An active-site carboxyl group in liquefying alpha-amylase: specific chemical modification.
Bacillus amyloliquefaciens alpha-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 alpha-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.
D001407:Bacillus / Q000201:enzymology; D001665:Binding Sites; D005022:Ethyldimethylaminopropyl Carbodiimide / Q000494:pharmacology; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D000516:alpha-Amylases / Q000037:antagonists & inhibitors / Q000378:metabolism*
D000516:alpha-Amylases; D005022:Ethyldimethylaminopropyl Carbodiimide