scholarly journals Determination of pKavalues of the histidine side chains of phosphatidylinositol-specific phospholipase C fromBacillus cereusby NMR spectroscopy and site-directed mutagenesis

1997 ◽  
Vol 6 (9) ◽  
pp. 1937-1944 ◽  
Author(s):  
Tun Liu ◽  
Margret Ryan ◽  
Frederick W. Dahlquist ◽  
O. Hayes Griffith
Keyword(s):  
Nmr Spectroscopy ◽  
Phospholipase C ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Side Chains

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.

Probing the Roles of Active Site Residues in Phosphatidylinositol-Specific Phospholipase C fromBacillus cereusby Site-Directed Mutagenesis†

Biochemistry ◽  
1997 ◽  
Vol 36 (42) ◽  
pp. 12802-12813 ◽  
Author(s):  
Claudia S. Gässler ◽  
Margret Ryan ◽  
Tun Liu ◽  
O. Hayes Griffith ◽  
Dirk W. Heinz
Keyword(s):  
Phospholipase C ◽  
Active Site ◽  
Site Directed Mutagenesis ◽  
Directed Mutagenesis ◽  
Active Site Residues
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