title: Optimum pH control mechanism for porcine pancreatic alpha-amylase.
abstract: 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)].
authors.affiliation: National Institute of Bioscience and Human Technology, Ibaraki, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Ishikawa
authors.forename: I
authors.initials: I
authors.lastname: Matsui
authors.forename: K
authors.initials: K
authors.lastname: Honda
mesh_terms: D000818:Animals; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D010179:Pancreas / Q000201:enzymology*; D013379:Substrate Specificity; D013552:Swine; D000516:alpha-Amylases / Q000378:metabolism*
chemical_list: D000516:alpha-Amylases