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Some aspects of the mechanism of complexation of red kidney bean a-amylase inhibitor and a-amylase

Some aspects of the mechanism of complexation of red kidney bean a-amylase inhibitor and a-amylase. Wilcox, Edward R.; Whitaker, John R. (Dep. Food Sci. Technol., Univ. California, Davis, CA 95616, USA). Biochemistry, 23(8), 1783-91 (English) 1984. CODEN: BICHAW. ISSN: 0006-2960. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) Bovine pancreatic a-amylase (I) binds 1 mol of acarbose (II), a carbohydrate I inhibitor, per mol at the active site and also binds II nonspecifically. The red kidney bean I inhibitor-bovine pancreatic I complex retained nonspecific binding for II only. The binding of p-nitrophenyl a-D-maltoside (III) to the final complex of red kidney bean I inhibitor and bovine pancreatic I had a bKs (Ks') value that was 3.4-fold greater than the Ks (16 mM) of I for III alone. The initial complex of I and inhibitor apparently hydrolyzed this substrate as rapidly as did I alone. The complex retained affinity for substrates and competitive inhibitors, which, when present in high concns., caused dissocn. of the complex. Maltose (0.5M), a competitive inhibitor of I, caused dissocn. of the red kidney bean I inhibitor-I complex. The interaction between red kidney bean I inhibitor and porcine pancreatic I proceeded through 2 steps. The 1st step has a Keq of 3.1 ′ 10-5M. The 2nd step (unimol.; 1st-order) had a forward rate const. of 3.05 min-1 at pH 6.In this experiment, several chemicals are used like 9000-90-2 and 17400-77-0 9 and 30°. I inhibitor combined with I noncompetitively in the presence of III. Thus, I may be inactivated by the I inhibitor through a conformational change. A kinetic model, in the presence and absence of substrate, is described for noncompetitive, slow, tight-binding inhibitors that proceed through 2 steps. .