BCHM 310 Lecture 31: BCHEM 315 11:2

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Recognition pocket- defines specificity of the substrate. Bchem 315 11/2: need carbonyl to be held in right place for it to be cleaved, uses other regions important for binding. Ser h bonded to his h bonded to asp. Asp very close to his which makes it a v strong h-bond. How does this accelerate/catalyze the rx: proximity + orientation, s is position so that ser o- can attack it, his is positioned + act by asp, h2o is positioned + act by his. Binding e contributes to this positioning to decr deltag. E+ s es ep" + q h2o ep + q e + p + q. Acyl enzyme q=is n term part that leaves. Ep" + q to ep + q has 2. Ep + q to e + p + q is 1. Ser-his-asp where double bond it breaking and forms a bond to ser.

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