Structure-function relationships in the sodium-potassium ATPase .alpha. subunit: site-directed mutagenesis of glutamine-111 to arginine and asparagine-122 to aspartic acid generates a ouabain-resistant enzyme

Biochemistry ◽  
1988 ◽  
Vol 27 (22) ◽  
pp. 8400-8408 ◽  
Author(s):  
Elmer M. Price ◽  
Jerry B. Lingrel
Keyword(s):  
Structure Function ◽  
Aspartic Acid ◽  
Site Directed Mutagenesis ◽  
Alpha Subunit ◽  
Directed Mutagenesis ◽  
Sodium Potassium ◽  
Potassium Atpase

Site-directed mutagenesis of a predicted cation binding site of sodium-potassium ATPase

Biochemistry ◽  
1993 ◽  
Vol 32 (3) ◽  
pp. 819-826 ◽  
Author(s):  
James W. Van Huysse ◽  
Elizabeth A. Jewell ◽  
Jerry B. Lingrel
Keyword(s):  
Binding Site ◽  
Cation Binding ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Sodium Potassium ◽  
Cation Binding Site ◽  
Potassium Atpase

scholarly journals Determination of the Catalytic Base in Family 48 Glycosyl Hydrolases

2011 ◽  
Vol 77 (17) ◽  
pp. 6274-6276 ◽  
Author(s):  
Maxim Kostylev ◽  
David B. Wilson
Keyword(s):  
Aspartic Acid ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Thermobifida Fusca ◽  
Glycosyl Hydrolases ◽  
Content Type ◽  
Modeling Data ◽  
Partial Activity

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.

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