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Catalytic activity, phenylimidazole

Both benzimidazole-containing polymer and phenylimidazole-containing polymer show the hydrophobic binding in the catalyses, obviously (35, 37). The polymers are poly(ABI-pr), poly-(ABI-am), poly(ABI-am-ap), poly(API-pr), poly(API-am) and poly(API-am-ap). Imidazole moieties in these polymers have hydrophobic binding properties themselves. Profiles of hydrolyses of p-acetoxybenzoic acid, ABA(7), show the Michaelis-Menten kinetics. Catalytic activities of those polymers are more than 30 times that of low molecular weight analogues. Several sets of data are tabulated in Table 5. [Pg.66]

Fig. 1. Inhibition of porcine pancreatic a-amylase. Substrates, an inhibitor, and their binding orientations in the active site are shown schematically. The arrows denote the catalytic site in each case, (a) The small substrate, G2PNP [17400-77-0] (3) (b) the large substrate, G6OH [13532-61 -1] (4) and (c) the inhibitor, 4-phenylimidazole (5) and the substrate G2PNP (3) in the binding orientation for noncompetitive inhibition. The binding orientation of G2PNP... Fig. 1. Inhibition of porcine pancreatic a-amylase. Substrates, an inhibitor, and their binding orientations in the active site are shown schematically. The arrows denote the catalytic site in each case, (a) The small substrate, G2PNP [17400-77-0] (3) (b) the large substrate, G6OH [13532-61 -1] (4) and (c) the inhibitor, 4-phenylimidazole (5) and the substrate G2PNP (3) in the binding orientation for noncompetitive inhibition. The binding orientation of G2PNP...
See other pages where Catalytic activity, phenylimidazole is mentioned: [Pg.163]    [Pg.206]    [Pg.66]    [Pg.428]    [Pg.210]    [Pg.67]    [Pg.208]   


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Phenylimidazole

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