An active-site carboxyl group in liquefying α-amylase: specific chemical modification

1984 ◽  
Vol 4 (7) ◽  
pp. 613-619 ◽  
Author(s):  
Sunil Kochhar ◽  
R. D. Dua
Keyword(s):  
Chemical Modification ◽  
Active Site ◽  
Amylase Activity ◽  
Enzymic Activity ◽  
Complete Loss ◽  
Inactivation Kinetics ◽  
Carboxyl Group ◽  
Specific Chemical ◽  
Specific Chemical Modification ◽  
Ph Dependent

Bacillus amyloliquefaciens α-amylase activity is pH-dependent and the plot log (Vmax/Km) versus pH implicated a carboxyl group of aspartic acid/glutamic acid at the active site. Chemical modification of α-amylase with EDC confirmed this view. Further, analysis of inactivation kinetics showed that modification of a single carboxyl group led to complete loss of the enzymic activity.

IL-4 Analogues with Site-Specific Chemical Modification at Position 121 Inhibit IL-4 and IL-13 Biological Activities

2013 ◽  
Vol 25 (1) ◽  
pp. 52-62 ◽  
Author(s):  
Viswanadham Duppatla ◽  
Maja Gjorgjevikj ◽  
Werner Schmitz ◽  
Heike M. Hermanns ◽  
Carmen M. Schäfer ◽  
...  
Keyword(s):  
Chemical Modification ◽  
Biological Activities ◽  
Specific Chemical ◽  
Site Specific ◽  
Specific Chemical Modification

scholarly journals Controlling activation of the RNA-dependent protein kinase by siRNAs using site-specific chemical modification

2006 ◽  
Vol 34 (17) ◽  
pp. 4900-4911 ◽  
Author(s):  
Sujiet Puthenveetil ◽  
Landon Whitby ◽  
Jin Ren ◽  
Kevin Kelnar ◽  
Joseph F. Krebs ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Chemical Modification ◽  
Dependent Protein Kinase ◽  
Specific Chemical ◽  
Site Specific ◽  
Specific Chemical Modification ◽  
Dependent Protein
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