Optimum pH control mechanism for porcine pancreatic alpha-amylase.
We studied the substrate-dependence of pH activity of porcine pancreatic alpha-amylase by using a series of p-nitrophenyl maltooligosaccharides. The mechanism controlling the optimum pH of mammalian alpha-amylase involved the reception and recognition of a substrate component at some other substrate binding sites, in addition to those at subsite 5 that were reported previously [K. Ishikawa et al., Biochemistry, 32, 6259-6265 (1993)].
Ishikawa
K
K
National Institute of Bioscience and Human Technology, Ibaraki, Japan.
Matsui
I
I
Honda
K
K
D000818:Animals; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D010179:Pancreas / Q000201:enzymology*; D013379:Substrate Specificity; D013552:Swine; D000516:alpha-Amylases / Q000378:metabolism*
D000516:alpha-Amylases