Determination of the Regulatory Disulfide Bonds of NADP-Dependent Malate Dehydrogenase from Pisum sativum by Site-Directed Mutagenesis

1997 ◽  
Vol 378 (9) ◽  
pp. 983-988 ◽  
Author(s):  
Robin Rießland ◽  
Rainer Jaenicke
2011 ◽  
Vol 77 (17) ◽  
pp. 6274-6276 ◽  
Author(s):  
Maxim Kostylev ◽  
David B. Wilson

ABSTRACTThe catalytic base in family 48 glycosyl hydrolases has not been previously established experimentally. Based on structural and modeling data published to date, we used site-directed mutagenesis and azide rescue activity assays to show definitively that the catalytic base inThermobifida fuscaCel48A is aspartic acid 225. Of the tested mutants, only Cel48A with the D225E mutation retained partial activity on soluble and insoluble substrates. In azide rescue experiments, only the D225G mutation, in the smallest residue tested, showed an increase in activity with added azide.


1992 ◽  
pp. 701-704
Author(s):  
Emmanuelle Issakidis ◽  
Jean-Pierre Jacquot ◽  
Myroslawa Miginiac-Maslow ◽  
Paulette Decottignies ◽  
Claude Crétin ◽  
...  

FEBS Letters ◽  
1993 ◽  
Vol 321 (1) ◽  
pp. 55-58 ◽  
Author(s):  
Emmanuelle Issakidis ◽  
Paulette Decottignies ◽  
Myroslawa Miginiac-Maslow

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