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- W2036695076 abstract "Abstract The role of exposed tyrosine side-chains in enzyme-catalysed reactions has been studied for porcine-pancreatic alpha-amylase, sweet-potato beta-amylase, and Aspergillus niger glucamylase using N -acetylimidazole as the specific protein reagent. The changes in activity binding affinity (Δ k −1 / k +1 ), and kinetic parameters ( K m, k 2 ) due to acetylation of the phenolic hydroxyl groups have been determined. Acetylation of each enzyme occurred by an “apparent” first-order reaction with a rate constant of 0.72–1.4 x 10 −1 min −1 . Acetylation increased the apparent K m (soluble starch as the substrate) for each enzyme (appreciably for alpha-amylase and glucamylase), whereas k 2 remained unchanged. Similarly, for each enzyme, the binding affinity for immobilised cyclohexa-amylose decreased appreciably, whereas the catalytic activity was reduced only to a small degree (and remained unchanged for beta-amylase). It is concluded that the tyrosine groups located in the active centre of each enzyme have a substrate-binding function." @default.
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- W2036695076 date "1980-05-01" @default.
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- W2036695076 title "A study of the role of tyrosine groups at the active centre of amylolytic enzymes" @default.
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- W2036695076 doi "https://doi.org/10.1016/s0008-6215(00)85682-7" @default.
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