  
Hans Jörnvall ◽  
Johannis A. Duine

2000 ◽  
Vol 26 (3) ◽  
pp. 157-163
Author(s):  
A. S. Kutsenko ◽  
D. A. Kuznetsov ◽  
V. V. Poroikov ◽  
V. G. Tumanyan

1995 ◽  
Vol 308 (2) ◽  
pp. 375-379 ◽  
Author(s):  
G E Cozier ◽  
I G Giles ◽  
C Anthony

The 1.94 A structure of methanol dehydrogenase has been used to provide a model structure for part of a membrane quinohaemoprotein alcohol dehydrogenase. The basic superbarrel structure and the active-site region are retained, indicating essentially similar mechanisms of action, but there are considerable differences in the external loops, particularly those involved in formation of the shallow funnel leading to the active site.


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